Exploring the Cytochrome c Folding Mechanism
نویسندگان
چکیده
منابع مشابه
Cytochrome c Folding and Unfolding: A Biphasic Mechanism
How an unstructured polypeptide chain condenses to form a biologically functional protein, the protein folding problem, has attracted great interest in recent years.1 In many proteins, this spontaneous self-organization reaction occurs with high efficiency and fidelity despite a marginal thermodynamic driving force.2 A full knowledge of the free energy landscape associated with all possible con...
متن کاملSnapshots 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 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 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 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m303990200