Conformational dynamics of cytochrome c: Correlation to hydrogen exchange
نویسندگان
چکیده
منابع مشابه
Cytochrome c folding pathway: kinetic native-state hydrogen exchange.
Native-state hydrogen exchange experiments under EX1 conditions can distinguish partially unfolded intermediates by their formation rates and identify the amide hydrogens exposed and protected in each. Results obtained define a cytochrome c intermediate seen only poorly before and place it early on the major unfolding pathway. Four distinct unfolding steps are found to be kinetically ordered in...
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Conformational transitions of oxidized and reduced cytochrome c at various solvent conditions are summarized. Sorbitol stabilizes and NaCl destabilizes native cytochrome c structure against the acid denaturation. In the process of heating, NaCl more strongly stabilizes molten globular cytochtome c state than sorbitol in secondary structure region, but in heme region, sorbitol is stronger stabil...
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Interactions of cytochrome c (cyt c) with cardiolipin (CL) are important for both electron transfer and apoptotic functions of this protein. A sluggish peroxidase in its native state, when bound to CL, cyt c catalyzes CL peroxidation, which contributes to the protein apoptotic release. The heterogeneous CL-bound cyt c ensemble is difficult to characterize with traditional structural methods and...
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Rational design of optogenetic tools is inherently linked to the understanding of photoreceptor function. Structural analysis of elements involved in signal integration in individual sensor domains provides an initial idea of their mode of operation, but understanding how local structural rearrangements eventually affect signal transmission to output domains requires inclusion of the effector r...
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Backbone dynamics of the camphor monoxygenase cytochrome P450(cam) (CYP101) as a function of oxidation/ligation state of the heme iron were investigated via hydrogen/deuterium exchange (H/D exchange) as monitored by mass spectrometry. Main chain amide NH hydrogens can exchange readily with solvent and the rate of this exchange depends upon, among other things, dynamic fluctuations in local stru...
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ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Genetics
سال: 1999
ISSN: 0887-3585,1097-0134
DOI: 10.1002/(sici)1097-0134(19990801)36:2<175::aid-prot4>3.3.co;2-i