Solution effects and the order of the helix-coil transition in polyalanine
arXiv:cond-mat/0211029 · doi:10.1063/1.1532348
Abstract
We study helix-coil transitions in an all-atom model of polyalanine. Molecules of up to length 30 residues are investigated by multicanonical simulations. Results from two implicit solvent models are compared with each other and with that from simulations in gas phase. While the helix-coil transition is in all three models a true thermodynamic phase transition, we find that its strength is reduced by the protein-solvent interaction term. The order of the helix-coil transition depends on the details of the solvation term.
19 pages, 11 figures
References in corpus (7)
- Multicanonical Recursions
- Finite-size scaling of helix-coil transitions in poly-alanine studied by multicanonical simulations
- Partition Function Zeros and Finite Size Scaling of Helix-Coil Transitions in a Polypeptide
- Solvation model dependency of helix-coil transition in polyalanine
- Yang-Lee zeros and the helix-coil transition in a continuum model of polyalanine
- Numerical comparison of two approaches for the study of phase transitions in small systems
- A new look at the 2D Ising model from exact partition function zeros for large lattice sizes
Cited by in corpus (7)
- Network rigidity at finite temperature: Relationships between thermodynamic stability, the non-additivity of entropy and cooperativity in molecular systems
- Helix vs. Sheet Formation in a Small Peptide
- Metropolis simulations of Met-Enkephalin with solvent-accessible area parameterizations
- On the Helix-coil Transition in Alanine-based Polypeptides in Gas Phase
- Short-time dynamics of polypeptides
- Side chain and backbone ordering in a polypeptide
- Rugged Metropolis Sampling with Simultaneous Updating of Two Dynamical Variables