منابع مشابه
Snapshots of cytochrome c folding.
Dansyl-to-heme distance distributions [P(r)] during folding have been determined in five variants of Saccharomyces cerevisiae iso-1 ferricytochrome c (labeled at mutant Cys residues 4, 39, 50, 66, and 99) by analysis of fluorescence energy-transfer kinetics. Moment analysis of the P(r) distributions clearly indicates that cytochrome c refolding is not a simple two-state process. After 1 ms of f...
متن کاملStructural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c
Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...
متن کاملMapping the cytochrome C folding landscape.
The solution to the riddle of how a protein folds is encoded in the conformational energy landscape for the constituent polypeptide. Employing fluorescence energy transfer kinetics, we have mapped the S.cerevisiae iso-1 cytochrome c landscape by monitoring the distance between a C-terminal fluorophore and the heme during folding. Within 1 ms after denaturant dilution to native conditions, unfol...
متن کاملFast and Slow Folding in Cytochrome c
A number of puzzling characteristics appear repeatedly in protein folding studies. Some proteins fold in a fast two-state manner with no apparent intermediates while others fold much more slowly in a multistate way. Many proteins fold heterogeneously; within the same controlled experiment some fraction of the population reaches the native state rapidly and others more slowly. These contradictor...
متن کاملParallel pathways in cytochrome c(551) folding.
The folding of cytochrome c(551) from Pseudomonas aeruginosa was previously thought to follow a simple sequential mechanism, consistent with the lack of histidine residues, other than the native His16 heme ligand, that can give rise to mis-coordinated species. However, further kinetic analysis reveals complexities indicative of a folding mechanism involving parallel pathways. Double-jump interr...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2005
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0509076102