NDLI: Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?

Content Provider	PubMed Central
Author	Kornblatt, J. A. Kornblatt, M. J. Hoa, G. H. Mauk, A. G.
Abstract	We have analyzed the stability of the cytochrome c-cytochrome b5 and cytochrome c-cytochrome c oxidase complexes as a function of solvent stress. High concentrations of glycerol were used to displace the two equilibria. Glycerol promotes complex formation between cytochrome c and cytochrome b5 but inhibits that between cytochrome c and cytochrome c oxidase. The results with cytochrome b5 and cytochrome c were expected; the association of this complex is largely entropy driven. Our interpretation is that the cytochrome c-cytochrome b5 complex excludes water. The results with the cytochrome c oxidase and cytochrome c couple were not expected. We interpret them to mean that either glycerol is binding to the oxidase, thereby displacing the cytochrome c, or that water is required at this protein-protein interface. A requirement for substantial quantities of water at the interface of some protein complexes is logical but has been reported only once.
Related Links	http://dx.doi.org/10.1016/s0006-3495(93)81168-8
Ending Page	1065
Page Count	7
Starting Page	1059
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	3
Volume Number	65
Language	English
Publisher Date	1993-09-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?