structural characteristics of stable folding intermediates of yeast iso-1-cytochrome-c
نویسندگان
چکیده
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 function makes it a primary candidate for studying molecular evolution, phylogenetics and sequence conservation. when amino acid sequences of mammalian cyts-c are aligned with the sequence of the yeast iso-1-cyt-c (y-cyt-c), it is observed that the yeast protein not only contains five extra n-terminal residues but it has only 60% sequence homology, e.g., with the horse heart cyt-c. structural and thermodynamic studies suggest that there are four states in the folding equation of y-cyt-c, i.e., denatured (d) state ↔ pre molten globule (pmg) state ↔ molten globule (mg) state ↔ n (native) state. this review summarises findings of structural and thermodynamic characteristics of these thermodynamic states of y-cyt-c and its folding mechanism.
منابع مشابه
Structural 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...
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عنوان ژورنال:
biomacromolecular journalناشر: iran society of biophysical chemistry (isobc)
ISSN
دوره 1
شماره 1 2015
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