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Helix–coil transitions in a simple polypeptide model

✍ Scribed by J. A. McCammon; S. H. Northrup; M. Karplus; R. M. Levy

Publisher
Wiley (John Wiley & Sons)
Year
1980
Tongue
English
Weight
764 KB
Volume
19
Category
Article
ISSN
0006-3525

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✦ Synopsis

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 stabilization energy of helix formation are included. The model is used to study equilibrium and dynamical aspects of the helix–coil transition. The equilibrium properties examined include helix–coil equilibrium constants and their dependence on chain position. Dynamical properties are examined by a stochastic simulation of the Brownian motion of the chain in its solvent surroundings. Correlations in the motions of the residues are found to have an important influence on the helix–coil transition rates.

📜 SIMILAR VOLUMES

Correlated helix–coil transitions in pol
Correlated helix–coil transitions in polypeptides
✍ Michael R. Pear; Scott H. Northrup; J. Andrew McCammon; Martin Karplus; Ronald M 📂 Article 📅 1981 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 218 KB 👁 2 views
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## Abstract Analogous with the Potts model that describes the helix‐coil transition in the isolated polypeptide chain (a Hamiltonian model allowing for the energy __U__ of hydrogen bond formation) the number Q of conformational states of a repeating unit of the chain and the topology of Δ = 3 hydro

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A simple way to incorporate the solvent-peptide interaction in any available theory of the helix-coil transition is developed. The competition between the intramolecular hydrogen bonding and the solvent-polymer hydrogen bonding is considered in multicomponent solvents where some of the components ha