* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download republique française - Laboratoire Léon Brillouin (LLB)
Point mutation wikipedia , lookup
Gene regulatory network wikipedia , lookup
Metalloprotein wikipedia , lookup
Two-hybrid screening wikipedia , lookup
Ribosomally synthesized and post-translationally modified peptides wikipedia , lookup
Western blot wikipedia , lookup
Peptide synthesis wikipedia , lookup
Multi-state modeling of biomolecules wikipedia , lookup
Homology modeling wikipedia , lookup
Interactome wikipedia , lookup
Size-exclusion chromatography wikipedia , lookup
Genetic code wikipedia , lookup
Amino acid synthesis wikipedia , lookup
Proteolysis wikipedia , lookup
Biosynthesis wikipedia , lookup
Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup
Protein structure prediction wikipedia , lookup
RÉPUBLIQUE FRANÇAISE CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE - COMMISSARIAT A L'ÉNERGIE ATOMIQUE LABORATOIRE LÉON BRILLOUIN 33 (0) 1.69.08.52.41 Séminaire Physico-chimie & Biologie Vendredi, 24 Juin 2005 11 :00 Bât. 563 - salle 15 A Molecular View of Hydration Dynamics Near a Model Peptide Daniela Russo OGG INFM/CRS SOFT Grenoble (Fr) New experimental techniques such as wide-angle neutron and quasi-elastic neutron scattering, third generation x-ray synchrotrons, accompanied by interpretation and analysis using molecular dynamics, have emerged for characterizing the structure and dynamics of complicated solvent environments near biological macromolecules and interfaces. How these solvents and cosolvents influence protein function or mediate protein-protein interactions have numerous connections to our understanding of the fundamental aspects of cellular function, self-assembly in bio-inspired nanomaterials and in high-throughput protein technologies and bioprocessing. Unfortunately, experimental studies of solvent influences on self-assembly and organization have been relatively rare and not systematic. One of the principal limitations is that techniques able to investigate solution organization or solvation dynamics give highly averaged information over all different kinds of molecular interactions, with a variety of time scales and length scales. To address these limitations, we have developed a well-defined model system based on amino acid monomers in solution that permits us to dissect interactions over nanometer length scales and picosecond time scales. This model system investigates the evolution of solution structure and dynamics by varying amino acid concentration, thereby modeling how the solvent behaves under dissociating conditions when the local concentration of amino acids is relatively dilute, while more concentrated solutions describe the consequences of hydration near assembled solute states or at proteinprotein interfaces when the local concentration of amino acids is very high. In this talk I will place our QENS measurements on model biological solutes in the context of other spectroscopic techniques, and provide both confirming as well as complementary dynamical information that attempts to give a unifying molecular view of hydration dynamics signatures near peptides and proteins. Laboratoire Léon Brillouin - CEA/Saclay - F - 91191 GIF-SUR-YVETTE Télécopieur 33 (0) 1.69.08.82.61