Detection of a very rapid first phase in complex formation of DnaK and peptide substrate
Complex formation of the Hsp70 chaperone DnaK with the fluorescence-labeled peptide ALLLSAPRR shows a very rapid first phase that has as yet not been observed with other peptides. This first phase is completed within the dead time (1–2 ms) of the stopped-flow instrument and corresponds to two thirds...
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Veröffentlicht in: | FEBS letters 2002-06, Vol.520 (1), p.25-29 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Complex formation of the Hsp70 chaperone DnaK with the fluorescence-labeled peptide ALLLSAPRR shows a very rapid first phase that has as yet not been observed with other peptides. This first phase is completed within the dead time (1–2 ms) of the stopped-flow instrument and corresponds to two thirds of the total increase in fluorescence. It occurs both in the presence and in the absence of ATP and is followed by a fast, a slow and a very slow step. These binding kinetics that are vastly different from those observed with other peptides might indicate the existence of a second substrate-binding site of DnaK. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(02)02752-7 |