Question:

What is an example of how structure and function are related in an organism?

Answer:

Proteins (also known as polypeptides) are organic compounds made of amino acids arranged in a linear chain and folded into a globular form. The amino acids in a polymer are joined together by the peptide bonds between the carboxyl.

More Info:

polypeptides Peptide

A peptide bond (amide bond) is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. The resulting C(O)NH bond is called a peptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called a peptide link. Polypeptides and proteins are chains of amino acids held together by peptide bonds, as is the backbone of PNA.

A peptide bond can be broken by hydrolysis (the adding of water). In the presence of water they will break down and release 8–16 kilojoule/mol (2–4 kcal/mol) of free energy. This process is extremely slow (up to 1000 years). In living organisms, the process is facilitated by enzymes. Living organisms also employ enzymes to form peptide bonds; this process requires free energy. The wavelength of absorbance for a peptide bond is 190–230 nm (which makes it particularly susceptible to UV radiation).

Peptide sequence, or amino acid sequence, is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.

Many peptide sequences have been in sequence databases. These databases may use various notations to describe the peptide sequence. The full names of the amino acids are rarely given; instead, 3-letter or 1-letter abbreviations are usually recorded for conciseness.

In organic chemistry, peptide synthesis is the production of peptides, which are organic compounds in which multiple amino acids are linked via amide bonds which are also known as peptide bonds. The biological process of producing long peptides (proteins) is known as protein biosynthesis.

A signal peptide (sometimes referred to as signal sequence, leader sequence or leader peptide) is a short (5-30 amino acids long) peptide present at the N-terminus of the majority of newly synthesized proteins that are destined towards the secretory pathway. These proteins include those that reside either inside certain organelles (the endoplasmic reticulum, golgi or endosomes), secreted from the cell, or inserted into most cellular membranes. Although most type I membrane-bound proteins have signal peptides, the majority of type II and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first transmembrane domain, which biochemically resembles a signal sequence except that it is not cleaved.

Antimicrobial peptides (also called host defense peptides) are part of the innate immune response and are found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antibiotics which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria (including strains that are resistant to conventional antibiotics), mycobacteria (including Mycobacterium tuberculosis), enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears as though antimicrobial peptides may also have the ability to enhance immunity by functioning as immunomodulators.

Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. Antimicrobial peptides are generally between 12 and 50 amino acids. These peptides include two or more positively charged residues provided by arginine, lysine or, in acidic environments, histidine, and a large proportion (generally >50%) of hydrophobic residues. The secondary structures of these molecules follow 4 themes, including i) α-helical, ii) β-stranded due to the presence of 2 or more disulfide bonds, iii) β-hairpin or loop due to the presence of a single disulfide bond and/or cyclization of the peptide chain, and iv) extended. Many of these peptides are unstructured in free solution, and fold into their final configuration upon partitioning into biological membranes. It contains hydrophilic amino acid residues aligned along one side and hydrophobic amino acid residues aligned along the opposite side of a helical molecule. This amphipathicity of the antimicrobial peptides allows them to partition into the membrane lipid bilayer. The ability to associate with membranes is a definitive feature of antimicrobial peptides although membrane permeabilisation is not necessary. These peptides have a variety of antimicrobial activities ranging from membrane permeabilization to action on a range of cytoplasmic targets.

Nonribosomal peptides (NRP) are a class of peptide secondary metabolites, usually produced by microorganisms like bacteria and fungi. Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms.]citation needed[ While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.

Nonribosomal peptides are synthesized by nonribosomal peptide synthetases, which, unlike the ribosomes, are independent of messenger RNA. Each nonribosomal peptide synthetase can synthesize only one type of peptide. Nonribosomal peptides often have a cyclic and/or branched structures, can contain non-proteinogenic amino acids including D-amino acids, carry modifications like N-methyl and N-formyl groups, or are glycosylated, acylated, halogenated, or hydroxylated. Cyclization of amino acids against the peptide "backbone" is often performed, resulting in oxazolines and thiazolines; these can be further oxidized or reduced. On occasion, dehydration is performed on serines, resulting in dehydroalanine. This is just a sampling of the various manipulations and variations that nonribosomal peptides can perform. Nonribosomal peptides are often dimers or trimers of identical sequences chained together or cyclized, or even branched.

Peptide hormones are proteins that have endocrine functions in living animals.

