|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6346
|
|
pubmed:dateCreated |
1991-11-29
|
|
pubmed:abstractText |
Members of the heat-shock protein family (hsp70s) can distinguish folded from unfolded proteins. This property is crucial to the role of hsp70s as molecular chaperones and is attributable to the amino-acid specificity of the peptide-binding site. The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length. The peptide-binding site selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0028-0836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
24
|
|
pubmed:volume |
353
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
726-30
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:1834945-Adenosine Triphosphatases,
pubmed-meshheading:1834945-Amino Acid Sequence,
pubmed-meshheading:1834945-Amino Acids,
pubmed-meshheading:1834945-Binding, Competitive,
pubmed-meshheading:1834945-Binding Sites,
pubmed-meshheading:1834945-Chemistry, Physical,
pubmed-meshheading:1834945-Fungal Proteins,
pubmed-meshheading:1834945-HSP70 Heat-Shock Proteins,
pubmed-meshheading:1834945-Heat-Shock Proteins,
pubmed-meshheading:1834945-Molecular Sequence Data,
pubmed-meshheading:1834945-Peptides,
pubmed-meshheading:1834945-Physicochemical Phenomena,
pubmed-meshheading:1834945-Protein Conformation,
pubmed-meshheading:1834945-Thermodynamics
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
Peptide-binding specificity of the molecular chaperone BiP.
|
|
pubmed:affiliation |
Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
