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Proceedings Paper

Static and dynamic disorder in protein folding: experiments with single maltoporin channels
Author(s): Lisen Kullman; Mathias Winterhalter; Sergey M. Bezrukov
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Paper Abstract

The reversible binding of sugar to a single maltoporin channel allows us to study time and ensemble variations in the channel functional properties and interpret them using the language of static and dynamic disorder in protein folding. The channel is a trimer that is characterized by two primary parameters: the rate of sugar binding and the ion conductance. Time-resolved binding of maltohexasose molecules shows that whereas dynamic disorder -- the fluctuations in binding rate or in ionic conductance of a single trimer channel with time -- is relatively small, static disorder -- the heterogeneity of reaction rates or conductances among different trimers -- is highly pronounced. This heterogeneity suggests variations in maltoporin folding. The disorder in conductance shows no measurable correlation with the disorder in binding strength; variations in protein folding that are responsible for variations in protein folding that are responsible for variations in ionic conductance do not seem to affect sugar binding. We find 'cooperativity' in static disroder: conductances of monomers in the same trimer are closely similar compared to the range of possible conductances seen over an ensemble of trimers.

Paper Details

Date Published: 30 April 2003
PDF: 7 pages
Proc. SPIE 5110, Fluctuations and Noise in Biological, Biophysical, and Biomedical Systems, (30 April 2003); doi: 10.1117/12.500833
Show Author Affiliations
Lisen Kullman, National Institutes of Health (United States)
Uppsala Univ. (Sweden)
Mathias Winterhalter, Institut Pharmacologie et Biologie Structurale (France)
Sergey M. Bezrukov, National Institutes of Health (United States)


Published in SPIE Proceedings Vol. 5110:
Fluctuations and Noise in Biological, Biophysical, and Biomedical Systems
Sergey M. Bezrukov; Hans Frauenfelder; Frank Moss, Editor(s)

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