Like other proteins, peptide hormones are synthesized in cells from amino acids according to mRNA transcripts, which are synthesized from DNA templates inside the cell nucleus. Preprohormones, peptide hormone precursors, are then processed in several stages, typically in the endoplasmic reticulum, including removal of the N-terminal signal sequence and sometimes glycosylation, resulting in prohormones. The prohormones are then packaged into membrane-bound secretory vesicles, which can be secreted from the cell by exocytosis in response to specific stimuli (e.g. --an increase in Ca2+ and cAMP concentration in cytoplasm).

1YK1, 3N56

Brain natriuretic peptide (BNP), now known as B-type natriuretic peptide or Ventricular Natriuretic Peptide (still BNP), is a 32-amino acid polypeptide secreted by the ventricles of the heart in response to excessive stretching of heart muscle cells (cardiomyocytes). The release of BNP is modulated by calcium ions. BNP is named as such because it was originally identified in extracts of porcine brain, although in humans it is produced mainly in the cardiac ventricles.

C-peptide

An organic compound is any member of a large class of gaseous, liquid, or solid chemical compounds whose molecules contain carbon. For historical reasons discussed below, a few types of carbon-containing compounds such as carbides, carbonates, simple oxides of carbon (such as CO and CO2), and cyanides are considered inorganic. The distinction between "organic" and "inorganic" carbon compounds, while "useful in organizing the vast subject of chemistry... is somewhat arbitrary".

Organic chemistry is the science concerned with all aspects of organic compounds. Organic synthesis is the methodology of their preparation.

An organic compound is any member of a large class of gaseous, liquid, or solid chemical compounds whose molecules contain carbon. For historical reasons discussed below, a few types of carbon-containing compounds such as carbides, carbonates, simple oxides of carbon (such as CO and CO2), and cyanides are considered inorganic. The distinction between "organic" and "inorganic" carbon compounds, while "useful in organizing the vast subject of chemistry... is somewhat arbitrary".

Organic chemistry is the science concerned with all aspects of organic compounds. Organic synthesis is the methodology of their preparation.

Organic chemistry is a chemistry subdiscipline involving the scientific study of the structure, properties, and reactions of organic compounds and organic materials, i.e., matter in its various forms that contain carbon atoms. Study of structure includes using spectroscopy and other physical and chemical methods to determine the chemical composition and constitution of organic compounds and materials. Study of properties includes both physical properties and chemical properties, and uses similar methods as well as methods to evaluate chemical reactivity, with the aim to understand the behavior of the organic matter in its pure form (when possible), but also in solutions, mixtures, and fabricated forms. The study of organic reactions includes both their preparation—by synthesis or by other means—as well as their subsequent reactivities, both in the laboratory and via theoretical (in silico) study.

The range of chemicals studied in organic chemistry include hydrocarbons, compounds containing only carbon and hydrogen, as well as compositions based on carbon but containing other elements. Organic chemistry overlaps with many areas including medicinal chemistry, biochemistry, organometallic chemistry, and polymer chemistry, as well as many aspects of materials science.

Organic matter (or organic material, natural organic matter, NOM) is matter composed of organic compounds that has come from the remains of once-living organisms such as plants and animals and their waste products in the environment. Basic structures are created from cellulose, tannin, cutin, and lignin, along with other various proteins, lipids, and sugars. It is very important in the movement of nutrients in the environment and plays a role in water retention on the surface of the planet.]citation needed[

All living organisms are composed of organic compounds. In life they secrete or excrete organic materials such as faeces into soils, shed body parts such as leaves and roots and after the organism dies, its body begins to decompose, broken down by bacterial and fungal action. Larger molecules of organic matter can be formed from the polymerization of different parts of already broken down matter.]citation needed[ Natural organic matter can vary greatly, depending on its origin, transformation mode, age, and existing environment, thus its bio-physico-chemical functions vary with different environments."

A natural product is a chemical compound or substance produced by a living organism – found in nature that usually has a pharmacological or biological activity for use in pharmaceutical drug discovery and drug design. A natural product can be considered as such even if it can be prepared by total synthesis.

These small molecules provide the source or inspiration for the majority of FDA-approved agents and continue to be one of the major sources of inspiration for drug discovery. In particular, these compounds are important in the treatment of life-threatening conditions.

