Dramatic influence of patchy attractions on short-time protein diffusion under crowded conditions
| Autor: | Jin Suk Myung, Anna Stradner, Gerhard Gompper, Saskia Bucciarelli, Bela Farago, Peter Schurtenberger, Shibananda Das, Olaf Holderer, Roland G. Winkler, Gerard A. Vliegenthart |
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| Rok vydání: | 2016 |
| Předmět: |
Cytoplasm
protein-protein interactions neutron spin echo technique 02 engineering and technology Neutron scattering 01 natural sciences Protein–protein interaction Neutron spin echo Diffusion Protein crowding short-time dynamics multiparticle collision dynamics Optics 0103 physical sciences Animals Computer Simulation computer simulations Diffusion (business) Eye lens Anisotropy Research Articles protein diffusion Multidisciplinary 010304 chemical physics anisotropic interactions business.industry Chemistry SciAdv r-articles 021001 nanoscience & nanotechnology Crystallins hydrodynamic interactions Physical Sciences Biophysics Cattle ddc:500 0210 nano-technology business Research Article |
| Zdroj: | Science Advances Science advances 2(12), e1601432-e1601432 (2016). doi:10.1126/sciadv.1601432 University of Copenhagen |
| ISSN: | 2375-2548 |
| DOI: | 10.1126/sciadv.1601432 |
| Popis: | We show that weak patchy attractions markedly slow down protein diffusion under conditions prevailing in living cells. In the dense and crowded environment of the cell cytoplasm, an individual protein feels the presence of and interacts with all surrounding proteins. While we expect this to strongly influence the short-time diffusion coefficient Ds of proteins on length scales comparable to the nearest-neighbor distance, this quantity is difficult to assess experimentally. We demonstrate that quantitative information about Ds can be obtained from quasi-elastic neutron scattering experiments using the neutron spin echo technique. We choose two well-characterized and highly stable eye lens proteins, bovine α-crystallin and γB-crystallin, and measure their diffusion at concentrations comparable to those present in the eye lens. While diffusion slows down with increasing concentration for both proteins, we find marked variations that are directly linked to subtle differences in their interaction potentials. A comparison with computer simulations shows that anisotropic and patchy interactions play an essential role in determining the local short-time dynamics. Hence, our study clearly demonstrates the enormous effect that weak attractions can have on the short-time diffusion of proteins at concentrations comparable to those in the cellular cytosol. |
| Databáze: | OpenAIRE |
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