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Showing 1 to 14 of 14 for “"Denatured State"”.
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Thermodynamics and Kinetics of Iso-1-cytochrome c Denatured State
… how proteins fold have focused on the transition state rather than the earliest folding events. We study these initial events using the assumption that protein folding must involve the formation of the most primitive structure possible – a simple loop. Our laboratory has developed a system of …
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Thermodynamics and Kinetics of Iso-1-cytochrome c Denatured State
… how proteins fold have focused on the transition state rather than the earliest folding events. We study these initial events using the assumption that protein folding must involve the formation of the most primitive structure possible – a simple loop. Our laboratory has developed a system of …
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Analysis of the thermodynamic determinants of protein fold specificity in the denatured state ensemble
… becoming clear that focusing only on the native states of protein folds will be insufficient for deciphering the protein folding problem. Knowledge of the thermodynamics of the denatured state is also necessary. In this project, the thermodynamic determinants of the native fold, present in the …
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THERMODYNAMIC AND KINETIC PROPERTIES OF CYTOCHROMES C AND C’ IN THE DENATURED STATE: PROPENSITY FOR RESIDUAL STRUCTURE
… helical propensity and residual structure in the denatured state, two approaches have been taken. In the first project, we have engineered serine in place of alanine near the center of the third helix (positions 83 and 87) in cytochrome c’ (Cytc’) and have measured histidine-heme loop formation in …
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THERMODYNAMIC AND KINETIC PROPERTIES OF CYTOCHROMES C AND C’ IN THE DENATURED STATE: PROPENSITY FOR RESIDUAL STRUCTURE
… helical propensity and residual structure in the denatured state, two approaches have been taken. In the first project, we have engineered serine in place of alanine near the center of the third helix (positions 83 and 87) in cytochrome c’ (Cytc’) and have measured histidine-heme loop formation in …
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NMR study of the unfolding of ribonuclease A, and dynamical studies of liquids in confined geometries
… method. It was found that the pressure denatured states of RNase A display some characteristics of a molten globule, and all three $\alpha$-helices and the $\beta$-sheet of the native protein remain partially folded structures in the pressure denatured state. $\sp1$H spectra of the …
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Direct observation of fast protein folding: Distinct nanosecond and microsecond events in the folding of apomyoglobin
… time scale in vitro. Collapse to a compact state is complete in under 20 microseconds under strongly-nativizing conditions. The intrinsic tryptophan fluorescence (residue 14 in the A alpha helix) serves as a local probe of the A-helix and the disposition of the H alpha helix. Methionine …
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Probing peptide binding to the second PDZ domain of hPTP1E using FT-IR and MS
… residual turn-like structures persisted in the denatured state. Evidence from CD spectroscopy suggested that helical structures remained intact during heating to 75C̕ for PDZ and the PDZ-ENEQVSAV complex.
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Observing the unfolding transition of [beta]-hairpin peptides with nonlinear infrared spectroscopy
… p-turn in the folding pathway. In addition, the denatured state is very poorly understood, which complicates any attempt to describe the folding pathway. In this work, amide I vibrational spectroscopy is used to resolve the secondary structure of P-hairpin peptides during thermal denaturation. …
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Structural and Biophysical Characterisation of Denatured States and Reversible Unfolding of Sensory Rhodopsin II
… 2 investigates the structural features of SDS-denatured states and the kinetics for reversible unfolding of sensory rhodopsin II (pSRII), a retinal-binding photophobic receptor from Natronomonas pharaonis. pSRII is difficult to denature, and only SDS can dislodge the retinal chromophore without …
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THERMODYNAMIC PROPERTIES OF THE UNFOLDED ENSEMBLE OF PROTEINS
… cycle of <italic>E. coli</italic>, in its acid-denatured state, and on a sequence-randomized version of this protein. The effect of variability in thermodynamic conditions, such as temperature and the presence of added chaotropes or kosmotropes, on the equilibrium properties and reconfiguration …
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Computational investigations of protein dynamics and its implications for biological functions
… carried out on the λ*YG mutant. High-pressure denatured states are found to contain a significant amount of helical structure. Upon pressure drop, the protein refolds into the native state in 20 μs. The simulations confirm the existence of pressure-jump induced fast folding pathway for λ*YG. We …
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Hydrodynamic behavior and thermal stability of a PEGylated protein: Studies with hen egg lysozyme
… extrapolated to infinite dilution. 2N---native state, D---denatured state, A---aggregate.</p>
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Pharmacological and Molecular Characterisation of P2Y Receptors in Endothelial and Epithelial Cells
… showed that they may be only recognising non-denatured receptors. These studies suggest that the L247 anti-P2Y2 antibody raised against peptide designed to mimic specific region in the third extracellular loop of human P2Y2 receptor is highly specific and sensitive and provides an important …