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
Depicting Conformational Ensembles of α-Synuclein by Single Molecule Force Spectroscopy and Native Mass Spectroscopy.
Roberta Corti,Claudia Adriana Marrano,Domenico Salerno,Stefania Brocca,Antonino Natalello,Carlo Santambrogio,Giuseppe Legname,Francesco Mantegazza,Rita Grandori,Cassina +9 more
TL;DR: This comparative analysis provides support to structural interpretation of charge-state distributions obtained by native mass spectrometry and helps, in turn, defining the conformational components detected by single molecule force spectroscopy.
Journal ArticleDOI
Mass spectrometric characterization of protein structures and protein complexes in condensed and gas phase.
Yelena Yefremova,Bright D. Danquah,Kwabena F.M. Opuni,Reham F. El-Kased,Cornelia Koy,Michael O. Glocker +5 more
TL;DR: Recent reports have shown that electrospray mass spectrometry provides direct access to six prime protein complex properties: stabilities, compositions, binding surfaces (epitopes), disassembly processes, stoichiometries, and thermodynamic parameters.
Journal ArticleDOI
Protein a resin lifetime study: Evaluation of protein a resin performance with a model-based approach in continuous capture
TL;DR: The degradation model can be extended to build effective cleaning strategies for continuous downstream processing, and demonstrates that the resin B exhibits the desirable performance, with higher reaction order indicating slower resin degradation, higher binding capacities, and increased sustenance of this binding capacity for extended duration.
Journal ArticleDOI
Mutations in Dynamic Structural Elements Alter the Kinetics and Fidelity of the Multifunctional Class II Lanthipeptide Synthetase, HalM2.
TL;DR: In this paper, a large conserved loop (HalM2 residues P349-P405) plays essential roles in defining the peptide binding site, facilitating efficient peptide dehydration, and guiding the order of thioether ring formation.
Book ChapterDOI
Noncovalent mass spectrometry for the characterization of antibody/antigen complexes.
Cédric Atmanene,Elsa Wagner-Rousset,Nathalie Corvaia,Alain Van Dorsselaer,Alain Beck,Sarah Sanglier-Cianférani +5 more
TL;DR: This chapter describes how recent noncovalent MS technologies are used to characterize immune complexes involving both murine and humanized mAb 6F4 directed against human JAM-A, a newly identified antigenic protein (Ag) over-expressed in tumor cells.
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