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pubmed-article:2756425pubmed:dateCreated1989-8-30lld:pubmed
pubmed-article:2756425pubmed:abstractTextTwo members of the hsp70 family, termed hsc70 and BiP, have been implicated in promoting protein folding and assembly processes in the cytoplasm and the lumen of the endoplasmic reticulum, respectively. Short hydrophilic (8 to 25 residues) synthetic peptides have now been tested as possible mimics of polypeptide chain substrates to help define an enzymatic basis for these activities. Both BiP and hsc70 have specific peptide binding sites. Peptide binding elicits hydrolysis of adenosine triphosphate, with the subsequent release of bound peptide.lld:pubmed
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pubmed-article:2756425pubmed:pagination385-90lld:pubmed
pubmed-article:2756425pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2756425pubmed:articleTitlePeptide binding and release by proteins implicated as catalysts of protein assembly.lld:pubmed
pubmed-article:2756425pubmed:affiliationDepartment of Biology, Lewis Thomas Laboratory, Princeton University, NJ 08544.lld:pubmed
pubmed-article:2756425pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2756425pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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