Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / metabolism
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Amino Acid Sequence
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Amino Acids / analysis
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Binding Sites
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Binding, Competitive
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Chemical Phenomena
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Chemistry, Physical
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Fungal Proteins / metabolism*
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HSP70 Heat-Shock Proteins*
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Heat-Shock Proteins / metabolism*
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / metabolism*
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Protein Conformation
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Thermodynamics
Substances
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Amino Acids
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Fungal Proteins
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HSP70 Heat-Shock Proteins
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Heat-Shock Proteins
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KAR2 protein, yeast
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Peptides
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Adenosine Triphosphatases