Chemical shift optimization in multidimensional NMR spectra by AUREMOL-SHIFTOPT

J Biomol NMR. 2009 Apr;43(4):197-210. doi: 10.1007/s10858-009-9304-4. Epub 2009 Feb 21.

Abstract

A problem often encountered in multidimensional NMR-spectroscopy is that an existing chemical shift list of a protein has to be used to assign an experimental spectrum but does not fit sufficiently well for a safe assignment. A similar problem occurs when temperature or pressure series of n-dimensional spectra are to be evaluated automatically. We have developed two different algorithms, AUREMOL-SHIFTOPT1 and AUREMOL-SHIFTOPT2 that fulfill this task. In the present contribution their performance is analyzed employing a set of simulated and experimental two-dimensional and three-dimensional spectra obtained from three different proteins. A new z-score based on atom and amino acid specific chemical shift distributions is introduced to weight the chemical shift contributions in different dimensions properly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms*
  • Bacterial Proteins / chemistry
  • Bayes Theorem
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry
  • Pressure
  • Proteins / chemistry*
  • Staphylococcus
  • Temperature

Substances

  • Bacterial Proteins
  • Nitrogen Isotopes
  • Proteins
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphocarrier protein HPr