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Thermodynamic and Structural Effects of a Single Backbone Hydrogen Bond Deletion in a Metal-Assembled Helical Bundle Protein

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Jian Zhou,^† Martin A. Case,^† James F. Wishart,^‡ and George L. McLendon*^†

Department of Chemistry, Princeton University, Princeton, New Jersey 08544, and Chemistry Department, Brookhaven National Laboratory, Upton, New York 11973

J. Phys. Chem. B, 1998, 102 (49), pp 9975–9980

DOI: 10.1021/jp982852f

Publication Date (Web): December 3, 1998

Section:

General Biochemistry

Abstract

Transition metal ion-assembled three-helix bundle proteins provide templates to investigate the thermodynamic and dynamic structural consequences of the deletion of a single backbone hydrogen bond from an α-helical architecture. This deletion does not perturb the steady-state secondary structure of the protein as measured by circular dichroism spectroscopy but does decrease the overall folding free energy by ca. 0.7 kcal/mol. We have used intraprotein electron transfer as a measure of the structure-sensitive dynamics of our system. The deletion of a single hydrogen bond in one of the helices of a three-helix bundle does not significantly change the measured electron-transfer rate. This is in agreement with “Greenpath” electron-transfer pathway calculations, which assume a constant and invariant structure for the architecture. Given the exponential dependence of electron-transfer rate on distance and that fluctuations in the intervening secondary structure will cause variations in electron donor−acceptor distances, the measured electron-transfer rate associated with hydrogen bond deletion allows us to calculate a differential dynamic structural fluctuation associated with hydrogen bond deletion of less than 0.6 Å over the millisecond time scale of the experiment.

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This article has been cited by 8 ACS Journal articles (5 most recent appear below).

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Do Main Chain Hydrogen Bonds Create Dominant Electron Transfer Pathways? An Investigation in Designed Proteins
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The Journal of Physical Chemistry B2003 107 (30), 7288-7292
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Electron Transfer through a Prenucleated Bimetalated Alanine-Based Peptide Helix
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