Nickel–Strunz classification is a scheme for categorizing minerals based upon their chemical composition, introduced by German mineralogist Karl Hugo Strunz (24 February 1910 – 19 April 2006) in his Mineralogische Tabellen (1941). The 4th and the 5th edition was edited by Christel Tennyson too (1966). It was followed by A.S. Povarennykh with a modified classification (1966 in Russian, 1972 in English).

As curator of the Mineralogical Museum of Friedrich-Wilhelms-Universität (now known as the Humboldt University of Berlin), Strunz had been tasked with sorting the museum's geological collection according to crystal-chemical properties. His Mineralogical Tables, has been through a number of modifications; the most recent edition, published in 2001, is the ninth (Mineralogical Tables by Hugo Strunz and Ernest H. Nickel (31 August 1925 – 18 July 2009). Nowadays, James A. Ferraiolo is responsible for it at Mindat.org. The IMA/CNMNC supports the Nickel–Strunz database.

Volatile organic compounds (VOCs) are organic chemicals that have a high vapor pressure at ordinary, room-temperature conditions. Their high vapor pressure results from a low boiling point, which causes large numbers of molecules to evaporate or sublimate from the liquid or solid form of the compound and enter the surrounding air. An example is formaldehyde, with a boiling point of –19 °C (–2 °F), slowly exiting paint and getting into the air.

VOCs are numerous, varied, and ubiquitous. They include both human-made and naturally occurring chemical compounds. Most scents or odours are of VOCs. VOCs play an important role in communication between plants. Some VOCs are dangerous to human health or cause harm to the environment. Anthropogenic VOCs are regulated by law, especially indoors, where concentrations are the highest. Harmful VOCs are typically not acutely toxic, but instead have compounding long-term health effects. Because the concentrations are usually low and the symptoms slow to develop, research into VOCs and their effects is difficult.

Organic synthesis is a special branch of chemical synthesis and is concerned with the construction of organic compounds via organic reactions. Organic molecules can often contain a higher level of complexity compared to purely inorganic compounds, so the synthesis of organic compounds has developed into one of the most important branches of organic chemistry. There are two main areas of research fields within the general area of organic synthesis: total synthesis and methodology.

A total synthesis is the complete chemical synthesis of complex organic molecules from simple, commercially available (petrochemical) or natural precursors. In a linear synthesis—often adequate for simple structures—several steps are performed one after another until the molecule is complete. The chemical compounds made in each step are usually deemed synthetic intermediates. For more complex molecules, a different approach may be preferable: convergent synthesis involves the individual preparation of several "pieces" (key intermediates), which are then combined to form the desired product.

Amino acids (/əˈmn/, /əˈmn/, or /ˈæmɪn/) are biologically important organic compounds made from amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. Structurally they can be classified according to the functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.) In the form of proteins, amino acids comprise the second largest component (after water) of human muscles, cells and other tissues. Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.

Amino acids having both the amine and carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance in biochemistry. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases where R is an organic substituent known as a "side-chain"); often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids which combine into peptide chains ("polypeptides") to form the building blocks of a vast array of proteins. These are all L-stereoisomers ("left-handed" isomers) although a few D-amino acids ("right-handed") occur in bacterial envelopes and some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are pyrrolysine (found in methanogenic organisms and other eukaryotes) and selenocysteine (present in many noneukaryotes as well as most eukaryotes). For example, 25 human proteins include selenocysteine (Sec) in their primary structure, and the structurally characterized enzymes (selenoenzymes) employ Sec as the catalytic moiety in their active sites. Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

In the fields of molecular biology and pharmacology, a small molecule is a low molecular weight (<900 Daltons) organic compound that may serve as a regulator of a biological process, with a size on the order of 10−9 m. In pharmacology, the term is usually restricted to a molecule that binds to a specific biopolymer such as protein or nucleic acid and acts as an effector, altering the activity or function of the biopolymer. Small molecules can have a variety of biological functions, serving as cell signaling molecules, as drugs in medicine, as pesticides in farming, and in many other roles. These compounds can be natural (such as secondary metabolites) or artificial (such as antiviral drugs); they may have a beneficial effect against a disease (such as drugs) or may be detrimental (such as teratogens and carcinogens).

Small molecules may also be used as research tools to probe biological function as well as leads in the development of new therapeutic agents. Some can inhibit a specific function of a multifunctional protein or disrupt protein–protein interactions.

