Origin of the designability of protein structures

Rie Tatsumi and George Chikenji
Phys. Rev. E 60, 4696 – Published 1 October 1999
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Abstract

We examined what determines the designability of two-letter codes (H and P) lattice proteins from three points of view. First, whether the native structure is searched within all possible structures or within maximally compact structures. Second, whether the structure of the used lattice is bipartite or not. Third, the effect of the length of the chain, namely, the number of monomers on the chain. We found that the bipartiteness of the lattice structure is not a main factor that determines the designability. Our results suggest that highly designable structures will be found when the length of the chain is sufficiently long to make the hydrophobic core consisting of a large enough number of monomers.

  • Received 7 December 1998

DOI:https://doi.org/10.1103/PhysRevE.60.4696

©1999 American Physical Society

Authors & Affiliations

Rie Tatsumi and George Chikenji

  • Department of Physics, Graduate School of Science, Osaka University, Machikaneyama-cho 1-1, Toyonaka, Osaka 560-0043, Japan

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Vol. 60, Iss. 4 — October 1999

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