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Title
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Effect of the Asn52----Ile mutation on the redox potential of yeast cytochrome c. Theory and experiment.
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Authors
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R.Langen,
G.D.Brayer,
A.M.Berghuis,
G.McLendon,
F.Sherman,
A.Warshel.
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Ref.
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J Mol Biol, 1992,
224,
589-600.
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PubMed id
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Abstract
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Theoretical methods for correlation of sequence changes and redox potential of
electron transport proteins are examined using the Asn52----Ile mutation in
cytochrome c as a test case. The first approach uses the protein dipoles
Langevin dipoles (PDLD) method and the high resolution X-ray structures of the
native and the mutant proteins. This approach is found to give reliable results
where all the solvent molecules are represented by Langevin dipoles and also
when some bound water molecules are represented explicitly. A free energy
perturbation method is also found to give reasonable results but at the expense
of much more computer time. Finally, an approach that generates mutant
structures from the native structure by molecular dynamics simulation and then
uses these configurations in PDLD calculations is found to give a reasonable
estimate of the effect of the mutation on the corresponding redox potential. The
encouraging results obtained here and in a preliminary test case of the
Phe82----Ser mutation indicates that the present strategies can provide a useful
tool for structure-redox and sequence-redox correlation in proteins.
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