Journal article icon

Journal article

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...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/nsb1095-865

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
Expand authors...
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

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP