Question:

Who discovered melatonin?

Answer:

Melatonin was discovered in 1958 by American physician Aaron B. Lerner & his colleagues at Yale University School of Medicine.Melatonin, a derivative of the amino acid tryptophan, is produced in humans, other mammals, birds, reptiles, and amphibians.

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physician

Aaron Bunsen Lerner (September 21, 1920–February 3, 2007) was an American physician, researcher and professor. Born in 1920 in Minneapolis, he received his medical degree and a PhD in chemistry from the University of Minnesota in 1945. After teaching at the universities of Michigan and Oregon, he joined the Yale University School of Medicine as an associate professor of medicine in 1955. The following year he became director of the dermatology section within the Department of Internal Medicine, and when the Department of Dermatology was established in 1971 he was appointed its first chair. When Professor Lerner retired in 1991 he was named a Professor Emeritus of Dermatology. He was in 1973 elected to membership in the National Academy of Sciences (Medical physiology and metabolism).

Dr. Lerner is perhaps best known for leading the team of researchers who isolated and named, in 1958, the hormone melatonin. He was an expert in the metabolic basis of inherited diseases, particularly vitiligo for which he, in the 1980s, developed a skin transplantation therapy. Lerner also isolated the compound melanocyte-stimulating hormone (MSH).

Yale University School of Medicine.Melatonin

A circadian rhythm /sɜrˈkdiən/ is any biological process that displays an endogenous, entrainable oscillation of about 24 hours. These rhythms are driven by a circadian clock, and rhythms have been widely observed in plants, animals, fungi and cyanobacteria. The term circadian comes from the Latin circa, meaning "around" (or "approximately"), and diem or dies, meaning "day". The formal study of biological temporal rhythms, such as daily, tidal, weekly, seasonal, and annual rhythms, is called chronobiology. Although circadian rhythms are endogenous ("built-in", self-sustained), they are adjusted (entrained) to the local environment by external cues called zeitgebers, commonly the most important of which is daylight.

Acetamides Antioxidants Melatonin

The emphasis of the treatment of bipolar disorder is on effective management of the long-term course of the illness, which can involve treatment of emergent symptoms. Treatment methods include pharmacological and psychological techniques.

Tryptophan

Aaron Bunsen Lerner (September 21, 1920–February 3, 2007) was an American physician, researcher and professor. Born in 1920 in Minneapolis, he received his medical degree and a PhD in chemistry from the University of Minnesota in 1945. After teaching at the universities of Michigan and Oregon, he joined the Yale University School of Medicine as an associate professor of medicine in 1955. The following year he became director of the dermatology section within the Department of Internal Medicine, and when the Department of Dermatology was established in 1971 he was appointed its first chair. When Professor Lerner retired in 1991 he was named a Professor Emeritus of Dermatology. He was in 1973 elected to membership in the National Academy of Sciences (Medical physiology and metabolism).

Dr. Lerner is perhaps best known for leading the team of researchers who isolated and named, in 1958, the hormone melatonin. He was an expert in the metabolic basis of inherited diseases, particularly vitiligo for which he, in the 1980s, developed a skin transplantation therapy. Lerner also isolated the compound melanocyte-stimulating hormone (MSH).

Amino acids (/əˈmn/, /əˈmn/, or /ˈæmɪn/) are biologically important organic compounds composed of 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.

Reptile Chemistry Biology

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.

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