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Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
In biochemistry, the Corey-Pauling rules are a set of three basic statements that govern the secondary nature of proteins, in particular, the CO-NH peptide link. They were originally proposed by Robert Corey and Linus Pauling. [1] The rules are as follows: The atoms in a peptide link all lie on the same plane.
In longer ribbons, this bonding is continued in peptides of 8, 10, etc., amino acid residues. A beta bend ribbon can be regarded as an aberrant 310 helix (3/10-helix) that has lost some of its hydrogen bonds. [9] Two websites are available to facilitate finding and examining these features in proteins: Motivated Proteins; [10] and PDBeMotif. [11]
Peptide fragments refer to fragments of proteins that are used to identify or quantify the source protein. [17] Often these are the products of enzymatic degradation performed in the laboratory on a controlled sample, but can also be forensic or paleontological samples that have been degraded by natural effects.
In molecular biology and biochemistry, glycoconjugates are the classification family for carbohydrates – referred to as glycans – which are covalently linked with chemical species such as proteins, peptides, lipids, and other compounds. [1] Glycoconjugates are formed in processes termed glycosylation.
Glycopeptides are peptides that contain carbohydrate moieties covalently attached to the side chains of the amino acid residues that constitute the peptide.. Over the past few decades it has been recognised that glycans on cell surface (attached to membrane proteins or lipids) and those bound to proteins (glycoproteins) play a critical role in biology.
The "chemical ligation" concept was introduced by Kent in the early 1990s. [1] It consisted of a novel approach to the covalent condensation of unprotected peptide segments by means of "unique, mutually reactive functionalities, one on each reacting peptide segment, designed to react only with each other and not with any of the functional groups found in (native) peptides".
Signaling peptide receptor is a type of receptor which binds one or more signaling peptides or signaling proteins.. An example is the tropomyosin receptor kinase B (TrkB), which is bound and activated by the neurotrophic protein brain-derived neurotrophic factor (BDNF).