Literature DB >> 11398477

Dynamics and thermodynamics of hyperthermophilic proteins by hydrogen exchange.

S W Englander1, R Hiller.   

Abstract

The naturally occurring hydrogen exchange of protein molecules can provide nonperturbing site-resolved measurements of protein stability and flexibility and changes therein. The measurement and understanding of these issues is especially pertinent to studies of thermophilic proteins. This chapter briefly reviews the considerations necessary for measuring hydrogen exchange and translating HX measurements into these detailed protein parameters.

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Year:  2001        PMID： 11398477     DOI： 10.1016/s0076-6879(01)34481-6

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN： 0076-6879            Impact factor:   1.600


  2 in total

1.  Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase.

Authors:  Zhao-Xun Liang; Thomas Lee; Katheryn A Resing; Natalie G Ahn; Judith P Klinman
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-21       Impact factor: 11.205

2.  High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome.

Authors:  Veronica C Casina; Wenbing Hu; Jian-Hua Mao; Rui-Nan Lu; Hayley A Hanby; Brandy Pickens; Zhong-Yuan Kan; Woon K Lim; Leland Mayne; Eric M Ostertag; Stephen Kacir; Don L Siegel; S Walter Englander; X Long Zheng
Journal:  Proc Natl Acad Sci U S A       Date:  2015-07-22       Impact factor: 11.205
  2 in total

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