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Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein.

Abstract:

The refolding from denaturing conditions of a small four-helix bundle, the acyl-coenzyme A binding protein, has been investigated by utilizing an array of fast-reaction techniques. Stopped-flow tryptophan fluorescence for measuring the incorporation of aromatic residues into the protein core and far- and near-ultraviolet circular dichroism to measure the formation of secondary and tertiary structure, respectively, together with the formation of persistent structure measured by hydrogen exchan...

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Publication status:
Published

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Publisher copy:
10.1021/bi00021a037

Authors


Kragelund, BB More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Knudsen, J More by this author
Dobson, CM More by this author
Poulsen, FM More by this author
Journal:
Biochemistry
Volume:
34
Issue:
21
Pages:
7217-7224
Publication date:
1995-05-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:5c5adf79-6b67-4371-b556-f08c86be149b
Source identifiers:
59437
Local pid:
pubs:59437

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