A general strategy is described for finding which amino acid sequences have native states in a desired conformation (inverse design). The approach is used to design sequences of 48 hydrophobic and polar amino acids on three-dimensional lattice structures. Previous studies employing a sequence-space Monte Carlo technique resulted in the successful design of one sequence in ten attempts. The present work also entails the exploration of conformations that compete significantly with the target structure for being its ground state. The design procedure is successful in all the ten cases.
|Titolo:||Protein design in a lattice model of hydrophobic and polar amino acids|
|Autori:||Micheletti C; Seno F; Maritan A; Banavar JR|
|Rivista:||PHYSICAL REVIEW LETTERS|
|Data di pubblicazione:||1998|
|Digital Object Identifier (DOI):||10.1103/PhysRevLett.80.2237|
|Appare nelle tipologie:||1.1 Journal article|