from The American Heritage® Dictionary of the English Language, 4th Edition
- n. A peptide, such as a small protein, containing many molecules of amino acids, typically between 10 and 100.
from Wiktionary, Creative Commons Attribution/Share-Alike License
- n. Any polymer of (same or different) amino acids joined via peptide bonds.
- n. Any such polymer that is not folded into a secondary structure of a protein.
- n. A small protein containing up to 100 amino acids; see also oligopeptide.
from The Century Dictionary and Cyclopedia
- n. A chemical product formed by the condensation of two or more amino-acid radicals.
from WordNet 3.0 Copyright 2006 by Princeton University. All rights reserved.
- n. a peptide containing 10 to more than 100 amino acids
Sorry, no etymologies found.
This greatly reduces errors in polypeptide chain elongation, and is therefore highly favored by natural selection.
For awhile I was studying up on the presence of d-aa in polypeptide chains, with these peptides being produced biotically.
A larger number of these amino acids combined are called a polypeptide or protein, and these are chemically active in making a living being.
Secretin and other hormones of similar nature are built up of amino acid chains containing more than a dozen and less than a hundred amino acids and are therefore sometimes called polypeptide hormones rather than protein hormones.
Although several constituents of bitter melon have hypoglycemic properties, most interest has focused on a polypeptide isolated from the seeds called polypeptide-p and a mixture of two steroid glycosides referred to as charantin.
Many hormones are of a polypeptide nature, and in 1955 Vincent du Vigneaud of Cornell University was given the prize for his synthesis of two such hormones, vasopressin and oxytocin.
But you, Mr. and Ms. Olympic “Could Be If You Only Made an Effort” Athlete, you are fully entitled to the rush to be gained from endogenous opioid polypeptide compounds.
In the 1950s to 1970s, molecular biologists were sure that each DNA sequence could not encode more than one polypeptide chain.
"These findings suggest that the beneficial effects of coffee consumption on type 2 diabetes mellitus may be partly due to the ability of the major coffee components and metabolites to inhibit the toxic aggregation of hIAPP human islet amyloid polypeptide," Ling Zheng, professor of cellular biology at Wuhan University in China, and colleagues wrote.
Her research focuses on determining the structure of ribosomes, a large complex of proteins and RNA that uses a messenger RNA template to assemble amino acids into polypeptide chains.