April 16-28, 1997
To be held at the Ettore Majorana Centre for Scientific Culture, Erice, Sicily, Italy
This Advanced Study Institute will cover structural and dynamic studies of proteins, relating them to protein function and the possibilities of protein design. Methods for the study of protein structure and dynamics continue to evolve and increase in accuracy and precision, with a resultant increase in the understanding of protein function. Our Course will integrate structure and dynamic information that has been obtained by different methods and provide a perspective on the major research questions in structural biology. Our aim is to provide the student with a critical appreciation of the principal methods that can be brought to bear on problems of protein structure, dynamics and function.
The basic principles of these methods of study of protein structure and dynamics - x-ray diffraction, NMR, molecular dynamics and molecular modeling - will first be given in a series of introductory lectures. Additional presentations will focus on specific examples of protein structure determination, experimental and theoretical studies of protein dynamics by different methods, protein-ligand interactions, structure-function relations in proteins, and protein and protein analog design. |
Day 1 | |
Oleg Jardetzky | Overview |
Hans Frauenfelder | The Energy Landscape of Proteins |
Jean-François Lefèvre | Principles of NMR and Dynamics |
Day 2 | |
William Lipscomb | Principles and Methods of Protein Crystallography |
Rudolf Rigler | Spectroscopy of Stochastic Processes and Correlated Motions |
Rudolf Rigler | Spectroscopy of Ensemble and Single Molecule Events |
Day 3 | |
Oleg Jardetzky | Protein Dynamics |
Hans Frauenfelder | Protein Dynamics and Reactions |
Hans Frauenfelder | Structure, Dynamics and Function of Myoglobin |
Jeff Hoch | Molecular Dynamics Simulations: Nuts, Bolts and an Application |
Poster Session I | |
Day 4 | |
William Lipscomb | The Structural Basis of Allostery |
Anthony A. Kossiakoff | Hormone-Receptor Complexes: The Role of Molecular Recognition in Receptor Specificity and Activation |
John Markley | Kinetics and Thermodynamis of Proteins |
Rudolf Rigler | Fluorescence Correlation Spectroscopy: Applications in Life Sciences |
Poster Session II | |
Day 5 | |
Anthony A. Kossiakoff | Design of Molecular Interfaces Using Phage Display Mutagenesis and Non-natural Amino Acids |
John Markley | NMR Investigations of Active Sites of Iron-Sulfur Proteins |
Andreas Plückthun | What if Rational Design Fails? The Power of Evolutionary Methods |
Day 6 - Excursion -Monreale and Palermo or Favignana | |
Day 7 | |
Brian Sykes | Interactions of Antifreeze Proteins with Ice: Sidechain Dynamics |
Angela Gronenborn | Flexibility of DNA-binding Proteins: Implications for Function |
Joseph D. Puglisi | RNA NMR Spectroscopy |
Student Workship I - Structure | |
Day 8 | |
Brian Sykes | Mechanism of Action of Calcium-signaling Proteins |
Jeff Hoch | Modern Spectrum Analysis and Reduced Structure Representation in Protein NMR |
Christopher Dobson | Following Protein Folding in Real Time using NMR |
Student Workship II - Protein Folding | |
Day 9 | |
Angela Gronenborn | Structures of Protein/Nucleic Acid Complexes |
Jeff Hoch | NMR and Physical Studies on Prolactin |
Joseph D. Puglisi | Structural Basis of Aminoglycoside Antibiotic Action |
Afternoon Excursion - Selinunte and Segesta | |
Day 10 | |
Christopher Dobson | The Structural Basis of Protein Folding |
Andreas Plückthun | Designing Antibodies with Improved Binding, Folding Efficiency and Stability |
Jean-François Lefèvre | Fucosylation and Structural Design |
Poster Session III | |
Day 11 | |
Student Workship III - Structure | |
Student Workship IV - Methods | |
Student Workship V - Methods |
You may apply using the attached on-line form!
<-Click there to go to on-line form. |
The total fee, including full board and lodging (arranged by the School) will be US $1,200.
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THE CLOSING DATE FOR RECEIPT OF APPLICATIONS IS MARCH 15, 1997.
©1997 By Robin Holbrook for SMRL, all rights reserved.