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
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Journal ArticleDOI
Vapor Treatment of Electrospray Droplets: Evidence for the Folding of Initially Denatured Proteins on the Sub-Millisecond Time-Scale
TL;DR: The exposure of electrospray droplets generated from either highly acidic or highly basic solutions to basic or acidic vapors, respectively, admitted into the counter-current drying gas, has been shown to lead to significant changes in the observed charge state distributions of proteins.
Journal ArticleDOI
Monitoring protein refolding induced by disulfide formation using capillary isoelectric focusing-electrospray ionization mass spectrometry.
TL;DR: On-line capillary isoelectric focusing-electrospray ionization mass spectrometry (CIEF-ESIMS) is demonstrated for kinetic studies of disulfide bond-induced protein refolding and the determination of conformational heterogeneity among groups of refolding intermediates.
Journal ArticleDOI
Nested Arg-specific bifunctional crosslinkers for MS-based structural analysis of proteins and protein assemblies.
TL;DR: Nested Arg-specific bifunctional crosslinkers are developed to obtain complementary information to typical Cys- and Lys-specific reagents available on the market and showed excellent correlation with the solvent accessibility and structural context of susceptible residues, and highlighted the significance of possible dynamic effects in determining the outcome of crosslinking reactions.
Journal ArticleDOI
Effects of Cations on Protein and Peptide Charging in Electrospray Ionization from Aqueous Solutions
TL;DR: The average protein and peptide charge with NH4+ is nearly the same as that with Rb+ and K+, cations with similar GSFE and ionic radii, indicating that proton transfer from NH4 + to proteins plays an insignificant role in the extent of protein charging in native mass spectrometry.
Journal ArticleDOI
Characterization of mutant xylanases using fourier transform ion cyclotron resonance mass spectrometry: stabilizing contributions of disulfide bridges and N-terminal extensions.
TL;DR: Residual activity measurements verified that the enzymes inactivated at significantly lower temperatures than expected on the basis of the apparent T(m) values, strongly suggesting that the inactivation takes place through minor conformational change other than observed by H/D exchange.
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