NMR for characterizing protein–protein complexes

16–18 April 2008, CERM – University of Florence

http://www.cerm.unifi.it

Programme

Participants

Aim

Nuclear magnetic resonance spectroscopy is the election technique to investigate molecular interactions in solution and is particularly suited for the study of low–affinity and transient complexes. In this workshop we wish to provide new comers with an overview of the potential of nuclear magnetic resonance to screen for macromolecule complex formation, to characterize their exchange regime and protein–protein interaction patterns and to study dynamic and structural properties of protein-protein complexes. In the tutorials, practical cases will be presented and discussed.

Topics

• Introduction to the NMR observables useful to study protein-protein interaction

• Strategies for samples preparation

• NMR methods to study protein–protein interactions

• Integration of NMR data with those of other techniques

• Software tools to describe and model protein–protein complexes.

Speakers

Rolf Boelens, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands

Michael Sattler, Institut of Sctructural Biology and Department Chemie, Technische Universität München

Lucia Banci, Isabella C. Felli, Roberta Pierattelli, and other Staff of CERM, Magnetic Resonance Center, University of Florence

Presentations

• Ivano_Bertini
• Isabella_Felli
• Lucia_Banci
• Michael_Sattler
• Roberta_Pierattelli

Location

The meeting was held at the Magnetic Resonance Center (CERM) of the University of Florence. CERM is located in the new Scientific Campus in Sesto Fiorentino. To reach the Campus, please follow directions reported here

Summary

A workshop for novice users of Nuclear Magnetic Resonance (NMR) was held on 16–18th April, 2008 in Florence, Italy. The workshop provided an overview of the potential of NMR to screen for macromolecular complex formation, to characterize protein–protein interaction patterns, and to study the dynamic and structural properties of protein–protein complexes. Lectures provided an overview of NMR spectroscopy where several cases and approaches were illustrated, with a particular focus on how structural information can be derived from chemical–shift mapping, relaxation measurements and more complex NMR experiments. Current strategies for integrating NMR with other techniques were illustrated and a variety of protein–protein, protein–DNA and protein–ligand interaction cases were presented during the tutorials. Open discussions ensured that the training was presented in a suitable context for individual experimental requirements.