Bernd Reif mainly investigates Solid-state nuclear magnetic resonance, Analytical chemistry, Magic angle spinning, Nuclear magnetic resonance spectroscopy and Crystallography. He interconnects Yield, Crystallization, Heteronuclear molecule and Membrane protein in the investigation of issues within Solid-state nuclear magnetic resonance. Bernd Reif studied Analytical chemistry and Molecular physics that intersect with Dipole, Homonuclear molecule and Two-dimensional nuclear magnetic resonance spectroscopy.
The various areas that he examines in his Magic angle spinning study include Relaxation, Biophysics, Paramagnetism, Resolution and Peptide. His research in Nuclear magnetic resonance spectroscopy intersects with topics in Dihedral angle and Polarization. His work deals with themes such as Protein dynamics, Ultra high resolution, Molecule and Amide proton, which intersect with Crystallography.
The scientist’s investigation covers issues in Solid-state nuclear magnetic resonance, Nuclear magnetic resonance spectroscopy, Analytical chemistry, Biophysics and Crystallography. The study incorporates disciplines such as Magic angle spinning, Relaxation, Carbon-13 NMR satellite and Deuterium in addition to Solid-state nuclear magnetic resonance. His Nuclear magnetic resonance spectroscopy research includes elements of Dihedral angle and Molecule.
Bernd Reif has researched Analytical chemistry in several fields, including Molecular physics, Protonation, Resolution and Dipole. His Biophysics research incorporates themes from Immunoglobulin light chain and Structural biology, Biochemistry, Protein aggregation. In Crystallography, he works on issues like Membrane protein, which are connected to Lipid bilayer.
His main research concerns Biophysics, Solid-state nuclear magnetic resonance, Fibril, Immunoglobulin light chain and Protein aggregation. Bernd Reif combines subjects such as Small molecule, Membrane associated, Derivative, Curcumin and Protein structure with his study of Biophysics. His Solid-state nuclear magnetic resonance research is multidisciplinary, relying on both Yield, Protonation, Magic angle spinning, Nuclear magnetic resonance spectroscopy and Resolution.
His Protonation research includes themes of Labelling and Analytical chemistry. His Analytical chemistry study integrates concerns from other disciplines, such as Isotopomers and Microcrystalline. His Fibril research is included under the broader classification of Biochemistry.
Fibril, Biophysics, Protein aggregation, Biochemistry and Yield are his primary areas of study. His Fibril study incorporates themes from Protein structure, Toxicity, Pharmacology and Intrinsic fluorescence. His biological study spans a wide range of topics, including Transient, Amyloid beta and Degree.
His Peptide and Protein degradation study in the realm of Biochemistry interacts with subjects such as Programmed cell death. His Yield research is multidisciplinary, incorporating perspectives in Resolution, Molecular physics, Spins and Solid-state nuclear magnetic resonance. His work on Solid-state nuclear magnetic resonance is being expanded to include thematically relevant topics such as Magic angle spinning.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils
Jan Bieschke;Martin Herbst;Martin Herbst;Thomas Wiglenda;Ralf P Friedrich.
Nature Chemical Biology (2012)
Ultrahigh resolution in proton solid-state NMR spectroscopy at high levels of deuteration.
Veniamin Chevelkov;Kristina Rehbein;Anne Diehl;Bernd Reif.
Angewandte Chemie (2006)
Direct measurement of angles between bond vectors in high-resolution NMR.
Bernd Reif;Mirko Hennig;Christian Griesinger.
De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.
Chad M. Rienstra;Lisa Tucker-Kellogg;Christopher P. Jaroniec;Morten Hohwy.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case
Salvador Ventura;Jesús Zurdo;Saravanakumar Narayanan;Matilde Parreño.
Proceedings of the National Academy of Sciences of the United States of America (2004)
Proton‐Detected Solid‐State NMR Spectroscopy of Fibrillar and Membrane Proteins
Rasmus Linser;Muralidhar Dasari;Muralidhar Dasari;Matthias Hiller;Victoria Higman;Victoria Higman.
Angewandte Chemie (2011)
1H-1H MAS correlation spectroscopy and distance measurements in a deuterated peptide.
B. Reif;C. P. Jaroniec;Chad Rienstra;M. Hohwy.
Journal of Magnetic Resonance (2001)
ADEQUATE, a New Set of Experiments to Determine the Constitution of Small Molecules at Natural Abundance
Bernd Reif;Matthias Köck;Rainer Kerssebaum;Heonjoong Kang.
Journal of Magnetic Resonance, Series A (1996)
Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers
Juan Miguel Lopez del Amo;Uwe Fink;Muralidhar Dasari;Muralidhar Dasari;Gerlinde Grelle.
Journal of Molecular Biology (2012)
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H−1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser;Benjamin Bardiaux;Victoria Higman;Uwe Fink.
Journal of the American Chemical Society (2011)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: