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In vulcanization, sulfur is the cross-linking agent. Its introduction changes rubber to a more rigid, durable material associated with car and bike tires. This process is often called sulfur curing. In most cases, cross-linking is irreversible, and the resulting thermosetting material will degrade or burn if heated, without melting. Chemical ...
Bissulfosuccinimidyl suberate is an example of a homobifunctional crosslinker. ... for isotopically labeling protein and peptides in mass spectrometry research ...
The cross-linked complex is highly stable and can be exposed to various enzymatic and digestion conditions, allowing many different peptide options for detection. MS or MS/MS techniques are used to detect the amino-acid locations of the labelled cross-linkers and the bound peptides (both epitope and paratope are determined in one experiment ...
Another case of an isopeptide linking enzyme for structural purposes is the actin cross-linking domain (ACD) of the MARTX toxin protein generated by V. cholerae. While it has been shown that the ACD when performing the catalysis uses magnesium and ATP for the formation of the cross-links the specifics of the mechanism are uncertain.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the
PBPs normally catalyze the cross-linking of the bacterial cell wall, but they can be permanently inhibited by penicillin and other β-lactam antibiotics. (NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine) [2] Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin.
Some models of bonding for desmosines, created through the study of bovine ligament elastin, suggest a combination of desmosine and secondary cross-linking to bind together peptide chains. This model has desmosine bonding near an alanine on the peptide chain, then to 3 other amino acids on the 2 peptide chains, despite being able to bond to up ...
Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. [1] Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). [2] The reaction is [1]