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Sequence design in coarse-grained protein models

In English

Författare

Summary, in English

Designing amino acid sequences that are stable in a given target structure amounts to maximizing a conditional probability. A straightforward approach to accomplish this is a nested Monte Carlo where the conformation space is explored over and over again for different fixed sequences. In this paper we discuss an alternative Monte Carlo approach, multisequence design, where conformation and sequence degrees of freedom are simultaneously probed. The method is explored on hydrophobic/polar models. A statistical analysis of sequence correlations is also discussed. It is found that hydrophobic/polar model sequences and enzymes display hydrophobicity correlations that are qualitatively similar.

Publiceringsår

2000

Språk

Engelska

Sidor

273-281

Publikation/Tidskrift/Serie

Progress of Theoretical Physics Supplement

Volym

138

Dokumenttyp

Konferensbidrag

Förlag

Oxford University Press

Status

Published