Transition in cytochrome c conformation observed by single-molecule fluorometry
نویسندگان
چکیده
منابع مشابه
Cytochrome c conformations resolved by the photon counting histogram: watching the alkaline transition with single-molecule sensitivity.
We apply the photon counting histogram (PCH) model, a fluorescence technique with single-molecule sensitivity, to study pH-induced conformational changes of cytochrome c. PCH is able to distinguish different protein conformations based on the brightness of a fluorophore sensitive to its local environment. We label cytochrome c through its single free cysteine with tetramethylrhodamine-5-maleimi...
متن کاملRelaxation of a single DNA molecule observed by optical microscopy.
Single molecules of DNA, visualized in video fluorescence microscopy, were stretched to full extension in a flow, and their relaxation was measured when the flow stopped. The molecules, attached by one end to a 1-micrometer bead, were manipulated in an aqueous solution with optical tweezers. Inverse Laplace transformations of the relaxation data yielded spectra of decaying exponentials with dis...
متن کاملUnfolding dynamics of cytochrome c revealed by single-molecule and ensemble-averaged spectroscopy.
Denaturant-induced conformational change of yeast iso-1-cytochrome c (Cytc) has been comprehensively investigated in the single-molecule and bulk phases. By fluorescence-quenching experiments with dye-labelled heme-protein (Alexa 488-labelled Cytc, Cytc-A488), we clearly show that the fluorescence quenching observed from folded Cytc-A488 is due mainly to photoinduced electron transfer (PET) bet...
متن کاملConformational 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...
متن کاملAllosteric effects on substrate dissociation from cytochrome P450 3A4 in nanodiscs observed by ensemble and single-molecule fluorescence spectroscopy.
Cytochrome P450 (CYP) 3A4 is a major human drug-metabolizing enzyme and displays pharmacologically relevant allosteric kinetics caused by multiple substrate and/or effector binding. Here, in the first single-molecule (SM) fluorescence studies of CYPs, we use total internal reflection fluorescence microscopy to measure residence times of the fluorescent dye Nile Red in CYP3A4 incorporated in sur...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s165_1