Two-Dimensional NMR and Protein Structure

Two-Dimensional NMR Lineshape Analysis

NMR titration experiments are a rich source of structural, mechanistic, thermodynamic and kinetic information on biomolecular interactions, which can be extracted through the quantitative analysis of resonance lineshapes. However, applications of such analyses are frequently limited by peak overlap inherent to complex biomolecular systems. Moreover, systematic errors may arise due to the analys...

Automated NMR protein structure calculation

Nmr Investigations of Protein Structure

Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination.

Several techniques for spectral editing of 2D (13)C-(13)C correlation NMR of proteins are introduced. They greatly reduce the spectral overlap for five common amino acid types, thus simplifying spectral assignment and conformational analysis. The carboxyl (COO) signals of glutamate and aspartate are selected by suppressing the overlapping amide N-CO peaks through (13)C-(15)N dipolar dephasing. ...

Two-Dimensional Fourier Transformation in NMR

The idea of two-dimensional Fourier transformation was originated by Jeener (1) in 1971, but the very wide significance of his proposal does not seem to have been generally realized until several years later, when several elegant applications were described (2-6). The basic idea is very simple. In modern nmr spectrometers, spectra are normally obtained by Fourier transformation of a transient f...