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Default Relaxation dispersion NMR spectroscopy for the study of protein allostery.

Relaxation dispersion NMR spectroscopy for the study of protein allostery.

Related Articles Relaxation dispersion NMR spectroscopy for the study of protein allostery.

Biophys Rev. 2015 Jun;7(2):191-200

Authors: Farber PJ, Mittermaier A

Abstract
Allosteric transmission of information between distant sites in biological macromolecules often involves collective transitions between active and inactive conformations. Nuclear magnetic resonance (NMR) spectroscopy can yield detailed information on these dynamics. In particular, relaxation dispersion techniques provide structural, dynamic, and mechanistic information on conformational transitions occurring on the millisecond to microsecond timescales. In this review, we provide an overview of the theory and analysis of Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments and briefly describe their application to the study of allosteric dynamics in the homeodomain from the PBX transcription factor (PBX-HD). CPMG NMR data show that local folding (helix/coil) transitions in one part of PBX-HD help to communicate information between two distant binding sites. Furthermore, the combination of CPMG and other spin relaxation data show that this region can also undergo local misfolding, reminiscent of conformational ensemble models of allostery.


PMID: 28510170 [PubMed]



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