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Molten globules cytochrome

The studies of RNase Aand cytochrome c (Qi etal., 1998 Sosnick etal., 1997) show that caution is required in interpreting burst phenomena in protein folding. However, they do not require a reinterpretation of the cases in which the molten globule character of the burst-intermediate has been established (Arai and Kuwajima, 2000 Chamberlain and Marqusee, 2000). [Pg.251]

Tremain SM, Kostic NM. Molten-globule and other conformational forms of zinc cytochrome c. Effect of partial and complete unfolding of the protein on its electron-transfer reactivity. Inorg Chem 2002 41 3291-301. [Pg.223]

Lyubovitsky, J.G., Gray, H.B., Winkler, J.R. Structural features of the cytochrome c molten globule revealed by fluorescence energy transfer kinetics, J. Am. Chem. Soc. 2002,124,14840-1. [Pg.30]

Structural Eeatures of the Cytochrome c Molten Globule Revealed by Eluorescence Energy Transfer Kinetics. [Pg.420]

An enhancement of the for cardiolipin phosphates through direct contact of the haem group in cytochrome c, a peripherally bovmd protein, suggests that this protein undergoes considerable conformational distortions (molten globule) when at the bilayer surface, on the 10 s time-scale, a feature of peripherally bound proteins which may be general. [Pg.129]

Cytochrome bs62 is a heme-containing, four-helix bundle, whose apo form has been proposed to be a molten globule. There is a relatively large amount of experimental information about the solution structure of apocytochrome b562, from a variety of experimental studies. The observed molten characteristics were not clearly related to a simple loss in secondary structure. ... [Pg.2215]


See other pages where Molten globules cytochrome is mentioned: [Pg.246]    [Pg.246]    [Pg.246]    [Pg.248]    [Pg.14]    [Pg.204]    [Pg.204]    [Pg.22]    [Pg.124]    [Pg.125]    [Pg.151]   
See also in sourсe #XX -- [ Pg.223 , Pg.224 ]




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