The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain)
A nutritional condition produced by a deficiency of proteins in the diet, characterized by adaptive enzyme changes in the liver, increase in amino acid synthetases, and diminution of urea formation, thus conserving nitrogen and reducing its loss in the urine. Growth, immune response, repair, and production of enzymes and hormones are all impaired in severe protein deficiency. Protein deficiency may also arise in the face of adequate protein intake if the protein is of poor quality (i.e., the content of one or more amino acids is inadequate and thus becomes the limiting factor in protein utilization). (From Merck Manual, 16th ed; Harrison's Principles of Internal Medicine, 12th ed, p406)
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Protein deficiency -- See Also the narrower term Marasmus
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Protein Deficiency : Glutathione and sulfur amino acids in human health and disease / edited by Roberta Masella, Giuseppe Mazza
2009
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Protein Deficiency -- complications. : Dietary proteins : how they alleviate disease and promote better health / edited by George U. Liepa ; associate editors, Donald C. Beitz, Anton C. Beynen, Mary Anne Gorman
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational
Here are entered works on biochemical and genetic engineering processes involved in the synthesis, modification, and production of protein products for various applications
Proteins which are present in or isolated from vegetables or vegetable products used as food. The concept is distinguished from PLANT PROTEINS which refers to non-dietary proteins from plants
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE
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Protein disulfide isomerase. : Foldases catalyzing the formation and isomerization of disulfide bonds in proteins / Natalya K. Nagradova
Protein drugs -- Physiological transport : Coordination chemistry in protein cages principles, design, and applications / edited by Takafumi Ueno, Yoshihito Watanabe
2013
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Protein electrophoresis : Chemical modification of proteins / A.N. Glazer, R.J. DeLange and D.S. Sigman. Separation methods for nucleic acids and oligonucleotides / Hannah Gould and H.R. Matthews
1976
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Protein-Energy Malnutrition -- See Also Emaciation
Clinical manifestation of excessive LEANNESS usually caused by disease or a lack of nutrition (MALNUTRITION)
Here are entered works on laboratory or engineering processes for the modification of proteins. Works on natural processes for the modification of proteins in cells and tissues are entered under Post-translational modification
Protein engineering -- Congresses : Understanding biology using peptides : proceedings of the Nineteenth American Peptide Symposium / edited by Sylvie E. Blondelle
Protein engineering -- Patents : Patenting proteomics : patentability and scope of protection of three-dimensional protein structure claims under German, European, and US Law / Martina Schuster