structural characteristics of stable folding intermediates of yeast iso-1-cytochrome-c

نویسندگان

faizan ahmad

sobia zaidi

md imtaiyaz hassan

asimul islam

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.

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Structural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c

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عنوان ژورنال:
biomacromolecular journal

ناشر: iran society of biophysical chemistry (isobc)

ISSN

دوره 1

شماره 1 2015

کلمات کلیدی
[ ' c y t o c h r o m e ' , ' c ' , ' f o l d i n g i n t e r m e d i a t e s ' , ' y e a s t i s o ' , 1 , ' c y t o c h r o m e ' , ' c ' , ' p r e ' , ' m o l t e n g l o b u l e ' , ' m o l t e n g l o b u l e ' ]

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