Protein dynamics in living cells studied by in-cell NMR spectroscopy

FEBS Lett. 2013 Apr 17;587(8):1008-11. doi: 10.1016/j.febslet.2012.12.023. Epub 2013 Jan 11.

Abstract

Most proteins function in cells where protein concentrations can reach 400 g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been characterized by in-cell NMR, and then discuss the remaining challenges and future directions.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Intracellular Space / metabolism
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Dynamics Simulation*
  • Protein Binding
  • Protein Conformation
  • Protein Interaction Mapping / methods*
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Proteins