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Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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A Multimodal Wide-Field Fourier-Transform Raman Microscope
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TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution

Anna Zawadzka-Kazimierczuk1, Wiktor Koźmiński, Martin Billeter

  • 1Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.

Journal of Biomolecular NMR
|July 19, 2012
PubMed
Summary

This study introduces TSAR, a new program for automating protein resonance assignments from sparse multidimensional Fourier transform (SMFT) NMR data. TSAR efficiently processes complex spectra, achieving high accuracy in residue assignments for challenging protein samples.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Structural biology
  • Biophysics
  • Computational chemistry

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is crucial for protein analysis, with resonance assignment being a fundamental initial step.
  • Increasing spectral complexity, especially for disordered proteins, makes manual assignment difficult and time-consuming.
  • High-dimensional NMR data acquisition is essential for resolving complex spectra.

Purpose of the Study:

  • To develop an automated tool for protein resonance assignment using sparse multidimensional Fourier transform (SMFT) data.
  • To leverage the efficiency and high-resolution capabilities of SMFT for NMR data analysis.
  • To address the challenges in assigning resonances for proteins with complex or disordered structures.

Main Methods:

  • Utilized random sampling of evolution time space combined with sparse multidimensional Fourier transform (SMFT) for efficient data acquisition.
  • Developed the TSAR (Tool for SMFT-based Assignment of Resonances) program to automate the assignment process.
  • Tested TSAR on various protein samples, including a disordered 81-residue protein fragment with repetitive sequences.

Main Results:

  • TSAR successfully exploits the advantages of SMFT input for automated resonance assignment.
  • The program demonstrated flexibility in processing data from various experiments yielding sequential connectivities.
  • High percentages of assigned residues were achieved across test cases without erroneous assignments.

Conclusions:

  • TSAR provides an efficient and accurate automated solution for protein resonance assignment from high-dimensional NMR data.
  • The tool is particularly valuable for analyzing complex or disordered protein structures where manual assignment is challenging.
  • TSAR facilitates faster and more reliable structural and dynamic studies of proteins using NMR spectroscopy.