Anders Irbäck
Professor
Sequence design in coarse-grained protein models
Author
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.
Department/s
- Computational Biology and Biological Physics - Undergoing reorganization
Publishing year
2000
Language
English
Pages
273-281
Publication/Series
Progress of Theoretical Physics Supplement
Volume
138
Document type
Conference paper
Publisher
Oxford University Press
Status
Published