Journal ArticleDOI
Hydrogen exchange mass spectrometry for the analysis of protein dynamics.
Thomas E. Wales,John R. Engen +1 more
TLDR
The general principles of the hydrogen exchange coupled to mass spectrometry method are summarized, the latest variations on the experimental protocol that probe different types of protein movements are discussed, and other recent work and improvements in the field are reviewed.Abstract:
Hydrogen exchange coupled to mass spectrometry (MS) has become a valuable analytical tool for the study of protein dynamics. By combining information about protein dynamics with more classical functional data, a more thorough understanding of protein function can be obtained. In many cases, protein dynamics are directly related to specific protein functions such as conformational changes during enzyme activation or protein movements during binding. The method is made possible because labile backbone hydrogens in a protein will exchange with deuterium atoms when the protein is placed in a D2O solution. The subsequent increase in protein mass over time is measured with high-resolution MS. The location of the deuterium incorporation is determined by monitoring deuterium incorporation in peptic fragments that are produced after the labeling reaction. In this review, we will summarize the general principles of the method, discuss the latest variations on the experimental protocol that probe different types of protein movements, and review other recent work and improvements in the field. © 2005 Wiley Periodicals, Inc.read more
Citations
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Journal ArticleDOI
Targeting Bcr–Abl by combining allosteric with ATP-binding-site inhibitors
Jianming Zhang,Francisco Adrian,Wolfgang Jahnke,Sandra W. Cowan-Jacob,Allen G. Li,Roxana E. Iacob,Taebo Sim,Taebo Sim,John T. Powers,John T. Powers,Christine Dierks,Fangxian Sun,Gui Rong Guo,Qiang Ding,Barun Okram,Yongmun Choi,Amy Wojciechowski,Xianming Deng,Guoxun Liu,Gabriele Fendrich,André Strauss,Navratna Vajpai,Stephan Grzesiek,Tove Tuntland,Yi Liu,Badry Bursulaya,Mohammad Azam,Mohammad Azam,Paul W. Manley,John R. Engen,George Q. Daley,George Q. Daley,Markus Warmuth,Nathanael S. Gray +33 more
TL;DR: The results show that therapeutically relevant inhibition of Bcr–Abl activity can be achieved with inhibitors that bind to the myristate-binding site and that combining allosteric and ATP-competitive inhibitors can overcome resistance to either agent alone.
Journal ArticleDOI
Electrospray Ionization Mass Spectrometry: A Technique to Access the Information beyond the Molecular Weight of the Analyte
TL;DR: The present review has described the development of Electrospray Ionization mass spectrometry (ESI-MS) during the last 25 years in the study of various properties of different types of biological molecules.
Journal ArticleDOI
An NMR perspective on enzyme dynamics.
TL;DR: Binding of substrate can lead to the repositioning of catalytic groups, effectively bridging the dynamic processes of substrate binding and catalysis.
Journal ArticleDOI
Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.
Glenn R. Masson,John E. Burke,Natalie G. Ahn,Ganesh S. Anand,Christoph H. Borchers,Sébastien Brier,George M. Bou-Assaf,John R. Engen,S. Walter Englander,Johan H. Faber,Rachel Garlish,Patrick R. Griffin,Michael L. Gross,Miklos Guttman,Yoshitomo Hamuro,Albert J. R. Heck,Damian Houde,Roxana E. Iacob,Thomas J. D. Jørgensen,Igor A. Kaltashov,Judith P. Klinman,Lars Konermann,Petr Man,Leland Mayne,Bruce D. Pascal,Dana Reichmann,Mark Skehel,Joost Snijder,Timothy S. Strutzenberg,Eric S. Underbakke,Cornelia Wagner,Thomas E. Wales,Benjamin T. Walters,David D. Weis,Derek J. Wilson,Patrick L. Wintrode,Zhongqi Zhang,Jie Zheng,David C. Schriemer,Kasper D. Rand +39 more
TL;DR: Recommendations arising from community discussions emerging out of the first International Conference on Hydrogen-Exchange Mass Spectrometry (IC-HDX; 2017) are provided, meant to represent both a consensus viewpoint and an opportunity to stimulate further additions and refinements as the field advances.
Journal ArticleDOI
Hydrogen exchange and mass spectrometry: A historical perspective.
TL;DR: The effort to measure protein hydrogen exchange behavior, understand the underlying chemistry and structural physics of hydrogen exchange processes, and use this information to learn about protein properties and function has continued for 50 years.
References
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Journal ArticleDOI
Functional organization of the yeast proteome by systematic analysis of protein complexes
Anne-Claude Gavin,Markus Bösche,Roland Krause,Paola Grandi,Martina Marzioch,Andreas Bauer,Jörg Schultz,Jens Rick,Anne-Marie Michon,Cristina-Maria Cruciat,Marita Remor,Christian Höfert,Malgorzata Schelder,Miro Brajenovic,Heinz Ruffner,Alejandro Merino,Karin Klein,Manuela Hudak,David Dickson,Tatjana Rudi,Volker Gnau,Angela Bauch,Sonja Bastuck,Bettina Huhse,Christina Leutwein,Marie-Anne Heurtier,Richard R. Copley,Angela Edelmann,Erich Querfurth,Vladimir Rybin,Gerard Drewes,Manfred Raida,Tewis Bouwmeester,Peer Bork,Bertrand Séraphin,Bernhard Kuster,Gitte Neubauer,Giulio Superti-Furga +37 more
TL;DR: The analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions, which contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.
Journal ArticleDOI
Proposal for a common nomenclature for sequence ions in mass spectra of peptides.
Roepstorff P,Fohlman J +1 more
Journal ArticleDOI
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
TL;DR: Peptide sequence analysis using a combination of gas-phase ion/ion chemistry and tandem mass spectrometry (MS/MS) is demonstrated and automated acquisition of high-quality, single-scan electron transfer dissociation MS/MS spectra of phosphopeptides separated by nanoflow HPLC is described.
Journal ArticleDOI
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
TL;DR: In this article, it was shown that one or more charges on such protein cations can be neutralized with low energy electrons to cause specific cleavage of the amine bond to form c, z products, in contrast to the amide cleavage b, y products formed by collisionally activated dissociation (CAD),8 infrared multiphoton (IRMPD)9 and UV10 photodissociation, 70 eV electron impact excitation,11 and SID.
Journal ArticleDOI
Primary Structure Effects on Peptide Group Hydrogen Exchange
TL;DR: The results provide the information necessary to evaluate measured protein NH to ND exchange rates by comparing them with rates to be expected for the same amino acid sequence is unstructured aligo‐ and polypeptides.
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