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Effects of macromol...
Effects of macromolecular crowding on burst phase kinetics of cytochrome c folding
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- Chen, Eefei (författare)
- Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States
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- Christiansen, Alexander, 1982- (författare)
- Umeå universitet,Kemiska institutionen
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- Wang, Qian (författare)
- Department of Physics, University of Houston, Houston, Texas 77204, United States
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- Cheung, Margaret S (författare)
- Department of Physics, University of Houston, Houston, Texas 77204, United States
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- Kliger, David S (författare)
- Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States
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- Wittung-Stafshede, Pernilla, 1968- (författare)
- Umeå universitet,Kemiska institutionen,Biological Chemistry
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(creator_code:org_t)
- 2012-11-26
- 2012
- Engelska.
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 51:49, s. 9836-9845
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Excluded volume and viscosity effects of crowding agents that mimic crowded conditions in vivo on "classical" burst phase folding kinetics of cytochrome c are assessed in vitro. Upon electron transfer-triggered folding of reduced cytochrome c, far-UV time-resolved circular dichroism (TRCD) is used to monitor folding under different conditions. Earlier work has shown that folding of reduced cytochrome c from the guanidinium hydrochloride-induced unfolded ensemble in dilute phosphate buffer involves kinetic partitioning: one fraction of molecules folds rapidly, on a time scale identical to that of reduction, while the remaining population folds more slowly. In the presence of 220 mg/mL dextran 70, a synthetic macromolecular crowding agent that occupies space but does not interact with proteins, the population of the fast folding step for cytochrome c is greatly reduced. Increasing the viscosity with sucrose to the same microviscosity exhibited by the dextran solution showed no significant decrease in the amplitude of the fast-folding phase of cytochrome c. Experiments show that the unfolded-state heme ligation remains bis-His in the presence of dextran 70, but coarse-grained simulations suggest that the unfolded-state ensemble becomes more compact in the presence of crowders. We conclude that excluded volume effects alter unfolded cytochrome c such that access to fast-folding conformations is reduced.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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