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CORR
2002
Springer

Long Proteins with Unique Optimal Foldings in the H-P Model

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Long Proteins with Unique Optimal Foldings in the H-P Model
It is widely accepted that (1) the natural or folded state of proteins is a global energy minimum, and (2) in most cases proteins fold to a unique state determined by their amino acid sequence. The H-P (hydrophobic-hydrophilic) model is a simple combinatorial model designed to answer qualitative questions about the protein folding process. In this paper we consider a problem suggested by Brian Hayes in 1998: what proteins in the two-dimensional H-P model have unique optimal (minimum energy) foldings? In particular, we prove that there are closed chains of monomers (amino acids) with this property for all (even) lengths; and that there are open monomer chains with this property for all lengths divisible by four. A preliminary version of this paper appeared at the 17th European Conference on Computational Geometry [2]. 1 Supported by the Austrian Programme for Advanced Research and Technology (APART). 2 Partially supported by NSERC Canada. 3 Supported by DURSI Gen. Cat. 1999SGR00356 and...
Oswin Aichholzer, David Bremner, Erik D. Demaine,
Added 18 Dec 2010
Updated 18 Dec 2010
Type Journal
Year 2002
Where CORR
Authors Oswin Aichholzer, David Bremner, Erik D. Demaine, Henk Meijer, Vera Sacristan, Michael A. Soss
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