Relaxation dispersion NMR spectroscopy for the study of protein allostery

Biophysics Reviews
Patrick Farber, Anthony K Mittermaier

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.

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Citations

Nov 12, 2017·Journal of Biomolecular NMR·Harold W Mackenzie, D Flemming Hansen
Mar 11, 2016·PLoS Computational Biology·Sarina GrutschMartin Tollinger
Apr 15, 2020·International Journal of Biological Macromolecules·Nidhi JoshiKrishna Mohan Poluri
Aug 30, 2017·Biochimica Et Biophysica Acta. General Subjects·Teppei IkeyaChristian Griesinger
Feb 23, 2020·Journal of Molecular Biology·Jens DanielssonEllinor Haglund
Apr 4, 2021·International Journal of Molecular Sciences·Kwang-Im OhJoon-Hwa Lee
May 2, 2021·Scientific Reports·Riley B PeacockElizabeth A Komives
Aug 21, 2018·Journal of the American Chemical Society·Srinivasa R PenumutchuBlanton S Tolbert
Dec 11, 2020·The Journal of Physical Chemistry. B·Khandekar Jishan Bari, Shrikant Sharma

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