Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions. Academic Article uri icon

abstract

  • The structures and conformational dynamics of proteins, protein complexes, and their noncovalent interactions with other molecules are controlled specifically by the Gibbs free energy (entropy and enthalpy) of the system. For some organisms, temperature is highly regulated, but the majority of biophysical studies are carried out at room, nonphysiological temperature. In this review, we describe variable-temperature electrospray ionization (vT-ESI) mass spectrometry (MS)-based studies with unparalleled sensitivity, dynamic range, and selectivity for studies of both cold- and heat-induced chemical processes. Such studies provide direct determinations of stabilities, reactivities, and thermodynamic measurements for native and non-native structures of proteins and protein complexes and for protein-ligand interactions. Highlighted in this review are vT-ESI-MS studies that reveal 40 different conformers of chymotrypsin inhibitor 2, a classic two-state (native unfolded) unfolder, and thermochemistry for a model membrane protein system binding lipid and its regulatory protein.

published proceedings

  • Annu Rev Biophys

altmetric score

  • 1.25

author list (cited authors)

  • Laganowsky, A., Clemmer, D. E., & Russell, D. H.

citation count

  • 14

complete list of authors

  • Laganowsky, Arthur||Clemmer, David E||Russell, David H

publication date

  • May 2022