Conformational dynamics in cytochrome c. A fragment exchange study
نویسندگان
چکیده
منابع مشابه
Conformational Transition of Cytochrome c
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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The fully oxidized complex of cytochrome c and cytochrome oxidase formed at low ionic strength was studied by resonance Raman spectroscopy. The spectra of the complex and of the individual components were compared over a wide frequency range using Soret band excitation. In both partners of the complex, structural changes occur in the heme groups and in their immediate protein environment. The s...
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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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Resonance energy transfer studies using a pyrene-labeled phospholipid derivative 1-palmitoyl-2-[10-(pyren-1-yl)decanoyl]-sn-glycero-3-phosphoglycerol (donor) and the heme (acceptor) of cytochrome c (cyt c) have indicated that ATP causes changes in the conformation of the lipid-bound protein (Rytömaa, M., Mustonen, P., and Kinnunen, P. K. J. (1992) J. Biol. Chem. 267, 22243-22248). Accordingly, ...
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Molecular Dynamics of PrP 180-193 has allowed us to investigate the stability of the α-helical conformation of the zwitterionic peptide (L1) and the neutralized (L2). In water, the helical structure of L1, is unstable; in L2, the α-helix breaks up in the middle at Gln186, and the two resulting connected helices are stable. The hydrophobic enviroment decreases the stability of the helical struct...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)30381-2