Organic compounds (minerals)

Amino acids (/əˈmn/, /əˈmn/, or /ˈæmɪn/) are biologically important organic compounds made from amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. Structurally they can be classified according to the functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.) In the form of proteins, amino acids comprise the second largest component (after water) of human muscles, cells and other tissues. Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.

Amino acids having both the amine and carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance in biochemistry. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases where R is an organic substituent known as a "side-chain"); often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids which combine into peptide chains ("polypeptides") to form the building blocks of a vast array of proteins. These are all L-stereoisomers ("left-handed" isomers) although a few D-amino acids ("right-handed") occur in bacterial envelopes and some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are pyrrolysine (found in methanogenic organisms and other eukaryotes) and selenocysteine (present in many noneukaryotes as well as most eukaryotes). For example, 25 human proteins include selenocysteine (Sec) in their primary structure, and the structurally characterized enzymes (selenoenzymes) employ Sec as the catalytic moiety in their active sites. Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

Amino acids (/əˈmn/, /əˈmn/, or /ˈæmɪn/) are biologically important organic compounds made from amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. Structurally they can be classified according to the functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.) In the form of proteins, amino acids comprise the second largest component (after water) of human muscles, cells and other tissues. Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.

Amino acids having both the amine and carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance in biochemistry. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases where R is an organic substituent known as a "side-chain"); often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids which combine into peptide chains ("polypeptides") to form the building blocks of a vast array of proteins. These are all L-stereoisomers ("left-handed" isomers) although a few D-amino acids ("right-handed") occur in bacterial envelopes and some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are pyrrolysine (found in methanogenic organisms and other eukaryotes) and selenocysteine (present in many noneukaryotes as well as most eukaryotes). For example, 25 human proteins include selenocysteine (Sec) in their primary structure, and the structurally characterized enzymes (selenoenzymes) employ Sec as the catalytic moiety in their active sites. Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

An essential amino acid or indispensable amino acid is an amino acid that cannot be synthesized natively by the organism being considered, and therefore must be supplied in its diet.

Proteinogenic amino acids are amino acids that are precursors to proteins, and are produced by cellular machinery coded for in the genetic code of any organism. There are 22 standard amino acids, but only 21 are found in eukaryotes. Of the 22, selenocysteine and pyrrolysine are incorporated into proteins by distinctive biosynthetic mechanisms. The other 20 are directly encoded by the universal genetic code. Humans can synthesize 11 of these 20 from each other or from other molecules of intermediary metabolism. The other 9 must be consumed (usually as their protein derivatives) in the diet and so are thus called essential amino acids. The essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

The word proteinogenic means "protein building". Proteinogenic amino acids can be condensed into a polypeptide (the subunit of a protein) through a process called translation (the second stage of protein biosynthesis, part of the overall process of gene expression).

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a protein, DNA, or RNA molecule, and which is important to its function. The structure of these molecules is frequently decomposed into primary structure, secondary structure, tertiary structure, and quaternary structure. The scaffold for this structure is provided by secondary structural elements which are hydrogen bonds within the molecule. This leads to several recognizable "domains" of protein structure and nucleic acid structure, including secondary structure like hairpin loops, bulges and internal loops for nucleic acids, and alpha helices and beta sheets for proteins.

The terms primary, secondary, tertiary, and quaternary structure were first coined by Kaj Ulrik Linderstrøm-Lang in his 1951 Lane Medical Lectures at Stanford University.

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. For example, humans are able to synthesise only 12 of the 20 standard amino acids.

A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.

[(4-formyl-5-hydroxy-6-methylpyridin-3-yl)methoxy]phosphonic acid

Pyridoxal 5-phosphate, PAL-P, PLP, Vitamin B6 phosphate

Inborn errors of amino acid metabolism are metabolic disorders which impair the synthesis and degradation of amino acids.

Types include:

Protein Lysine

Peptide sequence, or amino acid sequence, is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.

