R
Renko de Vries
Researcher at Wageningen University and Research Centre
Publications - 112
Citations - 4835
Renko de Vries is an academic researcher from Wageningen University and Research Centre. The author has contributed to research in topics: Chemistry & Globular protein. The author has an hindex of 32, co-authored 101 publications receiving 4164 citations. Previous affiliations of Renko de Vries include University Medical Center Groningen.
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Complex coacervation of proteins and anionic polysaccharides
TL;DR: The structure of the concentrated polymer phase seems to resemble a continuous polymer phase in which the protein can diffuse around, as well as the individual polysaccharide molecules, which resembles the behaviour of a (viscous) concentrated particle dispersion.
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CRISPR Immunity Relies on the Consecutive Binding and Degradation of Negatively Supercoiled Invader DNA by Cascade and Cas3
Edze R. Westra,Paul B. G. van Erp,Tim Künne,Shi Pey Wong,Raymond H.J. Staals,Christel L.C. Seegers,Sander Bollen,Matthijs M. Jore,Ekaterina Semenova,Konstantin Severinov,Konstantin Severinov,Willem M. de Vos,Willem M. de Vos,Remus T. Dame,Renko de Vries,Stan J. J. Brouns,John van der Oost +16 more
TL;DR: It is shown that Cascade efficiently locates target sequences in negatively supercoiled DNA, but only if these are flanked by a protospacer-adjacent motif (PAM), which exclusively involves the crRNA-complementary DNA strand.
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Thermally Induced Fibrillar Aggregation of Hen Egg White Lysozyme
Luben N. Arnaudov,Renko de Vries +1 more
TL;DR: From atomic force microscopy, it is found that most of the fibrils from hen egg white lysozyme have a thickness of approximately 4 nm and have a coiled structure with a periodicity of approximately 30 nm and show characteristic defects after every four or five turns.
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Multiple steps during the formation of beta-lactoglobulin fibrils.
TL;DR: In this study, the heat induced fibrilar aggregation of the whey protein beta-lactoglobulin is investigated at low pH and at low ionic strength and results indicate that the fibrils formed have a periodic structure with a period of about 25 nm and a thickness of one or two protein monomers.
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Design and self-assembly of simple coat proteins for artificial viruses
Armando Hernandez-Garcia,Daniela J. Kraft,Anne F. J. Janssen,Paul H. H. Bomans,Nico A. J. M. Sommerdijk,Dominique M. E. Thies-Weesie,Marco E. Favretto,Roland Brock,Frits A. de Wolf,Marc W. T. Werten,Paul van der Schoot,Martien A. Cohen Stuart,Renko de Vries +12 more
TL;DR: A rational design for a self-assembling minimal viral coat protein based on simple polypeptide domains is reported, which features precise control over the cooperativity of its self-assembly with single DNA molecules to finally form rod-shaped virus-like particles.