Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review.
 

Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review.

Related Articles Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review.

Rep Prog Phys. 2015 Oct 30;78(12):126601

Authors: Salmon L, Blackledge M

Abstract
Nuclear magnetic resonance spectroscopy is exquisitely sensitive to protein dynamics. In particular inter-nuclear dipolar couplings, that become measurable in solution when the protein is dissolved in a dilute liquid crystalline solution, report on all conformations sampled up to millisecond timescales. As such they provide the opportunity to describe the Boltzmann distribution present in solution at atomic resolution, and thereby to map the conformational energy landscape in unprecedented detail. The development of analytical methods and approaches based on numerical simulation and their application to numerous biologically important systems is presented.


PMID: 26517337 [PubMed - as supplied by publisher]



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