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Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.

Artikel i vetenskaplig tidskrift
Författare Jennifer C Lee
Cecilia Engman
F Akif Tezcan
Harry B Gray
Jay R Winkler
Publicerad i Proceedings of the National Academy of Sciences of the United States of America
Volym 99
Nummer/häfte 23
Sidor 14778-82
ISSN 0027-8424
Publiceringsår 2002
Publicerad vid Institutionen för kemi
Sidor 14778-82
Språk en
Länkar dx.doi.org/10.1073/pnas.192574099
Ämnesord Amino Acids, analysis, Bacterial Proteins, chemistry, metabolism, Crystallography, X-Ray, methods, Cytochromes c1, chemistry, metabolism, Energy Transfer, Guanidine, Kinetics, Protein Conformation, Protein Folding, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, chemistry, metabolism, Spectrometry, Fluorescence
Ämneskategorier Kemi, Biokemi

Sammanfattning

We employed fluorescence energy-transfer probes to investigate the polypeptide dynamics accompanying cytochrome c' folding. Analysis of fluorescence energy-transfer kinetics from wild-type Trp-72 or Trp-32 in a crystallographically characterized (1.78 A) Q1A/F32W/W72F mutant shows that there is structural heterogeneity in denatured cytochrome c'. Even at guanidine hydrochloride concentrations well beyond the unfolding transition, a substantial fraction of the polypeptides ( approximately 50%) adopts compact conformations (tryptophan-to-heme distance, approximately 25 A) in both pseudo-wild-type (Q1A) and mutant proteins. A burst phase (< or =5 ms) is revealed when stopped flow-triggered refolding is probed by tryptophan intensity: measurements on the Q1A protein show that approximately 75% of the Trp-72 fluorescence (83% for Trp-32) is quenched within the mixing deadtime, suggesting that most of the polypeptides have collapsed.

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