Time-Resolved Fluorescence Resonance Energy Transfer Study Shows a Compact Denatured State of the B Domain of Protein A-Reference-Cited by-同舟云学术

Time-Resolved Fluorescence Resonance Energy Transfer Study Shows a Compact Denatured State of the B Domain of Protein A

Published:2009-03-25 Issue:15 Volume:48 Page:3468-3476
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Huang F.¹,Lerner E.¹,Sato S.¹,Amir D.¹,Haas E.¹,Fersht A. R.¹

Affiliation:

1. MRC Center for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom, and The Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat Gan, Israel 52900

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801890w

Reference43 articles.

1. The complete folding pathway of a protein from nanoseconds to microseconds

2. Protein Folding and Unfolding at Atomic Resolution

3. The protein folding ‘speed limit’

4. Ultrafast and downhill protein folding

5. Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump

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