Literature DB >> 23345744

Assessment of the quality of energy functions for protein folding by using a criterion derived with the help of the noisy go model.

M Vendruscolo1.   

Abstract

We propose a simple criterion based on the Z-scoreto assess the quality of energy functions for protein folding: one should obtain Z>-10 for the equilibrium ensembleat about native conditions. We derive this criterionby studying a Go model with random errors added to the native interactions. The dependence of the Z-score on the thermodynamic parameters,including the noise, can be precisely obtained in this case,as the ground state of the model is known exactly.We apply this criterion to rapidly rule out two otherwise promisingpairwise energy approximations.The advantage of adopting the present criterionis that it is not necessary to know the ground state of an energy function to assess its quality. It is sufficient to compute the Z-scorefrom a single equilibrium simulation at around the folding temperature.

Keywords:  Effective energy functions; Go model; Protein folding; Z-score

Year:  2001        PMID: 23345744      PMCID: PMC3456590          DOI: 10.1023/A:1013152026788

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  18 in total

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Journal:  J Mol Biol       Date:  2000-03-10       Impact factor: 5.469

3.  A statistical mechanical method to optimize energy functions for protein folding.

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4.  Experiment and theory highlight role of native state topology in SH3 folding.

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Journal:  Nat Struct Biol       Date:  1999-11

5.  Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A.

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Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

6.  Three key residues form a critical contact network in a protein folding transition state.

Authors:  M Vendruscolo; E Paci; C M Dobson; M Karplus
Journal:  Nature       Date:  2001-02-01       Impact factor: 49.962

7.  Effective energy function for proteins in solution.

Authors:  T Lazaridis; M Karplus
Journal:  Proteins       Date:  1999-05-01

8.  Comparison of two optimization methods to derive energy parameters for protein folding: perceptron and Z score.

Authors:  M Vendruscolo; L A Mirny; E I Shakhnovich; E Domany
Journal:  Proteins       Date:  2000-11-01

9.  Role of secondary motifs in fast folding polymers: a dynamical variational principle.

Authors:  A Maritan; C Micheletti; J R Banavar
Journal:  Phys Rev Lett       Date:  2000-03-27       Impact factor: 9.161

10.  What should the Z-score of native protein structures be?

Authors:  L Zhang; J Skolnick
Journal:  Protein Sci       Date:  1998-05       Impact factor: 6.725

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  2 in total

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Authors:  Marco Berrera; Henriette Molinari; Federico Fogolari
Journal:  BMC Bioinformatics       Date:  2003-02-28       Impact factor: 3.169

2.  How good are simplified models for protein structure prediction?

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