Sequence design in coarse-grained protein models
(2000) 138. p.273-281- Abstract
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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/9d829fc8-41f4-4a71-bc6f-362a5d9eeb41
- author
- Irbäck, Anders
LU
- organization
- publishing date
- 2000
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- host publication
- Progress of Theoretical Physics Supplement
- volume
- 138
- pages
- 9 pages
- publisher
- Oxford University Press
- external identifiers
-
- scopus:0034337312
- DOI
- 10.1143/PTPS.138.273
- language
- English
- LU publication?
- yes
- id
- 9d829fc8-41f4-4a71-bc6f-362a5d9eeb41
- date added to LUP
- 2016-08-17 17:49:20
- date last changed
- 2024-01-04 11:00:43
@inproceedings{9d829fc8-41f4-4a71-bc6f-362a5d9eeb41, abstract = {{<p>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.</p>}}, author = {{Irbäck, Anders}}, booktitle = {{Progress of Theoretical Physics Supplement}}, language = {{eng}}, pages = {{273--281}}, publisher = {{Oxford University Press}}, title = {{Sequence design in coarse-grained protein models}}, url = {{http://dx.doi.org/10.1143/PTPS.138.273}}, doi = {{10.1143/PTPS.138.273}}, volume = {{138}}, year = {{2000}}, }