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Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature.

Abstract:

We have used low temperatures (down to -20°C) and high pressures (up to 2000 bar) to populate low-lying excited state conformers of hen lysozyme, and have analyzed their structures site-specifically using (15)N/(1)H two-dimensional HSQC NMR spectroscopy. The resonances of a number of residues were found to be selectively broadened, as the temperature was lowered at a pressure of 2000 bar. The resulting disappearance of cross-peaks includes those of residues in the β-domain of the protein and ...

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Publication status:
Published

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Publisher copy:
10.1016/j.bpc.2011.01.009

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Biophysical chemistry
Volume:
156
Issue:
1
Pages:
24-30
Publication date:
2011-06-05
DOI:
EISSN:
1873-4200
ISSN:
0301-4622
URN:
uuid:580cbcb0-2302-49d1-a481-e37ac934eb48
Source identifiers:
159334
Local pid:
pubs:159334

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