Dresden 2017 – scientific programme

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BP: Fachverband Biologische Physik

BP 24: Posters - Protein Structure and Dynamics

BP 24.1: Poster

Tuesday, March 21, 2017, 14:00–16:00, P1A

NMR Investigation of Protein Aggregation in Concentrated Solutions of Eye Lens Crystallins. — •Maria Camilles, Susanne Link, Alexey Krushelnitsky, Jochen Balbach, and Kay Saalwächter — Institute of Physics, Faculty of Natural Sciences II, Betty-Heimann-Str. 7, 06120 Halle/Saale, GERMANY

Crystallins are the major vision-related (i.e. refractive) proteins found in the eye lens. The mammalian lens consist of three classes of proteins, i.e alpha-, beta- and gamma-crystallins, which are structural proteins. The former also acts as chaperone. Commonly, proteins are subject to a continuous degradation and replacement process, but the eye lens proteins have to remain stable and soluble for a lifetime. Heat, shock or other stressors can cause aggregation and lead to cataract, thus the major chaperone function is to prevent aggregation. The conventionally used methods to study aggregation include observations by optical techniques applied mostly to dilute solutions. Here we demonstrate the use of 1H pulsed field gradient (PFG) NMR as an alternative to study the aggregation kinetics of crystallin proteins in highly concentrated protein solutions. PFG-NMR provides self-diffusion coefficients and is thus sensitive to aggregate size. We have studied the thermal denaturation and aggregation kinetics of gammaB-crystallin in the absence and presence of alphaB-crystallin. The components can be easily distinguished by their rather different sizes, thus their self diffusion coefficients. Our data demonstrate qualitative changes in the thermal degradation of gammaB-crystallin in the presence of alphaB-crystallin.