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[Untitled]

Authors :
Ionescu Rm
Matthews Cr
Source :
Nature Structural Biology. 6:304-307
Publication Year :
1999
Publisher :
Springer Science and Business Media LLC, 1999.

Abstract

Refolding experiments of acylphosphatase in the presence of trifluoroethanol, a cosolvent known to increase the stability of α-helices, suggest that productive folding depends on optimizing the number of native-like interactions present in the unfolded state.

Subjects

Subjects :
Folding (chemistry)
Protein structure
Structural Biology
Computational chemistry
Chemistry
Genetics
Biophysics
Protein folding
Acylphosphatase
Biochemistry

Details

ISSN :
10728368
Volume :
6
Database :
OpenAIRE
Journal :
Nature Structural Biology
Accession number :
edsair.doi...........6b97dc1575202c576aef36e333147603
Full Text :
https://doi.org/10.1038/7534
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