In-cell solid-state NMR as a tool to study proteins in large complexes

Chembiochem. 2012 Mar 5;13(4):534-7. doi: 10.1002/cbic.201100721. Epub 2012 Feb 1.

Abstract

A major limitation of solution NMR is molecular tumbling, which is often too slow for detection. Here we demonstrate that solid-state NMR spectroscopy in combination with flash freezing of cells can be used to detect proteins in the cellular environment and provides information on backbone chemical shifts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / chemistry
  • Escherichia coli / cytology
  • Humans
  • Molecular Weight
  • Nuclear Magnetic Resonance, Biomolecular*
  • Tacrolimus Binding Protein 1A / chemistry*
  • Tacrolimus Binding Protein 1A / metabolism
  • Thioredoxins / chemistry*
  • Thioredoxins / metabolism

Substances

  • Thioredoxins
  • Tacrolimus Binding Protein 1A