Literature DB >> 7648327

Statistics of sequence-structure threading.

S H Bryant1, S F Altschul.   

Abstract

The past two years have seen the rapid development of new recognition methods for protein structure prediction. These algorithms 'thread' the sequence of one protein through the known structure of another, looking for an alignment that corresponds to an energetically favorable model structure. Because they are based on energy calculation, rather than evolutionary distance, these methods extend the possibility of structure prediction by comparative modeling to a larger class of new sequences, where similarity to known structures is recognizable by no other means. The strength of the evidence they offer should be judged by objective statistical tests, however, so as to rule out the possibility that favorable scores arise from chance factors such as similarity of length, composition, or the consideration of a large number of alternative alignments. Calculation of objective p-values by analytical means is not yet possible, but it would appear that approximate values may be obtained by simulation, as they are in gapped, global sequence alignment. We propose that the results of threading experiments should include Z-scores relative to the composition-corrected score distribution obtained for shuffled and optimally aligned sequences.

Mesh:

Year:  1995        PMID: 7648327     DOI: 10.1016/0959-440x(95)80082-4

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  18 in total

1.  Factors limiting the performance of prediction-based fold recognition methods.

Authors:  X de la Cruz; J M Thornton
Journal:  Protein Sci       Date:  1999-04       Impact factor: 6.725

2.  Statistical significance of protein structure prediction by threading.

Authors:  L A Mirny; A V Finkelstein; E I Shakhnovich
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-29       Impact factor: 11.205

3.  A novel approach to decoy set generation: designing a physical energy function having local minima with native structure characteristics.

Authors:  Chen Keasar; Michael Levitt
Journal:  J Mol Biol       Date:  2003-05-23       Impact factor: 5.469

4.  Finding weak similarities between proteins by sequence profile comparison.

Authors:  Anna R Panchenko
Journal:  Nucleic Acids Res       Date:  2003-01-15       Impact factor: 16.971

5.  Statistical significance of threading scores.

Authors:  Afshin Fayyaz Movaghar; Guillaume Launay; Sophie Schbath; Jean-François Gibrat; François Rodolphe
Journal:  J Comput Biol       Date:  2011-12-09       Impact factor: 1.479

6.  The protein structure prediction problem could be solved using the current PDB library.

Authors:  Yang Zhang; Jeffrey Skolnick
Journal:  Proc Natl Acad Sci U S A       Date:  2005-01-14       Impact factor: 11.205

7.  Fold prediction by a hierarchy of sequence, threading, and modeling methods.

Authors:  L Jaroszewski; L Rychlewski; B Zhang; A Godzik
Journal:  Protein Sci       Date:  1998-06       Impact factor: 6.725

8.  A unified statistical framework for sequence comparison and structure comparison.

Authors:  M Levitt; M Gerstein
Journal:  Proc Natl Acad Sci U S A       Date:  1998-05-26       Impact factor: 11.205

9.  Comparison of protein structures using 3D profile alignment.

Authors:  M Suyama; Y Matsuo; K Nishikawa
Journal:  J Mol Evol       Date:  1997       Impact factor: 2.395

10.  Structural and ligand binding analyses of the periplasmic sensor domain of RsbU in Chlamydia trachomatis support a role in TCA cycle regulation.

Authors:  Katelyn R Soules; Aidan Dmitriev; Scott D LaBrie; Zoë E Dimond; Benjamin H May; David K Johnson; Yang Zhang; Kevin P Battaile; Scott Lovell; P Scott Hefty
Journal:  Mol Microbiol       Date:  2019-11-07       Impact factor: 3.501

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