Flynn G C, Pohl J, Flocco M T, Rothman J E
Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021.
Nature. 1991 Oct 24;353(6346):726-30. doi: 10.1038/353726a0.
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.
热休克蛋白家族(hsp70s)的成员能够区分折叠态和未折叠态的蛋白质。这一特性对于hsp70s作为分子伴侣的作用至关重要,并且归因于肽结合位点的氨基酸特异性。使用一组具有随机序列但确定链长的肽来研究对肽配体的特异性。肽结合位点选择脂肪族残基,并将它们容纳在能量上等同于折叠蛋白内部的环境中。