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
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Journal ArticleDOI
Total Chemical Synthesis of Biologically Active Vascular Endothelial Growth Factor
TL;DR: The covalent structure of the synthetic VEGF was confirmed by precise mass measurement, and the three-dimensional structure ofThe synthetic protein was determined by high-resolution X-ray crystallography.
Journal ArticleDOI
Direct characterization of enzyme-substrate complexes by using electrosonic spray ionization mass spectrometry.
TL;DR: In the course of the study, it is shown that noncovalent solution interactions between the enzyme imidazole-3-glycerol phosphate synthase (IGP synthase) and the substrate/inhibitor are preserved in the gas-phase ions.
Journal ArticleDOI
Influence of Dimehylsulfoxide on Protein–Ligand Binding Affinities
Dragana Cubrilovic,Renato Zenobi +1 more
TL;DR: The effects of DMSO on different noncovalent protein-ligand complexes, in particular in terms of the binding affinities, are investigated using nanoESI-MS to emphasize the importance of effects ofDMSO as a co-solvent for quantification of protein- ligand binding strengths in the early stages of drug discovery.
Journal ArticleDOI
Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments: implications for ubiquitin folding.
TL;DR: The results of this work suggest that the occurrence of transient intermediates may be more widespread than commonly thought, especially in cases where a cursory analysis indicates two-state behavior.
Journal ArticleDOI
Correlation between the Charge of Proteins in Solution and in the Gas Phase Investigated by Protein Charge Ladders, Capillary Electrophoresis, and Electrospray Ionization Mass Spectrometry
Jeffrey D. Carbeck,Joanne C. Severs,Jinming Gao,Qinyuan Wu,Richard D. Smith,George M. Whitesides +5 more
TL;DR: In this paper, the authors analyzed the charge ladders of bovine carbonic anhydrase II, hen egg-white lysozyme, and bovinea pancreatic trypsin inhibitor, prepared by partial acetylation of primary amino groups on the surface of the protein, using capillary electrophoresis (CE) and online electrospray ionization mass spectrometry (ESIMS).
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