Abstract:
:Few techniques can identify interactions between proteins and individual water molecules when the protein is in solution. The present work has sought to bridge the gap between the molecular level studies and the search for a physical property of the solution (bathing the proteins) that would regulate the protein hydration level. The properties of the solution were varied by adding nondenaturing solutes and solvents to the protein solutions and then studying their effect on the intrinsic fluorescence of apomyoglobin. The resolution of the tryptophan emission into the two component spectra corresponding to tryptophans W7 (accessible to the solvent) and W14 (buried in the protein matrix) has allowed us to probe two specific parts of the protein. Whereas W14 is not affected when the medium is altered, the analysis of W7 fluorescence has shown that cosolvent diffusion plays a dominant role in the mobility of water molecules near the protein surface.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Twist C,Royer C,Alpert Bdoi
10.1021/bi012210+subject
Has Abstractpub_date
2002-08-13 00:00:00pages
10343-50issue
32eissn
0006-2960issn
1520-4995pii
bi012210+journal_volume
41pub_type
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