Application of the random coil index to studying protein flexibility.

Application of the random coil index to studying protein flexibility. Research Abstract Details 

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Application of the random coil index to studying protein flexibility. Abstract Text:

Mark V Berjanskii,David S Wishart,

Protein flexibility lies at the heart of many protein-ligand binding events and enzymatic activities. However, the experimental measurement of protein motions is often difficult, tedious and error-prone. As a result, there is a considerable interest in developing simpler and faster ways of quantifying protein flexibility. Recently, we described a method, called Random Coil Index (RCI), which appears to be able to quantitatively estimate model-free order parameters and flexibility in protein structural ensembles using only backbone chemical shifts. Because of its potential utility, we have undertaken a more detailed investigation of the RCI method in an attempt to ascertain its underlying principles, its general utility, its sensitivity to chemical shift errors, its sensitivity to data completeness, its applicability to other proteins, and its general strengths and weaknesses. Overall, we find that the RCI method is very robust and that it represents a useful addition to traditional methods of studying protein flexibility. We have implemented many of the findings and refinements reported here into a web server that allows facile, automated predictions of model-free order parameters, MD RMSF and NMR RMSD values directly from backbone (1)H, (13)C and (15)N chemical shift assignments. The server is available at http://wishart.biology.ualberta.ca/rci .

Application of the random coil index to studying protein flexibility. Publishing Authors By Initials

MV Berjanskii,DS Wishart,

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Application of the random coil index to studying protein flexibility. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biomolecular NMR

VOLUME: 40

Page Numbers: 31-48

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ISSN: 0925-2738

DAY: 6

MONTH: 11

YEAR: 2007

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LANGUAGE: eng

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AFFILIATION: Department of Computing Science, University of Alberta, Edmonton, AB, Canada.

Country: Netherlands

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MEDLINETA: J Biomol NMR

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