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Following protein folding in real time using NMR spectroscopy.

Abstract:

The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative manner from an intermediate formed in the dead-time of the experiments. The kinetics of folding to the native state are closely similar to those observed by stopped-flow fluorescence and near-UV circular d...

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Publication status:
Published

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Publisher copy:
10.1038/nsb1095-865

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Journal:
Nature structural biology
Volume:
2
Issue:
10
Pages:
865-870
Publication date:
1995-10-01
DOI:
ISSN:
1072-8368
Source identifiers:
35625
Language:
English
Keywords:
Pubs id:
pubs:35625
UUID:
uuid:1db76a9a-f6ae-4f77-8407-ea6fd28a045a
Local pid:
pubs:35625
Deposit date:
2012-12-19

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