Adamczyk, Katrin and Candelaresi, Marco and Kania, Rafal and Robb, Kirsty and Bellota-Anton, Cesar and Greetham, Gregory M. and Pollard, Mark R. and Towrie, Michael and Parker, Anthony W. and Hoskisson, Paul A. and Tucker, Nicholas P. and Hunt, Neil T. (2012) The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin. Physical Chemistry Chemical Physics, 14 (20). pp. 7411-7419. ISSN 1463-9076Full text not available in this repository. (Request a copy from the Strathclyde author)
The ultrafast equilibrium fluctuations of the FeIII-NO complex of a single point mutation of Myoglobin (H64Q) have been studied using Fourier Transform 2D-IR spectroscopy. Comparison with data from wild type Myoglobin (wt-Mb) shows the presence of two conformational substates of the mutant haem pocket where only one exists in the wild type form. One of the substates of the mutant exhibits an almost identical NO stretching frequency and spectral diffusion dynamics to wt-Mb while the other is distinctly different in both respects. The remarkably contrasting dynamics are largely attributable to interactions between the NO ligand and a nearby distal side chain which provides a basis for understanding the roles of these side chains in other ferric haem proteins.
|Keywords:||point mutation , ferric Myoglobin , Myoglobin , NO ligand, Solid state physics. Nanoscience, Therapeutics. Pharmacology|
|Subjects:||Science > Physics > Solid state physics. Nanoscience|
Medicine > Therapeutics. Pharmacology
|Department:||Faculty of Science > Physics|
Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
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|Depositing user:||Pure Administrator|
|Date Deposited:||30 May 2012 15:48|
|Last modified:||12 Feb 2014 19:20|
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