- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/nsb1095-865
-
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- Journal:
- Nature structural biology
- Volume:
- 2
- Issue:
- 10
- Pages:
- 865-870
- Publication date:
- 1995-10-05
- DOI:
- ISSN:
-
1072-8368
- URN:
-
uuid:1db76a9a-f6ae-4f77-8407-ea6fd28a045a
- Source identifiers:
-
35625
- Local pid:
- pubs:35625
- Language:
- English
- Keywords:
- Copyright date:
- 1995
Journal article
Following protein folding in real time using NMR spectroscopy.
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