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Protein structure prediction using sparse dipolar coupling data.

Abstract：

:Residual dipolar coupling (RDC) represents one of the most exciting emerging NMR techniques for protein structure studies. However, solving a protein structure using RDC data alone is still a highly challenging problem. We report here a computer program, RDC-PROSPECT, for protein structure prediction based on a structural homolog or analog of the target protein in the Protein Data Bank (PDB), which best aligns with the (15)N-(1)H RDC data of the protein recorded in a single ordering medium. Since RDC-PROSPECT uses only RDC data and predicted secondary structure information, its performance is virtually independent of sequence similarity between a target protein and its structural homolog/analog, making it applicable to protein targets beyond the scope of current protein threading techniques. We have tested RDC-PROSPECT on all (15)N-(1)H RDC data (representing 43 proteins) deposited in the BioMagResBank (BMRB) database. The program correctly identified structural folds for 83.7% of the target proteins, and achieved an average alignment accuracy of 98.1% residues within a four-residue shift.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Qu Y,Guo JT,Olman V,Xu Y

doi

10.1093/nar/gkh204

keywords:

subject

Has Abstract

pub_date

2004-01-26 00:00:00

pages

551-61

issue

2

eissn

0305-1048

issn

1362-4962

pii

32/2/551

journal_volume

32

pub_type

杂志文章

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