From molecular chaperones to membrane motors: through the lens of a mass spectrometrist

Biochem Soc Trans. 2017 Feb 8;45(1):251-260. doi: 10.1042/BST20160395.

Abstract

Twenty-five years ago, we obtained our first mass spectra of molecular chaperones in complex with protein ligands and entered a new field of gas-phase structural biology. It is perhaps now time to pause and reflect, and to ask how many of our initial structure predictions and models derived from mass spectrometry (MS) datasets were correct. With recent advances in structure determination, many of the most challenging complexes that we studied over the years have become tractable by other structural biology approaches enabling such comparisons to be made. Moreover, in the light of powerful new electron microscopy methods, what role is there now for MS? In considering these questions, I will give my personal view on progress and problems as well as my predictions for future directions.

Keywords: ion mobility; mass spectrometry; membrane proteins; molecular chaperones.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Cell Membrane / metabolism*
  • Chaperonin 60 / chemistry
  • Chaperonin 60 / metabolism
  • Mass Spectrometry / methods*
  • Mass Spectrometry / trends
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Microscopy, Electron
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Molecular Motor Proteins / metabolism*
  • Protein Conformation
  • Ribosomes / chemistry
  • Ribosomes / metabolism
  • Thermus thermophilus / metabolism
  • Time Factors

Substances

  • Bacterial Proteins
  • Chaperonin 60
  • Membrane Proteins
  • Molecular Chaperones
  • Molecular Motor Proteins
  • Adenosine Triphosphatases