Abstract：
:The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic resonance experiments. Distinct differences between the two states of the protein were observed. According to our data, the apo form interacts more extensively with solvent than the peptide-bound form. Significantly, the open hydrophobic substrate binding cleft of DnaK in the apo form is found to contain several molecules of water which are displaced by the binding of the hydrophobic substrate, the peptide NRLLLTG. The solvent in the hydrophobic cleft has a residence time longer than 400 ps. It is predicted that the displacement of this trapped water must contribute to the binding free energy of the natural hydrophobic substrates of this class of protein-folding chaperone proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Cai S,Stevens SY,Budor AP,Zuiderweg ERdoi
10.1021/bi030097csubject
Has Abstractpub_date
2003-09-30 00:00:00pages
11100-8issue
38eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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