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http://hdl.handle.net/10397/89987
Title: | Protein dynamics revealed by hydrogen/deuterium exchange mass spectrometry : correlation between experiments and simulation | Authors: | Huang, L So, PK Yao, ZP |
Issue Date: | Jul-2019 | Source: | Rapid communications in mass spectrometry, July 2019, v. 33, no. S3, p. 83-89 | Abstract: | Hydrogen deuterium exchange mass spectrometry (HDX-MS) is a powerful technique for studying protein dynamics, which is an important factor governing protein functions. However, the process of hydrogen/deuterium exchange (HDX) of proteins is highly complex and the underlying mechanism has not yet been fully elucidated. Meanwhile, molecular dynamics (MD) simulation is a computational technique that can be used to elucidate HDX behaviour on proteins and facilitate interpretation of HDX-MS data. This article aims to summarize the current understandings on the mechanism of HDX and its correlation with MD simulation, to discuss the recent developments in the techniques of HDX-MS and MD simulation and to extend the perspectives of these two techniques in protein dynamics study. | Publisher: | John Wiley & Sons | Journal: | Rapid communications in mass spectrometry | ISSN: | 0951-4198 | EISSN: | 1097-0231 | DOI: | 10.1002/rcm.8307 | Rights: | © 2018 John Wiley & Sons, Ltd. This is the peer reviewed version of the following article: Huang, L, So, P-K, Yao, Z-P. Protein dynamics revealed by hydrogen/deuterium exchange mass spectrometry: Correlation between experiments and simulation. Rapid Commun Mass Spectrom. 2019; 33 (S3):83–89, which has been published in final form at https://doi.org/10.1002/rcm.8307. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. |
Appears in Collections: | Journal/Magazine Article |
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