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- W2334669195 abstract "Ovalbumin is a 45 kDa egg-white glycoprotein which belongs to the class of serpin superfamily. We have studied the structural properties of both native and partially unfolded molten-globule forms of ovalbumin using a diverse array of spectroscopic tools. Time-resolved fluorescence measurements provided important structural and dynamical insights into the native and molten-globule states. Fluorescence anisotropy decay analysis indicated that there is a conformational swelling from the native to the molten-globule form of ovalbumin. We have also carried out red-edge excitation shift measurements to probe the dipolar relaxation dynamics around the intrinsic tryptophan residues. Additionally, stopped-flow fluorescence experiments revealed that the conformational transition from the native to the molten-globule form proceeds in a stepwise manner involving a burst-phase with a submillisecond conformational change followed by biphasic slower conformational reorganizations on the millisecond time scale leading to the final molten-globule state." @default.
- W2334669195 created "2016-06-24" @default.
- W2334669195 creator A5004633083 @default.
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- W2334669195 date "2011-12-12" @default.
- W2334669195 modified "2023-10-16" @default.
- W2334669195 title "Structural and Dynamical Insights into the Molten-Globule Form of Ovalbumin" @default.
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- W2334669195 doi "https://doi.org/10.1021/jp208416d" @default.
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