Literature DB >> 11970334

Origin of the designability of protein structures.

R Tatsumi1, G Chikenji.   

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.

Year:  1999        PMID: 11970334     DOI: 10.1103/physreve.60.4696

Source DB:  PubMed          Journal:  Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics        ISSN: 1063-651X


  2 in total

1.  Protein topology and stability define the space of allowed sequences.

Authors:  Patrice Koehl; Michael Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-22       Impact factor: 11.205

2.  Energy landscape of a peptide consisting of alpha-helix, 3(10)-helix, beta-turn, beta-hairpin, and other disordered conformations.

Authors:  J Higo; N Ito; M Kuroda; S Ono; N Nakajima; H Nakamura
Journal:  Protein Sci       Date:  2001-06       Impact factor: 6.725

  2 in total

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