Heteropolymer Sequence Design and Preferential Solvation of Hydrophilic Monomers: One More Application of Random Energy Model
arXiv:cond-mat/0701578 · doi:10.1103/PhysRevE.75.041921
Abstract
In this paper, we study the role of surface of the globule and the role of interactions with the solvent for designed sequence heteropolymers using random energy model (REM). We investigate the ground state energy and surface monomer composition distribution. By comparing the freezing transition in random and designed sequence heteropolymers, we discuss the effects of design. Based on our results, we are able to show under which conditions solvation effect improves the quality of sequence design. Finally, we study sequence space entropy and discuss the number of available sequences as a function of imposed requirements for the design quality.
References in corpus (6)
- Why Do Proteins Look Like Proteins?
- Universality Classes for Extreme Value Statistics
- Random Hydrophilic-Hydrophobic Copolymers
- What thermodynamic features characterize good and bad folders? Results from a simplified off-lattice protein model
- Solvation vs. freezing in a heteropolymer globule
- Design of amino acid sequences to fold into C_alpha-model proteins