Multiple helix–coil transitions
✍ Scribed by Donald B. Dupré
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1990
- Tongue
- English
- Weight
- 728 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Conditions for the occurrence of one, two, and even three helix–coil transitions are summarized and further delineated in terms of thermodynamic parameters in simple modifications of a 2 × 2 matrix of statistical weights for amino acid residues in the coiled and helical conformations. Solvent interaction with segments in both the exposed, coiled and compact, helical conformations is worked into the model. Theoretical expressions for the temperature dependence of helical fractions, maximum attained degrees of helicity, and the compositional dependence of transition temperatures are compared with experimental data for two synthetic polypeptides that exhibit multiple helix–coil transitions.
📜 SIMILAR VOLUMES
## Abstract An evolution of procedures to simulate protein structure and folding pathways is described. From an initial focus on the helix–coil transition and on hydrogen‐bonding and hydrophobic interactions, our original attempts to determine protein structure and folding pathways were based on an
## Abstract Certain discrepancies in measured heats of helix–coil transitions in polypeptides are examined in terms of the theory of the effect of solvent composition on transition temperatures and heats in such systems. It is found, generally, that disagreement between enthalpy measurements conduc
## Abstract The broadening of a helix–coil transition due to base pair heterogeneity is calculated on the basis of a cumulant perturbation expansion in the quasi‐grand ensemble. In this ensemble the fictitious, homogeneous chain, to which the perturbation is referred, automatically decreases its co
## Abstract A simplified model of a polypeptide chain is described. Each residue is represented by a single interaction center. The energy of the chain and the force acting on each residue are given as a function of the residue coordinates. Terms to approximate the effect of solvent and the stabili
## Abstract The Lifson‐Roig Model (LRM) and all its variants describe the α‐helix to coil transition in terms of additive component‐free energies within a free energy decomposition scheme, and these contributions are interpreted through sequence‐context dependent nucleation and propagation paramete