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Measuring the refolding of [beta]-sheets with different turn sequences on a nanosecond time scale
- Source :
- Proceedings of the National Academy of Sciences of the United States. May 11, 2004, Vol. 101 Issue 19, p7305, 6 p.
- Publication Year :
- 2004
-
Abstract
- Whether turns play an active or passive role in protein folding remains a controversial issue at this juncture. Here we use a photolabile cage strategy in combination with laser-flash photolysis and photoacoustic calorimetry to study the effects of different turns on the kinetics of [beta]-hairpin refolding on a nanosecond time scale. This strategy opens up a temporal window to allow the observation of early kinetic events in the protein refolding process at ambient temperature and pH without interference from any denaturants. Our results provide direct evidence demonstrating that even a one-residue difference in the turn region can change the refolding kinetics of a peptide. This observation suggests an active role for turn formation in directing protein folding.
- Subjects :
- Proteins -- Research
Science and technology
Subjects
Details
- Language :
- English
- ISSN :
- 00278424
- Volume :
- 101
- Issue :
- 19
- Database :
- Gale General OneFile
- Journal :
- Proceedings of the National Academy of Sciences of the United States
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.117668556