Literature DB >> 16132820

Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.

Anja Böckmann1, Michel Juy, Emmanuel Bettler, Lyndon Emsley, Anne Galinier, François Penin, Anne Lesage.   

Abstract

We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for site-specific assignments of carbons nearby labile protein protons. We compare the proton T2' selective scheme to frequency selective water observation in deuterated proteins, and discuss the impacts of deuteration on 13C linewidths in Crh. We observe that in micro-crystalline proteins, solvent accessible hydroxyl and amino protons show comparable exchange rates with water protons as for proteins in solution, and that structural constraints, such as hydrogen bonding or solvent accessibility, more significantly reduce exchange rates.

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Year:  2005        PMID： 16132820     DOI： 10.1007/s10858-005-8073-y

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


  40 in total

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