منابع مشابه
The relationship of disulfide bonds and activity in ribonuclease.
The RNase molecule consists of a single chain, arranged in a compact, folded structure, cross-linked through 4 disulfide bridges (1). After hydrolysis to determine the amino acid composition of RNase, 8 half-cystine or cysteic acid residues have been identified (2,3) and the approximate location of these residues in the partial structural formula for oxidized RNase has been determined (4). More...
متن کاملRibonuclease A: Disulfide Bonds, Conformational Stability, and Cytotoxicity
Disulfide bonds between the side chains of cysteine residues are the only common crosslinks in proteins. Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-CysllO, and Cys65-Cys72) and catalyzes the cleavage of RNA. The contribution of each disulfide bond to the confonnational stability and catalyti...
متن کاملContribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A.
Disulfide bonds between the side chains of cysteine residues are the only common crosslinks in proteins. Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-Cys110, and Cys65-Cys72) and catalyzes the cleavage of RNA. The contribution of each disulfide bond to the conformational stability and catalyti...
متن کاملStudies on the antigenic structure of ribonuclease. I. General role of hydrogen and disulfide bonds.
Studies of protein structure have reached a stage at which chemical configuration should shortly be correlated with biological activity. Although important advances have been made in describing the antigenic structure of polysaccharides (la, 2), little progress has been made in elucidating the antigenic structure of native proteins. Reagents that modify certain types of groups on proteins have ...
متن کاملInteraction of Phosphorothioate with the Disulfide Bonds of Ribonuclease and Lysozyme.
Disulfide bonds are undoubtedly of great importance in stabilizing the native conformations of many proteins. For studies of the covalent structure of proteins it is desirable, as a first step, to cleave the disulfide bonds (1). This has been carried out either by oxidation (l-3) or by reduction followed by alkylation of the sulfhydryl groups formed (4). Iodoacetic acid (or iodoacetamide) has b...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1960
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)67918-4