Distance Learning: Techniques in Structural Molecular Biology (TSMB)

Nuclear magnetic resonance (NMR) is the second most important technique for determining the three- dimensional structure of macromolecules. This section provides an introduction to NMR with an emphasis on those techniques that are particularly important in structural biology.

• One Dimensional NMR (Peptides)

Spin Physics
Magnetisation
NMR Spectral Parameters
1H NMR Spectra of Amino-acids and Peptides

• Dynamic Aspects of NMR Spectroscopy

Relaxation (T1)
The Nuclear Overhauser Effect
Relaxation (T2)

• Chemical Exchange
• Two and Three-Dimensional NMR of Proteins

COSY and TOCSY
NOESY and ROESY
Application of 2D NMR to the Determination of Protein Structure
Isotope Labelling
3D NMR Structures of Proteins
Protein Folding

Objectives

To provide background material for students unfamiliar with NMR spectroscopy and revision material for those that are.  To show how 1H NMR is a valuable analytical technique in protein studies.  To show how dynamic aspects of NMR can be used to determine the structure and dynamics of proteins in solution. At the end of this section, students should

• Be confident in the basic principles of NMR and be able to understand and analyse simple 1H 1D spectra of amino acids
• Understand how dynamic aspects of NMR (through-bond spin-spin and through-space nuclear Overhauser effects) can be used to determine the three-dimensional structure and dynamics of macromolecules in solution
• Know a few examples of the use of NMR techniques to solve real questions in protein chemistry