Journal
JOURNAL OF COMPUTATIONAL CHEMISTRY
Volume 25, Issue 7, Pages 974-984Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/jcc.20029
Keywords
conformational fluctuations; electronic properties; Myoglobin; perturbed matrix method
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In this article we use the recently developed perturbed matrix method (PMM) to investigate the effect of conformational fluctuations on the electronic properties of heme in Myoglobin. This widely studied biomolecule has been chosen as a benchmark for evaluating the accuracy of PMM in a large and complex system. Using a long, 80-ns, molecular dynamics simulation and unperturbed Configuration Interaction (CISD) calculations in PMM, we reproduced the main spectroscopic features of deoxy-Myoglobin. Moreover, in line with our previous results on a photosensitive protein, this study reveals a clear dynamical coupling between electronic properties and conformational fluctuations, suggesting that this correlation could be a general feature of proteins. (C) 2004 Wiley Periodicals, Inc.
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