- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1110/ps.9.8.1466
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 2000
Journal article
Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization.
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