Origin of the designability of protein structures

Citation
R. Tatsumi et G. Chikenji, Origin of the designability of protein structures, PHYS REV E, 60(4), 1999, pp. 4696-4700
Citations number
27
Categorie Soggetti
Physics
Journal title
PHYSICAL REVIEW E
ISSN journal
1063651X → ACNP
Volume
60
Issue
4
Year of publication
1999
Part
B
Pages
4696 - 4700
Database
ISI
SICI code
1063-651X(199910)60:4<4696:OOTDOP>2.0.ZU;2-G
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 stru cture is searched within all possible structures or within maximally compac t structures. Second, whether the structure of the used lattice is bipartit e 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 st ructure 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. [S1063-651(99)18810-X].