Functional Subconformations in Protein Folding: Evidence from Single-Channel Experiments

Lisen Kullman, Philip A. Gurnev, Mathias Winterhalter, and Sergey M. Bezrukov
Phys. Rev. Lett. 96, 038101 – Published 23 January 2006

Abstract

We study fluctuations in ion conductance and enzymatic rates of the sugar-specific channel-forming membrane protein, Maltoporin, at the single-molecule level. Specifically, we analyze time-persistent deviations in the transport parameters of individual channels from the multichannel averages and discuss our findings in the context of static disorder in protein folding. We show that the disorder responsible for variations in ion conductance does not affect sugar binding, suggesting that Maltoporin can exist in a wide set of fully functional, yet distinctly different, subconformations.

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  • Received 24 August 2005

DOI:https://doi.org/10.1103/PhysRevLett.96.038101

©2006 American Physical Society

Authors & Affiliations

Lisen Kullman1,2, Philip A. Gurnev1, Mathias Winterhalter3, and Sergey M. Bezrukov1

  • 1Laboratory of Physical and Structural Biology, NICHD, NIH, Bethesda, Maryland 20892-0924, USA
  • 2Department of Medical Cell Biology, Uppsala University, Box 571, 751 23 Uppsala, Sweden
  • 3International University of Bremen, P.O. Box 750 561, 28725 Bremen, Germany

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Issue

Vol. 96, Iss. 3 — 27 January 2006

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