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Journal article

The origin of the alpha-domain intermediate in the folding of hen lysozyme.

Abstract:

Stopped-flow fluorescence and circular dichroism spectroscopy have been used in conjunction with quenched-flow hydrogen exchange labelling, monitored by electrospray ionization mass spectrometry, to compare the refolding kinetics of hen egg-white lysozyme at 20 degrees C and 50 degrees C. At 50 degrees C there is clear evidence for distinct fast and slow refolding populations, as observed at 20 degrees C, although folding occurs significantly more rapidly. The folding process is, however, sub...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1998.1657

Authors


Matagne, A More by this author
Radford, SE More by this author
Robinson, CV More by this author
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Journal:
Journal of molecular biology
Volume:
277
Issue:
5
Pages:
997-1005
Publication date:
1998-04-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:a56e6836-3fe1-4d58-959c-7952f641073d
Source identifiers:
59353
Local pid:
pubs:59353

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