Protein structure prediction using sparse dipolar coupling data

AUTOR(ES)

Qu, Youxing

FONTE

Oxford University Press

RESUMO

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 15N–1H 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 15N–1H 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.

Documentos Relacionados

• Protein structure prediction and analysis using the Robetta server
• The protein structure prediction problem could be solved using the current PDB library
• Water in protein structure prediction
• A program for prediction of protein secondary structure from nucleotide sequence data: application to histocompatibility antigens.
• Magnetic order and energetics of dipolar coupling in magnetic superconductors