Picture of a black hole

Strathclyde Open Access research that creates ripples...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of research papers by University of Strathclyde researchers, including by Strathclyde physicists involved in observing gravitational waves and black hole mergers as part of the Laser Interferometer Gravitational-Wave Observatory (LIGO) - but also other internationally significant research from the Department of Physics. Discover why Strathclyde's physics research is making ripples...

Strathprints also exposes world leading research from the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin

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 1463-9076

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

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.