Protein folding in contact map space

Eytan Domany

Physica A: Statistical Mechanics and its Applications, 2000, vol. 288, issue 1, 1-9

Abstract: We represent a protein's structure by its contact map. Our aim is to identify the unknown fold of a known sequence by minimizing a (free) energy defined in the space of contact maps. To this end, we developed an efficient method to search this space and to generate low energy maps that are also physical. We proved that the standard pairwise approximation to the free energy is unable to stabilize the native fold of a single protein against a set of carefully generated decoys.

Date: 2000
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
http://www.sciencedirect.com/science/article/pii/S0378437100004106
Full text for ScienceDirect subscribers only. Journal offers the option of making the article available online on Science direct for a fee of $3,000

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:288:y:2000:i:1:p:1-9

DOI: 10.1016/S0378-4371(00)00410-6

Access Statistics for this article

Physica A: Statistical Mechanics and its Applications is currently edited by K. A. Dawson, J. O. Indekeu, H.E. Stanley and C. Tsallis

More articles in Physica A: Statistical Mechanics and its Applications from Elsevier
Bibliographic data for series maintained by Catherine Liu ().