Many peptide sequences have been in sequence databases. These databases may use various notations to describe the peptide sequence. The full names of the amino acids are rarely given; instead, 3-letter or 1-letter abbreviations are usually recorded for conciseness.

polymer Polymer

Polymer banknotes are banknotes made from a polymer such as biaxially oriented polypropylene (BOPP). Such notes incorporate many security features not available to paper banknotes, including the use of metameric inks; they also last significantly longer than paper notes, resulting in a decrease in environmental impact and a reduction of production and replacement costs. Modern polymer banknotes were first developed by the Reserve Bank of Australia (RBA), CSIRO and The University of Melbourne. They were first issued as currency in Australia in 1988 (coinciding with that country's Bicentenary year). In 1996 Australia switched completely to polymer banknotes . Countries that have since switched completely to polymer banknotes include Brunei, New Zealand, Papua New Guinea, Romania, Vietnam and Canada.

In 1967 forgeries of the Australian $10 note were found in circulation and the Reserve Bank of Australia was concerned about an increase in counterfeiting with the release of colour photocopiers that year. In 1968 the RBA started collaborations with CSIRO and funds were made available in 1969 for the experimental production of distinctive papers. The insertion of an optically variable device (OVD) created from diffraction gratings in plastic as a security device inserted in banknotes was proposed in 1972. The first patent arising from the development of polymer banknotes was filed in 1973. In 1974 the technique of lamination was used to combine materials; the all-plastic laminate eventually chosen was a clear, BOPP laminate, in which OVDs could be inserted without needing to punch holes.

Polymer chemistry or macromolecular chemistry is a multidisciplinary science that deals with the chemical synthesis and chemical properties of polymers or macromolecules. According to IUPAC recommendations, macromolecules refer to the individual molecular chains and are the domain of chemistry. Polymers describe the bulk properties of polymer materials and belong to the field of polymer physics as a subfield of physics.

Polymer chemistry is that branch of one, which deals with the study of synthesis and properties of macromolecules.

Polymer science or macromolecular science is a subfield of materials science concerned with polymers, primarily synthetic polymers such as plastics and elastomers. The field of polymer science includes researchers in multiple disciplines including chemistry, physics, and engineering.

This science comprises three main sub-disciplines:

Biopolymer

Polymer engineering is generally an engineering field that designs, analyses, and/or modifies polymer materials. Polymer engineering covers aspects of petrochemical industry, polymerization, structure and characterization of polymers, properties of polymers, compounding and processing of polymers and description of major polymers, structure property relations and applications.

The basic division of polymers into thermoplastics and thermosets helps define their areas of application. The latter group of materials includes phenolic resins, polyesters and epoxy resins, all of which are used widely in composite materials when reinforced with stiff fibres such as fibreglass and aramids. Since crosslinking stabilises the thermosetting matrix of these materials, they have physical properties more similar to traditional engineering materials like steel. However, their very much lower densities compared with metals makes them ideal for lightweight structures. In addition, they suffer less from fatigue, so are ideal for safety-critical parts which are stressed regularly in service.

Ferroelectric Polymers are a group of crystalline polar polymers that are also ferroelectric, meaning that they maintain a permanent electric polarization that can be reversed, or switched, in an external electric field.

Ferroelectric polymers, such as polyvinylidene fluoride(PVDF), are used in acoustic transducers and electromechanical actuators because of their inherent piezoelectric response, and as heat sensors because of their inherent pyroelectric response.

Adsorption is the adhesion of ions or molecules onto the surface of another phase. Adsorption may occur via physisorption and chemisorption. Ions and molecules can adsorb to many types of surfaces including polymer surfaces. A polymer is a large molecule composed of repeating subunits bound together by covalent bonds. The adsorption of ions and molecules to polymer surfaces plays a role in many applications including: biomedical, structural, and coatings.

Polymer Journal is the official journal of the Society of Polymer Science, Japan (SPSJ) and publishes original articles, notes, short communications and reviews on developments in macromolecule research. It is an international peer-reviewed journal that is published on a monthly basis. The current Editor-in-Chief is Toshikazu Takata of Tokyo Institute of Technology.


1.5-1.7US$/A·h

Lithium-ion polymer batteries, polymer lithium ion or more commonly lithium polymer batteries (abbreviated Li-poly, Li-Pol, LiPo, LIP, PLI or LiP) are rechargeable (secondary cell) batteries. LiPo batteries are usually composed of several identical secondary cells in parallel to increase the discharge current capability, and are often available in series "packs" to increase the total available voltage.

A peptide bond (amide bond) is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. The resulting C(O)NH bond is called a peptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called a peptide link. Polypeptides and proteins are chains of amino acids held together by peptide bonds, as is the backbone of PNA.

