Scanning and Escape during Protein-disulfide Isomerase-assisted Protein Folding

During oxidative protein folding, efficient catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escape mechanism that prevents the enzyme from becoming trapped in covalent complexes with substrates that fail to rearrange in a timely fashion. Protein-disulfide...

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Veröffentlicht in:	The Journal of biological chemistry 1997-04, Vol.272 (14), p.8845-8848
Hauptverfasser:	Walker, K W, Gilbert, H F
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Buffers Cattle Dithiothreitol - pharmacology Glutathione - analogs & derivatives Glutathione - pharmacology Glutathione Disulfide Isomerases - metabolism Isomerism Models, Molecular Oxidation-Reduction Protein Conformation Protein Disulfide-Isomerases Rats Ribonucleases - metabolism Sulfhydryl Reagents - pharmacology
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