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Showing 1 to 5 of 5 for “"Apomyoglobin"”.
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Millisecond and Submillisecond Folding Kinetics of Horse Apomyoglobin and Yeast Phosphoglycerate Kinase
Yeast phosphoglycerate kinase is a 415 residue dual domain protein which contains two tryptophans located in the C-terminus. PGK readily cold denatures yielding a state generally devoid of stable secondary structure. Kinetic measurements indicated the molecule collapses to a molten globule type …
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Direct observation of fast protein folding: Distinct nanosecond and microsecond events in the folding of apomyoglobin
The rapid refolding dynamics of horse apomyoglobin are followed by a new temperature-jump fluorescence technique on a nanosecond to 0.5 millisecond time scale in vitro. Collapse to a compact state is complete in under 20 microseconds under strongly-nativizing conditions. The intrinsic tryptophan …
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Ultrasonic Absorption in Solutions of Proteins and Peptides and in Suspensions of Liposomes
… technique: aqueous solutions of myoglobin, apomyoglobin, (alpha)-lactalbumin, bacitracin, and the C and N-terminal CNBr cleavage fragments of myoglobin and equeous suspensions of large unilamellar lipid vesicles (LUV) of various compositions. Measurements were performed at temperatures …
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Polymeric microfluidic platform combined with Fourier Transform infrared imaging to explore biomolecular reactions
… studies by tracing the conformational change of apomyoglobin, and its unfolding kinetics. We successfully showed that the secondary structures of apomyoglobin behave differently during unfolding, and the unfolding kinetics changed depending on the dodine concentration.
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Efficient sampling of protein conformational dynamics and prediction of mutation effects.
… the native-state conformational ensemble of apomyoglobin at neutral pH.