Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly

Haipeng Gong, Yang Shen, George D. Rose

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


We have been analyzing the extent to which protein secondary structure determines protein tertiary structure in simple protein folds. An earlier paper demonstrated that three-dimensional structure can be obtained successfully using only highly approximate backbone torsion angles for every residue. Here, the initial information is further diluted by introducing a realistic degree of experimental uncertainty into this process. In particular, we tackle the practical problem of determining three-dimensional structure solely from backbone chemical shifts, which can be measured directly by NMR and are known to be correlated with a protein's backbone torsion angles. Extending our previous algorithm to incorporate these experimentally determined data, clusters of structures compatible with the experimentally determined chemical shifts were generated by fragment assembly Monte Carlo. The cluster that corresponds to the native conformation was then identified based on four energy terms: steric clash, solventsqueezing, hydrogen-bonding, and hydrophobic contact. Currently, the method has been applied successfully to five small proteins with simple topology. Although still under development, this approach offers promise for high-throughput NMR structure determination. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1515-1521
Number of pages7
JournalProtein Science
Issue number8
StatePublished - Aug 2007


  • Computational analysis
  • NMR spectroscopy
  • Protein structure/folding

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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