2023 - Research.com Chemistry in Switzerland Leader Award
Roland Riek mostly deals with Protein structure, Biochemistry, Amyloid, Fibril and Nuclear magnetic resonance spectroscopy. His biological study spans a wide range of topics, including Crystallography, Biophysics, Bovine spongiform encephalopathy, Prion protein and Cell biology. His Biochemistry research is multidisciplinary, incorporating elements of Fungal prion, Antiparallel, Fungal protein and Substantia nigra.
His research integrates issues of Protein aggregation, Cooperativity, Beta sheet, Peptide and Alzheimer's disease in his study of Amyloid. His Fibril research incorporates elements of Senile plaques, P3 peptide, Alpha-synuclein and Protein folding. His work in Nuclear magnetic resonance spectroscopy addresses subjects such as Protein secondary structure, which are connected to disciplines such as Scrapie.
His scientific interests lie mostly in Biochemistry, Biophysics, Crystallography, Protein structure and Amyloid. In Biochemistry, he works on issues like Cell biology, which are connected to Programmed cell death. His Crystallography study integrates concerns from other disciplines, such as Lipid bilayer and Intermolecular force.
His Protein structure research incorporates themes from Nuclear magnetic resonance spectroscopy, Prion protein and Rhodanese. His research investigates the connection between Nuclear magnetic resonance spectroscopy and topics such as Spectroscopy that intersect with issues in Transverse relaxation-optimized spectroscopy. The study incorporates disciplines such as Fibril and Peptide in addition to Amyloid.
His main research concerns Biophysics, Amyloid, Fibril, Nuclear magnetic resonance spectroscopy and Alpha-synuclein. His study in Biophysics is interdisciplinary in nature, drawing from both Vesicle, Membrane, Membrane protein and Biological membrane. His study on Membrane is covered under Biochemistry.
His Amyloid research includes themes of Amino acid, Stereochemistry and Peptide. His work investigates the relationship between Fibril and topics such as Intermolecular force that intersect with problems in Resolution. His work carried out in the field of Nuclear magnetic resonance spectroscopy brings together such families of science as Protein structure, Gating, Crystallography and Protonation.
The scientist’s investigation covers issues in Biophysics, Amyloid, Fibril, Biochemistry and Crystallography. The Biophysics study combines topics in areas such as Helix, Membrane, Protein aggregation and Model lipid bilayer. His Fibril study combines topics from a wide range of disciplines, such as Pharmacophore, Structural biology, Alpha-synuclein and Cryo-electron microscopy.
His Biochemistry research is multidisciplinary, relying on both Amyloid fibril, Amyloid β, Solid-state nuclear magnetic resonance and Antiparallel. His studies in Crystallography integrate themes in fields like Nanodisc, Lipid bilayer, Lipid bilayer phase behavior, NMR spectra database and Nuclear magnetic resonance spectroscopy. His Nuclear magnetic resonance spectroscopy research integrates issues from Protein structure and Cooperativity.
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Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
Konstantin Pervushin;Roland Riek;Gerhard Wider;Kurt Wüthrich.
Proceedings of the National Academy of Sciences of the United States of America (1997)
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Thorsten Lührs;Christiane Ritter;Marc Adrian;Dominique Riek-Loher.
Proceedings of the National Academy of Sciences of the United States of America (2005)
NMR structure of the mouse prion protein domain PrP(121–231)
Roland Riek;Simone Hornemann;Gerhard Wider;Martin Billeter.
In vivo demonstration that alpha-synuclein oligomers are toxic.
Beate Winner;Roberto Jappelli;Samir K. Maji;Paula A. Desplats.
Proceedings of the National Academy of Sciences of the United States of America (2011)
NMR Solution Structure of the Human Prion Protein
Ralph Zahn;Aizhuo Liu;Thorsten Lührs;Roland Riek.
Proceedings of the National Academy of Sciences of the United States of America (2000)
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).
Roland Riek;Simone Hornemann;Gerhard Wider;Rudi Glockshuber.
FEBS Letters (1997)
Amyloid fibrils of the HET-s(218–289) prion form a β-solenoid with a triangular hydrophobic core.
Christian Wasmer;Adam Lange;Hélène Van Melckebeke;Ansgar B. Siemer.
Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules
Samir K. Maji;Marilyn H. Perrin;Michael R. Sawaya;Sebastian Jessberger.
Prion (PrPSc)-specific epitope defined by a monoclonal antibody.
Carsten Korth;Beat Stierli;Peter Streit;Markus Moser.
Identifying the amylome, proteins capable of forming amyloid-like fibrils
Lukasz Goldschmidt;Poh K. Teng;Roland Riek;David Eisenberg.
Proceedings of the National Academy of Sciences of the United States of America (2010)
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