Overview on the Use of NMR to Examine Protein Structure

Vincent Breukels1, Albert Konijnenberg1, Sanne M. Nabuurs1, Jurgen F. Doreleijers1, Nadezda V. Kovalevskaya1, Geerten W. Vuister1

1 Protein Biophysics, Institute for Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands
Publication Name:  Current Protocols in Protein Science
Unit Number:  Unit 17.5
DOI:  10.1002/0471140864.ps1705s64
Online Posting Date:  April, 2011
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Any protein structure determination process contains several steps, starting from obtaining a suitable sample, then moving on to acquiring data and spectral assignment, and lastly to the final steps of structure determination and validation. This unit describes all of these steps, starting with the basic physical principles behind NMR and some of the most commonly measured and observed phenomena such as chemical shift, scalar and residual coupling, and the nuclear Overhauser effect. Then, in somewhat more detail, the process of spectral assignment and structure elucidation is explained. Furthermore, the use of NMR to study protein‐ligand interaction, protein dynamics, or protein folding is described. Curr. Protoc. Protein Sci. 64:17.5.1‐17.5.44. © 2011 by John Wiley & Sons, Inc.

Keywords: NMR; protein structure; interactions

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Table of Contents

  • Introduction
  • Basic Principles
  • Multi‐Dimensional Spectroscopy
  • 15N‐HSQC
  • Instrumentation
  • Sample Preparation
  • Chemical Shift
  • Scalar Coupling, NOE, and Residual Dipolar Coupling
  • Resonance Assignment
  • Fast Methods
  • Structure Determination
  • Relaxation and Dynamic Processes
  • Protein Interactions
  • Protein Folding
  • Conclusions
  • Literature Cited
  • Figures
  • Tables
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Literature Cited

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