M.Sc. dissertation, Postgraduate School of Studies inChemistry, University of Bradford.
|The Physical Object|
|Number of Pages||199|
Statistical thermodynamics of pressure-induced helix–coil transition of a polypeptide. We discuss the changes in the solvent entropy and the conformational entropy of the polypeptide S C upon the transition from the coil state to the helix by: 5. Solvent Effects in the Helix-Coil Transition Model and the Unusual Biophysics of Intrinsically Disordered Proteins Article (PDF Available) in The Journal of . We discuss the effects of the solvent composition on the helix-coil transition of a polypeptide chain. We use a simple model to demonstrate that improving the hydrogen-bonding ability of the solvent can make the transition less cooperative, without affecting the transition temperature. This effect is very different from other solvent effects Cited by: 8. Crowding effect on helix-coil transition: Beyond entropic stabilization J. Chem. Phys. , (); / Solution effects and the order of the helix–coil transition in polyalanine J. Chem. Phys. , (); / Solvent effects on conformational dynamics of proteins: Cytochrome c in a dried trehalose film.
For a wide variety of synthetic and natural peptides, including both single helices and coiled coils, it is shown that [θ λi] is also essentially independent of substance and of whether the transition is induced by temperature, ionic strength, pH, chain length changes, amino acid substitution, or solvent perturbation. the solvent-free GMPC model of the helix-coil transition and brieﬂy describe the methods we apply. Then, to account for both mechanisms of solvent action we complement the basic, in vacuo Hamiltonian[13,14] these terms has been treated separately before [20,21], but . the helix-coil transition is a conformational diffusion search process (Huang et al., ). With this ongoing debate and the small molecular size of helical polypeptides relative to more complex protein structures, a signiﬁcant amount of interest in helix-coil processes has been generated in the simulation community within the last decade. Solvent effects on excited state relaxation phenomena formation, - causing, however, an increase in the non-radiative decay efficiency -was observed for aniline solutions (ref. 15). In this case excited state association kinetics were observed, supporting the conclusion, that excited complexe formation (solute-solwt# uciplexes) are responsible for the higher deactivation rate.
Effects of pressure and temperature on the helix‐coil transition of an alanine‐based peptide (Ac‐ AA(AAKAA) 3 AAY‐NH 2) have been investigated using CD and FTIR the correlation between CD and FTIR data, we showed that the change in infrared intensity of the amide I′ band at cm −1 is almost identical to the change in the helical content calculated from the CD. CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Abstract. We discuss the effects of the solvent composition on the helix-coil transition of a polypeptide chain. We use a simple model to demonstrate that improving the hydrogen-bonding ability of the sol-vent can make the transition less cooperative, without affecting the transition temperature. Helix-coil transition of gelatin: Helical morphology and stability for an investigation of the effect of solvent molecule size on helix. the exact effect depending upon the concentration. The effects of the main variables on the phase state, the phase diagram, and the main complexation and binding parameters as well as the temperature and enthalpy of the helix–coil transition of Gel within the complexes were investigated. Associative phase separation is observed only for .