Literature DB >> 10508778

Branch-and-terminate: a combinatorial optimization algorithm for protein design.

D B Gordon1, S L Mayo.   

Abstract

BACKGROUND: Several deterministic and stochastic combinatorial optimization algorithms have been applied to computational protein design and homology modeling. As structural targets increase in size, however, it has become necessary to find more powerful methods to address the increased combinatorial complexity.
RESULTS: We present a new deterministic combinatorial search algorithm called 'Branch-and-Terminate' (B&T), which is derived from the Branch-and-Bound search method. The B&T approach is based on the construction of an efficient but very restrictive bounding expression, which is used for the search of a combinatorial tree representing the protein system. The bounding expression is used both to determine the optimal organization of the tree and to perform a highly effective pruning procedure named 'termination'. For some calculations, the B&T method rivals the current deterministic standard, dead-end elimination (DEE), sometimes finding the solution up to 21 times faster. A more significant feature of the B&T algorithm is that it can provide an efficient way to complete the optimization of problems that have been partially reduced by a DEE algorithm.
CONCLUSIONS: The B&T algorithm is an effective optimization algorithm when used alone. Moreover, it can increase the problem size limit of amino acid sidechain placement calculations, such as protein design, by completing DEE optimizations that reach a point at which the DEE criteria become inefficient. Together the two algorithms make it possible to find solutions to problems that are intractable by either algorithm alone.

Mesh:

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Year:  1999        PMID: 10508778     DOI: 10.1016/s0969-2126(99)80176-2

Source DB:  PubMed          Journal:  Structure        ISSN: 0969-2126            Impact factor:   5.006


  24 in total

1.  Folding free energy function selects native-like protein sequences in the core but not on the surface.

Authors:  Alfonso Jaramillo; Lorenz Wernisch; Stéphanie Héry; Shoshana J Wodak
Journal:  Proc Natl Acad Sci U S A       Date:  2002-10-04       Impact factor: 11.205

Review 2.  Structural genomics: computational methods for structure analysis.

Authors:  Sharon Goldsmith-Fischman; Barry Honig
Journal:  Protein Sci       Date:  2003-09       Impact factor: 6.725

3.  A graph-theory algorithm for rapid protein side-chain prediction.

Authors:  Adrian A Canutescu; Andrew A Shelenkov; Roland L Dunbrack
Journal:  Protein Sci       Date:  2003-09       Impact factor: 6.725

4.  Paradigms for computational nucleic acid design.

Authors:  Robert M Dirks; Milo Lin; Erik Winfree; Niles A Pierce
Journal:  Nucleic Acids Res       Date:  2004-02-27       Impact factor: 16.971

5.  Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library.

Authors:  Ronald W Peterson; P Leslie Dutton; A Joshua Wand
Journal:  Protein Sci       Date:  2004-03       Impact factor: 6.725

6.  Action-at-a-distance interactions enhance protein binding affinity.

Authors:  Brian A Joughin; David F Green; Bruce Tidor
Journal:  Protein Sci       Date:  2005-03-31       Impact factor: 6.725

Review 7.  Advances in homology protein structure modeling.

Authors:  Zhexin Xiang
Journal:  Curr Protein Pept Sci       Date:  2006-06       Impact factor: 3.272

8.  Configurational-bias sampling technique for predicting side-chain conformations in proteins.

Authors:  Tushar Jain; David S Cerutti; J Andrew McCammon
Journal:  Protein Sci       Date:  2006-09       Impact factor: 6.725

9.  Modeling backbone flexibility to achieve sequence diversity: the design of novel alpha-helical ligands for Bcl-xL.

Authors:  Xiaoran Fu; James R Apgar; Amy E Keating
Journal:  J Mol Biol       Date:  2007-05-05       Impact factor: 5.469

Review 10.  Challenges in the computational design of proteins.

Authors:  María Suárez; Alfonso Jaramillo
Journal:  J R Soc Interface       Date:  2009-03-11       Impact factor: 4.118

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