Conformation-Dependent Sequence Design (Engineering) ofCopolymers
- 26 April 1999
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 82 (17) , 3456-3459
- https://doi.org/10.1103/physrevlett.82.3456
Abstract
A sequence design scheme to generate special primary structures in copolymers is proposed. In this scheme the type which is attributed to a given monomeric unit ( or ) depends on the spatial position of this unit in some “parent” homopolymer chain conformation. We consider two possible parent conformations: globular (giving rise to “proteinlike copolymers”) and adsorbed (generating “adsorption-tuned copolymers”). By means of the Monte Carlo simulations it is shown that the copolymers with specially generated sequences have the physical properties different from those for random copolymers, i.e., they “inherit” some features of the parent conformation.
This publication has 11 references indexed in Scilit:
- Protein design: a perspective from simple tractable modelsFolding and Design, 1998
- Protein-like copolymers: computer simulationPhysica A: Statistical Mechanics and its Applications, 1998
- Symmetry and Kinetic Optimization of Proteinlike HeteropolymersPhysical Review Letters, 1997
- Self-organization in ion-containing polymer systemsPhysics-Uspekhi, 1997
- Criterion that Determines the Foldability of ProteinsPhysical Review Letters, 1996
- Phase Diagram of Heteropolymers with an Imprinted ConformationMacromolecules, 1995
- Minimum energy compact structures of random sequences of heteropolymersPhysical Review Letters, 1993
- Engineering of stable and fast-folding sequences of model proteins.Proceedings of the National Academy of Sciences, 1993
- The bond fluctuation method: a new effective algorithm for the dynamics of polymers in all spatial dimensionsMacromolecules, 1988
- Some problems of the statistical physics of polymer chains with volume interactionReviews of Modern Physics, 1978