Literature DB >> 9032057

Protein structure: what is it possible to predict now?

A V Finkelstein1.   

Abstract

The computational techniques of sorting out protein folds (these techniques include dynamic programming, self-consistent field theory, etc.) have already ceased to be the bottleneck of predictions. The main problem is that all the methods of recognition and prediction of protein structure can actually use only some part of the interactions operating in the chain, and that even their energies are not known precisely. This is the principal source of errors now. The errors can be reduced by employment of many distant homologues, but this opens a possibility to predict a generalized folding pattern rather than a particular fold with all its details.

Mesh:

Year:  1997        PMID: 9032057     DOI: 10.1016/s0959-440x(97)80008-5

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


  4 in total

1.  Prediction of protein thermostability with a direction- and distance-dependent knowledge-based potential.

Authors:  Christian Hoppe; Dietmar Schomburg
Journal:  Protein Sci       Date:  2005-09-09       Impact factor: 6.725

2.  Thermodynamics of interactions between amino acid side chains: experimental differentiation of aromatic-aromatic, aromatic-aliphatic, and aliphatic-aliphatic side-chain interactions in water.

Authors:  A F Pereira de Araujo; T C Pochapsky; B Joughin
Journal:  Biophys J       Date:  1999-05       Impact factor: 4.033

3.  Comparative modelling techniques: where are we?

Authors:  Anna Tramontano
Journal:  Comp Funct Genomics       Date:  2003

4.  Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display.

Authors:  Arumay Pal; Ranjit Prasad Bahadur; Partha Sarathi Ray; Pinak Chakrabarti
Journal:  BMC Bioinformatics       Date:  2009-04-08       Impact factor: 3.169

  4 in total

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