Dresden 2009 – scientific programme
Parts | Days | Selection | Search | Downloads | Help
BP: Fachverband Biologische Physik
BP 22: Transport Processes and Cellular Trafficking
BP 22.5: Talk
Thursday, March 26, 2009, 15:30–15:45, ZEU 260
Spot biopolymer motion by NMR — •Michael Kovermann, Martin Schöne, and Jochen Balbach — Institut für Physik/Fachgruppe Biopyhsik, Martin-Luther-Universität Halle-Wittenberg, Betty-Heimann-Straße 7, 06120 Halle/Saale, Germany
The dynamics and the motional behaviour of a protein are important parameters to describe a protein and to understand its function. To learn more about this we characterized the translational motion of various peptides and proteins in solution.
By using a diffusion measurement setup running on an NMR spectrometer we are able to determine the hydrodynamic radius of biopolymers. We compare the correlation times extracted from the diffusion measurements (and known viscosity) with the values from 15N relaxation measurements. From these data we are able to conclude whether the overall tumbling of the biopolymer inside the hydration shell is, on the one hand, caused by the microviscosity or, on the other hand, by the size of the protein.
Additionally we are able to follow a kinetic reaction (fibrillation of the amyloid protein Aβ) which revealed an increase of the hydrodynamic radius by the fibrillation time. This property cannot be observed by using only the signal intensity in the NMR spectrum.