A simple method to predict protein flexibility using secondary chemical shifts

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DOIResolve DOI: http://doi.org/10.1021/ja054842f
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TypeArticle
Journal titleJACS: Journals of the American Chemical Society
ISSN00027863
Volume127
Issue43
Pages1497014971; # of pages: 2
AbstractProtein motions play a critical role in many biological processes, such as enzyme catalysis, allosteric regulation, antigen-antibody interactions, and protein-DNA binding. NMR spectroscopy occupies a unique place among methods for investigating protein dynamics due to its ability to provide site-specific information about protein motions over a large range of time scales. However, most NMR methods require a detailed knowledge of the 3D structure and/or the collection of additional experimental data (NOEs, T₁, T₂, etc.) to accurately measure protein dynamics. Here we present a simple method based on chemical shift data that allows accurate, quantitative, site-specific mapping of protein backbone mobility without the need of a three-dimensional structure or the collection and analysis of NMR relaxation data. Further, we show that this chemical shift method is able to quantitatively predict per-residue RMSD values (from both MD simulations and NMR structural ensembles) as well as model-free backbone order parameters.
Publication date
LanguageEnglish
Peer reviewedNo
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

Identifier10072378
NPARC number12338298
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Record identifierbd23755d-bbf3-4db9-b0e8-055e79f6d825
Record created2009-09-10
Record modified2016-05-09
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