Literature DB >> 9094322

Perspectives in protein-fold recognition.

A E Torda1.   

Abstract

Fold recognition force fields based on statistics from native structures have become commonplace. New, nonphysical force fields based on optimizing parameters rather than reflecting Boltzmann statistics may offer improvement in force-field performance for threading and other applications. Improvements in sequence-to-structure alignments will also be essential for improved fold recognition.

Mesh：

Substances：

Year:  1997        PMID： 9094322     DOI： 10.1016/s0959-440x(97)80026-7

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


  13 in total

1.  LiveBench-1: continuous benchmarking of protein structure prediction servers.

Authors:  J M Bujnicki; A Elofsson; D Fischer; L Rychlewski
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

2.  Statistical potentials for fold assessment.

Authors:  Francisco Melo; Roberto Sánchez; Andrej Sali
Journal:  Protein Sci       Date:  2002-02       Impact factor: 6.725

3.  Enhanced protein fold recognition using secondary structure information from NMR.

Authors:  D J Ayers; P R Gooley; A Widmer-Cooper; A E Torda
Journal:  Protein Sci       Date:  1999-05       Impact factor: 6.725

4.  Can correct protein models be identified?

Authors:  Björn Wallner; Arne Elofsson
Journal:  Protein Sci       Date:  2003-05       Impact factor: 6.725

5.  Wurst: a protein threading server with a structural scoring function, sequence profiles and optimized substitution matrices.

Authors:  Andrew E Torda; James B Procter; Thomas Huber
Journal:  Nucleic Acids Res       Date:  2004-07-01       Impact factor: 16.971

6.  Alignment of protein sequences by their profiles.

Authors:  Marc A Marti-Renom; M S Madhusudhan; Andrej Sali
Journal:  Protein Sci       Date:  2004-04       Impact factor: 6.725

7.  Fold recognition by combining sequence profiles derived from evolution and from depth-dependent structural alignment of fragments.

Authors:  Hongyi Zhou; Yaoqi Zhou
Journal:  Proteins       Date:  2005-02-01

8.  Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions.

Authors:  O Keskin; I Bahar; A Y Badretdinov; O B Ptitsyn; R L Jernigan
Journal:  Protein Sci       Date:  1998-12       Impact factor: 6.725

9.  Seeking an ancient enzyme in Methanococcus jannaschii using ORF, a program based on predicted secondary structure comparisons.

Authors:  R Aurora; G D Rose
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205

10.  Protein fold recognition without Boltzmann statistics or explicit physical basis.

Authors:  T Huber; A E Torda
Journal:  Protein Sci       Date:  1998-01       Impact factor: 6.725
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.