Journal ArticleDOI
Probing conformational changes in proteins by mass spectrometry
TLDR
The authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.Abstract:
Mass spectrometry has found wide application for the elucidation of the primary structures of proteins. However, with the exception of topographical studies of membrane-bound proteins, mass spectrometry has not previously been utilized to obtain information concerning in three-dimensional conformation of proteins. In the present communication, the authors describe the first use of mass spectrometry for probing conformational changes in proteins in a manner analogous to that employed in techniques like optical rotary dispersion, circular dichroism, and spectrophotometry.read more
Citations
More filters
Journal ArticleDOI
Probing the Nature of Noncovalent Interactions by Mass Spectrometry. A Study of Protein−CoA Ligand Binding and Assembly
Carol V. Robinson,Evonne W. Chung,Birthe B. Kragelund,Jens Knudsen,Robin T. Aplin,F.M. Poulsen,Christopher M. Dobson +6 more
TL;DR: Despite the very low dissociation constants of the acyl CoA ligand complexes high ratios of ligand-to-protein concentration in the electrospray solution were found to increase the proportion of intact complex observed in the spectrum.
Journal ArticleDOI
Anhydrous Protein Ions
TL;DR: Studies of biomolecular ions in the gas phase provide information about the nature of conformation in the absence of solvent; thus, the roles of intramolecular interactions and solvent can be discerned by comparison of similarities between gas and solutionphase structure.
Journal ArticleDOI
Structural stability from solution to the gas phase: native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment.
TL;DR: The native state of ubiquitin is preserved in the transition from solution to the desolvated state during the ESI process and survives for >100 ms in a 294 K solvent-free environment; the A state is charged more extensively than the native state during ESI and decays more rapidly following ESI.
Journal ArticleDOI
Hsp70 Chaperone Ligands Control Domain Association via an Allosteric Mechanism Mediated by the Interdomain Linker
Joanna F. Swain,Gizem Dinler,Renuka Sivendran,Diana L. Montgomery,Mathias Stotz,Lila M. Gierasch +5 more
TL;DR: It is shown that the interdomain linker controls ATPase activity by binding to a hydrophobic cleft between subdomains IA and IIA and results in destabilization of regions of the latter domain and consequent weaker substrate binding.
Journal ArticleDOI
Mechanism of Charging and Supercharging Molecules in Electrospray Ionization
TL;DR: It is demonstrated that in the absence of other factors, the surface tension of the electrospray droplet late in the desolvation process is a significant factor in determining the overall analyte charge.
Related Papers (5)
Electrospray ionization for mass spectrometry of large biomolecules
Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
Viswanatham Katta,Brian T. Chait +1 more