Folding Control and Unfolding Free Energy of Yeast Iso-1-cytochrome c Bound to Layered Zirconium Phosphate Materials Monitored by Surface Plasmon Resonance
نویسندگان
چکیده
منابع مشابه
Folding control and unfolding free energy of yeast iso-1-cytochrome c bound to layered zirconium phosphate materials monitored by surface plasmon resonance.
The free energy change (Delta G degrees ) for the unfolding of immobilized yeast iso-1-cytochrome c (Cyt c) at nanoassemblies was measured by surface plasmon resonance (SPR) spectroscopy. Data show that SPR is sensitive to protein conformational changes, and protein solid interface exerts a major influence on bound protein stability. First, Cyt c was self-assembled on the Au film via the single...
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 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 function makes it a primary ca...
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We attempted to evaluate the affinity of the anionic phospholipids to cytochrome c by means of surface plasmon resonance (SPR) technique and to correlate it with the cytochrome c active site alterations and peroxidase activity. Our experiments showed a strong interdependence between the phospholipid fatty acid saturation degree, the active site structure alterations and peroxidase activity of t...
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Fluorescence resonance energy transfer was used for measuring the distances between the following three sites of purified yeast cytochrome c oxidase: (a) a highly reactive sulfhydryl group on the mitochondrially made Subunit II; (b) endogenous heme a; (c) cytochrome c bound to the mitochondrially made Subunit III. Subunit II of purified cytochrome c oxidase was stoichiometrically and covalently...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2008
ISSN: 1520-6106,1520-5207
DOI: 10.1021/jp7121642