Literature DB >> 11102231

Multiple-sequence information provides protection against mis-specified potential energy functions in the lattice model of proteins

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Abstract

The neutral nets in the lattice models of proteins are composed of a group of similar sequences that encode for the same native structure. The maximal neutral nets in an HP and an AB lattice model are investigated by exhaustive enumeration in the conformation space. The result demonstrates that the performance of mis-specified potential functions can be improved significantly by averaging over sequences in the neutral nets.

Year:  2000        PMID: 11102231     DOI: 10.1103/PhysRevLett.85.5242

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  3 in total

1.  Recombinatoric exploration of novel folded structures: a heteropolymer-based model of protein evolutionary landscapes.

Authors:  Yan Cui; Wing Hung Wong; Erich Bornberg-Bauer; Hue Sun Chan
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-22       Impact factor: 11.205

2.  Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins.

Authors:  Susanne Moelbert; Eldon Emberly; Chao Tang
Journal:  Protein Sci       Date:  2004-02-06       Impact factor: 6.725

3.  Biophysics of protein evolution and evolutionary protein biophysics.

Authors:  Tobias Sikosek; Hue Sun Chan
Journal:  J R Soc Interface       Date:  2014-11-06       Impact factor: 4.118

  3 in total

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