A peptide bond can be broken by hydrolysis (the adding of water). In the presence of water they will break down and release 8–16 kilojoule/mol (2–4 kcal/mol) of free energy. This process is extremely slow (up to 1000 years). In living organisms, the process is facilitated by enzymes. Living organisms also employ enzymes to form peptide bonds; this process requires free energy. The wavelength of absorbance for a peptide bond is 190–230 nm (which makes it particularly susceptible to UV radiation).

A peptide bond (amide bond) is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. The resulting C(O)NH bond is called a peptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called a peptide link. Polypeptides and proteins are chains of amino acids held together by peptide bonds, as is the backbone of PNA.

A peptide bond can be broken by hydrolysis (the adding of water). In the presence of water they will break down and release 8–16 kilojoule/mol (2–4 kcal/mol) of free energy. This process is extremely slow (up to 1000 years). In living organisms, the process is facilitated by enzymes. Living organisms also employ enzymes to form peptide bonds; this process requires free energy. The wavelength of absorbance for a peptide bond is 190–230 nm (which makes it particularly susceptible to UV radiation).

Protein

Amino acids (/əˈmn/, /əˈmn/, or /ˈæmɪn/) are biologically important organic compounds made from amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. Structurally they can be classified according to the functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.) In the form of proteins, amino acids comprise the second largest component (after water) of human muscles, cells and other tissues. Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.

Amino acids having both the amine and carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance in biochemistry. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases where R is an organic substituent known as a "side-chain"); often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids which combine into peptide chains ("polypeptides") to form the building blocks of a vast array of proteins. These are all L-stereoisomers ("left-handed" isomers) although a few D-amino acids ("right-handed") occur in bacterial envelopes and some antibiotics. Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are pyrrolysine (found in methanogenic organisms and other eukaryotes) and selenocysteine (present in many noneukaryotes as well as most eukaryotes). For example, 25 human proteins include selenocysteine (Sec) in their primary structure, and the structurally characterized enzymes (selenoenzymes) employ Sec as the catalytic moiety in their active sites. Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

Proline

Pyrrolidine-2-carboxylic acid

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. In general, this occurs by the hydrolysis of the peptide bond, and is most commonly achieved by cellular enzymes called proteases, but may also occur by intramolecular digestion, as well as by non-enzymatic methods such as the action of mineral acids and heat.

Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells.

The Peptidyl transferase is an aminoacyltransferase (EC 2.3.2.12) as well as the primary enzymatic function of the ribosome, which forms peptide bonds between adjacent amino acids using tRNAs during the translation process of protein biosynthesis.

Peptidyl transferase activity is carried out by the ribosome. Peptidyl transferase activity is not mediated by any ribosomal proteins but by ribosomal RNA (rRNA), a ribozyme. This RNA relic is the most significant piece of evidence supporting the RNA World hypothesis.

Hydrolysis

A condensation reaction, also commonly referred to as dehydration synthesis, is a chemical reaction in which two molecules or moieties (functional groups) combine to form a larger molecule, together with the loss of a small molecule. Possible small molecules lost are water, hydrogen chloride, methanol, or acetic acid. The word "condensation" suggests a process in which two or more things are brought "together" (Latin "con") to form something "dense", like in condensation from gaseous to liquid state of matter; this does not imply, however, that condensation reaction products have greater density than reactants.

When two separate molecules react, the condensation is termed intermolecular. A simple example is the condensation of two amino acids to form the peptide bond characteristic of proteins. This reaction example is the opposite of hydrolysis, which splits a chemical entity into two parts through the action of the polar water molecule, which itself splits into hydroxide and hydrogen ions. Hence energy is released.

Peptide sequence, or amino acid sequence, is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.

Many peptide sequences have been in sequence databases. These databases may use various notations to describe the peptide sequence. The full names of the amino acids are rarely given; instead, 3-letter or 1-letter abbreviations are usually recorded for conciseness.

In geometry, a dihedral or torsion angle is the angle between two planes.

