Related Research Articles
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, in turn relating greatly to the understanding of tissues and organs as well as organism structure and function. Biochemistry is closely related to molecular biology, the study of the molecular mechanisms of biological phenomena.
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). In the gas phase, it is a molecule with the chemical formula NH2‐CH2‐COOH. In solution or in the solid, glycine exists as the zwitterion. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction.
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. It contains an α-amino group (which is in the protonated −NH+
3 form when dissolved in water), an α-carboxylic acid group (which is in the deprotonated −COO− form when dissolved in water), and a side chain lysyl ((CH2)4NH2), classifying it as a basic, charged (at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the S configuration.
Glutamine is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral, polar amino acid. It is non-essential and conditionally essential in humans, meaning the body can usually synthesize sufficient amounts of it, but in some instances of stress, the body's demand for glutamine increases, and glutamine must be obtained from the diet. It is encoded by the codons CAA and CAG. It is named after glutamic acid, which in turn is named after its discovery in cereal proteins, gluten.
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid.
Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC.
A nutrient is a substance used by an organism to survive, grow, and reproduce. The requirement for dietary nutrient intake applies to animals, plants, fungi, and protists. Nutrients can be incorporated into cells for metabolic purposes or excreted by cells to create non-cellular structures, such as hair, scales, feathers, or exoskeletons. Some nutrients can be metabolically converted to smaller molecules in the process of releasing energy, such as for carbohydrates, lipids, proteins, and fermentation products, leading to end-products of water and carbon dioxide. All organisms require water. Essential nutrients for animals are the energy sources, some of the amino acids that are combined to create proteins, a subset of fatty acids, vitamins and certain minerals. Plants require more diverse minerals absorbed through roots, plus carbon dioxide and oxygen absorbed through leaves. Fungi live on dead or living organic matter and meet nutrient needs from their host.
Ornithine is a non-proteinogenic α-amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl.
An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine.
William Cumming Rose was an American biochemist and nutritionist. He discovered the amino acid threonine, and his research determined the necessity for essential amino acids in diet and the minimum daily requirements of all amino acids for optimal growth.
Proteins are essential nutrients for the human body. They are one of the building blocks of body tissue and can also serve as a fuel source. As a fuel, proteins provide as much energy density as carbohydrates: 4 kcal per gram; in contrast, lipids provide 9 kcal per gram. The most important aspect and defining characteristic of protein from a nutritional standpoint is its amino acid composition.
1-Pyrroline-5-carboxylic acid is a cyclic imino acid. Its conjugate base and anion is 1-pyrroline-5-carboxylate (P5C). In solution, P5C is in spontaneous equilibrium with glutamate-5-semialdhyde (GSA).
Vernon Robert Young was an expert on protein and amino acid requirements and researched how the human body processes nutrients into protein. Young was a principal organizer of amino acid Workshops sponsored by the International Council of Amino Acid Science and was the Chairman of the Council's Scientific Advisory Board.
Grace Medes was an American biochemist, who discovered tyrosinosis—a metabolic disorder today known as tyrosinemia—and studied fatty acid metabolism. She was awarded the Garvan-Olin Medal in 1955 for her work.
Constance Virginia Kies was an American nutrition scientist and dietitian. Kies worked as a public school teacher for three years before going against the traditional gender norms of her time and completing an M.S. and Ph.D. from the University of Wisconsin–Madison. Over the duration of her 30-year career at the University of Nebraska–Lincoln, Kies researched nutritional biochemistry. She demonstrated relationships between minerals, proteins, and dietary fiber through pioneering human subject research. Her findings led to advancements in human knowledge of copper and protein metabolism. She was honored with the Borden Award and was a fellow of the American College of Nutrition. Kies was a feminist and a member of the National Organization for Women and the Women's Equity Action League. She died of uterine cancer three months after her diagnosis.
Daisy Yen Wu was the first Chinese woman engaged as an academic researcher in biochemistry and nutrition. Born into a wealthy industrial family in Shanghai, from a young age she was tutored in English and encouraged to study. She graduated from Nanjing Jinling Women's University in 1921 and then studied in the United States, graduating with a master's degree in biochemistry from Teachers College, Columbia University in 1923. Returning to China, she became an assistant professor at Peking Union Medical College between 1923 and her marriage at the end of 1924 to Hsien Wu. Collaborating with him, she conducted research on proteins and studied nutrition. After their marriage she continued to assist in the research conducted by Wu as an unpaid staff member until 1928. She and her husband collaborated in writing the first Chinese textbook on nutrition, which remained in print through the 1990s.
Patrick J. Stover is an American nutrition scientist who researches B vitamins. He is a fellow of the American Association for the Advancement of Science and a member of the National Academy of Sciences. He has been co-editor of the Annual Review of Nutrition since 2015.
Barbara Jean Francis Apgar is an American biochemist. She worked on important research on ribonucleic acids (RNA), and on zinc deficiency as a risk factor in reproduction. She won the Federal Woman's Award in 1970, and the Arthur S. Flemming Award in 1973.
References
- 1 2 "Guoyao Wu". Texas A&M University . Retrieved November 17, 2015.
- ↑ "Guoyao Wu, Ph.D." Texas A&M University. Archived from the original on November 18, 2015. Retrieved November 17, 2015.
- ↑ "AAAS Members Elected as Fellows". American Association for the Advancement of Science . Retrieved November 17, 2015.
- ↑ "Archives: 2014 HCR as of September 8 2015". Thomson Reuters . Retrieved November 17, 2015.
- ↑ "Past FASS-AFIA New Frontiers in Animal Nutrition Award Winners". Federation of Animal Science Societies. Retrieved November 17, 2015.
- ↑ "The Journal of Nutritional Biochemistry Editorial Board". Elsevier . Retrieved November 17, 2015.