NMR Methods to Study Dynamic Allostery

PLoS Comput Biol. 2016 Mar 10;12(3):e1004620. doi: 10.1371/journal.pcbi.1004620. eCollection 2016 Mar.

Abstract

Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of allosteric mechanisms and increasing the proportion of the conformational ensemble that can be observed by experiment. Here, we present an overview of NMR spectroscopic methods for characterizing equilibrium fluctuations in free and bound states of allosteric proteins that have been most influential in the field. By combining NMR experimental approaches with molecular simulations, atomistic-level descriptions of the mechanisms by which allosteric phenomena take place are now within reach.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Regulation
  • Allosteric Site
  • Amino Acid Sequence
  • Enzyme Activation
  • Enzymes / chemistry*
  • Enzymes / ultrastructure*
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Chemical*
  • Molecular Dynamics Simulation*
  • Molecular Sequence Data
  • Protein Binding
  • Sequence Analysis, Protein

Substances

  • Enzymes

Grants and funding

This work is supported by funding from Austrian Science Fund, FWF, project number P22735. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.