The dihedral angle of two planes can be seen by looking at the planes "edge on", i.e., along their line of intersection. The dihedral angle \scriptstyle \varphi_{AB} between two planes denoted A and B is the angle between their two normal unit vectors \scriptstyle \mathbf{n}_{A} and \scriptstyle \mathbf{n}_{B}:

A carboxylic acid /ˌkɑrbɒkˈsɪlɪk/ is an organic acid characterized by the presence of at least one carboxyl group. The general formula of a carboxylic acid is R-COOH, where R is some monovalent functional group. A carboxyl group (or carboxy) is a functional group consisting of a carbonyl (RR'C=O) and a hydroxyl (R-O-H), which has the formula -C(=O)OH, usually written as -COOH or -CO2H.

Carboxylic acids are Brønsted-Lowry acids because they are proton (H+) donors. They are the most common type of organic acid. Among the simplest examples are formic acid H-COOH, which occurs in ants, and acetic acid 3CH-COOH, which gives vinegar its sour taste. Acids with two or more carboxyl groups are called dicarboxylic, tricarboxylic, etc. The simplest dicarboxylic example is oxalic acid (COOH)2, which is just two connected carboxyls. Mellitic acid is an example of a hexacarboxylic acid. Other important natural examples are citric acid (in lemons) and tartaric acid (in tamarinds).

A carboxylic acid /ˌkɑrbɒkˈsɪlɪk/ is an organic acid characterized by the presence of at least one carboxyl group. The general formula of a carboxylic acid is R-COOH, where R is some monovalent functional group. A carboxyl group (or carboxy) is a functional group consisting of a carbonyl (RR'C=O) and a hydroxyl (R-O-H), which has the formula -C(=O)OH, usually written as -COOH or -CO2H.

Carboxylic acids are Brønsted-Lowry acids because they are proton (H+) donors. They are the most common type of organic acid. Among the simplest examples are formic acid H-COOH, which occurs in ants, and acetic acid 3CH-COOH, which gives vinegar its sour taste. Acids with two or more carboxyl groups are called dicarboxylic, tricarboxylic, etc. The simplest dicarboxylic example is oxalic acid (COOH)2, which is just two connected carboxyls. Mellitic acid is an example of a hexacarboxylic acid. Other important natural examples are citric acid (in lemons) and tartaric acid (in tamarinds).

2,4,6-trihydroxybenzoic acid

PGCA
Phloroglucinic acid
Acetylphloroglucinol

Ester

Formic acid

Methanoic Acid

Perfluorinated carboxylic acids (PFCAs), or perfluorocarboxylates are fully fluorinated organofluorine compounds—or perfluorinated compounds—with carboxylic acid or carboxylate functional groups. PFCAs are fluorocarbon derivatives. The simplest PFCA is trifluoroacetic acid.

Larger PFCAs such as perfluorooctanoic acid (PFOA) are under scrutiny for their toxicity and presence in humans, which is more than that of wildlife. Longer chained PFCAs such as perfluorononanoic acid are more bioaccumulative and can predominate in wildlife biomonitoring samples.

3,4-dihydro-2H-pyrrole-2-carboxylic acid

C1CC(N=C1)C(=O)O

1-Aminocyclopropanecarboxylic acid

C(O)(=O)C1(CC1)(N) 

In chemistry, and especially in biochemistry, a fatty acid is a carboxylic acid with a long aliphatic tail (chain), which is either saturated or unsaturated. Most naturally occurring fatty acids have a chain of an even number of carbon atoms, from 4 to 28. Fatty acids are usually derived from triglycerides or phospholipids. When they are not attached to other molecules, they are known as "free" fatty acids. Fatty acids are important sources of fuel because, when metabolized, they yield large quantities of ATP. Many cell types can use either glucose or fatty acids for this purpose. In particular, heart and skeletal muscle prefer fatty acids. Despite long-standing assertions to the contrary, the brain can use fatty acids as a source of fuel in addition to glucose and ketone bodies.

Azetidine-2-carboxylic Acid

O=C(O)[C@H]1NCC1

Pentanoic acid

Valeric acid
Butane-1-carboxylic acid
Valerianic acid

Chemistry Biology Nutrition

Molecular biology /məˈlɛkjʊlər/ is the branch of biology that deals with the molecular basis of biological activity. This field overlaps with other areas of biology and chemistry, particularly genetics and biochemistry. Molecular biology chiefly concerns itself with understanding the interactions between the various systems of a cell, including the interactions between the different types of DNA, RNA and protein biosynthesis as well as learning how these interactions are regulated.

Writing in Nature in 1961, William Astbury described molecular biology as:

Proteomics Proteins Biochemistry Metabolism Education
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