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Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization.

Abstract:

The folding kinetics of human common-type acylphosphatase (cAcP) from its urea- and TFE-denatured states have been determined by stopped-flow fluorescence techniques. The refolding reaction from the highly unfolded state formed in urea is characterized by double exponential behavior that includes a slow phase associated with isomerism of the Gly53-Pro54 peptide bond. However, this slow phase is absent when refolding is initiated by dilution of the highly a-helical denatured state formed in th...

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Publication status:
Published

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Publisher copy:
10.1110/ps.9.8.1466

Authors


Pertinhez, TA More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Protein science : a publication of the Protein Society
Volume:
9
Issue:
8
Pages:
1466-1473
Publication date:
2000-08-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:673a8183-6b8e-4bd2-89cc-1ec02c50652f
Source identifiers:
31750
Local pid:
pubs:31750

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