Journal article icon

Journal article

Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.

Abstract:

The refolding of equine lysozyme from guanidinium chloride has been studied using hydrogen exchange pulse labelling in conjunction with NMR spectroscopy and stopped flow optical methods. The stopped flow optical experiments indicate that extensive hydrophobic collapse occurs rapidly after the initiation of refolding. Pulse labelling experiments monitoring nearly 50 sites within the protein have enabled the subsequent formation of native-like structure to be followed in considerable detail. Th...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1006/jmbi.1999.2741

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics, Atomic and Laser Physics
Role:
Author
Journal:
Journal of molecular biology
Volume:
289
Issue:
4
Pages:
1055-1073
Publication date:
1999-06-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:e649b2db-6fea-4c72-8bce-5bf464a7ed91
Source identifiers:
28694
Local pid:
pubs:28694

Terms of use


Metrics


Views and Downloads






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

TO TOP