Berlin 2012 – scientific programme
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BP: Fachverband Biologische Physik
BP 7: Posters: Proteins
BP 7.13: Poster
Monday, March 26, 2012, 17:30–19:30, Poster A
Lactoferrin: dynamics of a flexible protein in solution investigated by neutron scattering — •Clemens Sill1, Ralf Biehl1, Bernd Hoffmann2, and Dieter Richter1 — 1JCNS-1 & ICS-1, Forschungszentrum Jülich, 52425 Jülich, Germany — 2ICS-7, Forschungszentrum Jülich, 52425 Jülich, Germany
The understanding of the functionality of proteins started with a rigid model, namely the Lock and Key analogy, in 1894. Meanwhile, a more dynamic and flexible picture of these macromolecules has evolved to explain protein function like catalyzing biochemical reactions, transport, regulation, storage or defensive tasks. The importance of thermodynamically driven, internal motions for the functioning of proteins is subject of ongoing research.
We will present recent investigations of protein dynamics on Lactoferrin, a protein with antimicrobial activity which is part of the innate immune system. It consists of two binding sites, each is capable of binding and releasing one iron ion. The crystallographic structures show that the binding sites have open and closed conformations, assumedly depending on the presence of iron. We are analyzing the internal dynamics of different binding states to elucidate the binding mechanism with neutron scattering. Our unique method includes large scale structural characterization with small angle neutron scattering and the observation of internal motions of subdomains with neutron spin echo spectroscopy on nanosecond scale. This combination provides the opportunity to investigate the link between binding mechanism, internal dynamics and conformational change.