We present and discuss a novel approach to the direct and inverse protein folding problem. The proposed strategy is based on a variational approach that allows the simultaneous extraction of amino acid interactions and the low-temperature free energy of sequences of amino acids. The knowledge-based technique is simple and straightforward to implement even for realistic off-lattice proteins because it does not entail threading-like procedures. its validity is assessed in the context of a lattice model by means of a variety of stringent checks.
|Titolo:||Variational approach to protein design and extraction of interaction potentials|
|Autori:||Seno F; Micheletti C; Maritan A; Banavar JR|
|Rivista:||PHYSICAL REVIEW LETTERS|
|Data di pubblicazione:||1998|
|Digital Object Identifier (DOI):||10.1103/PhysRevLett.81.2172|
|Appare nelle tipologie:||1.1 Journal article|