Published November 2007
| Accepted Version
Journal Article
Open
Probing the cytochrome c′ folding landscape
Abstract
The folding kinetics of R. palustris cytochrome c′ (cyt c′) have been monitored by heme absorption and native Trp72 fluorescence at pH 5. The Trp72 fluorescence burst signal suggests early compaction of the polypeptide ensemble. Analysis of heme transient absorption spectra reveals deviations from two-state behavior, including a prominent slow phase that is accelerated by the prolyl isomerase cyclophilin. A nonnative proline configuration (Pro21) likely interferes with the formation of the helical bundle surrounding the heme.
Additional Information
© 2007 Elsevier Inc. Received 3 April 2007; received in revised form 31 May 2007; accepted 1 June 2007; Available online 21 June 2007. We thank Professor Amy H. Andreotti for providing human cyclophilin plasmid and Binghai Ling for screening bacterial colonies for cyt c′ expression. Our work was supported by NIH (GM068461 to J.R.W.), the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.), the Caltech SURF program (Mr. and Mrs. Samuel Krown fellowship to Z.Z.), and the Japan Society for the Promotion of Science for Young Scientists (Research Fellowship to T.K.).Attached Files
Accepted Version - nihms33827.pdf
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Additional details
- PMCID
- PMC2110879
- Eprint ID
- 77845
- Resolver ID
- CaltechAUTHORS:20170531-085209969
- GM068461
- NIH
- Ellison Medical Foundation
- Caltech Summer Undergraduate Research Fellowship (SURF)
- Japan Society for the Promotion of Science (JSPS)
- Created
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2017-05-31Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field