Fibril, Crystallography, Solid-state nuclear magnetic resonance, Peptide and Protein structure are his primary areas of study. His Fibril study incorporates themes from Electron microscope and Senile plaques, Amyloid. His Crystallography research includes themes of Intermolecular force, Nuclear magnetic resonance spectroscopy, Beta sheet, Superconductivity and Alkali metal.
The study incorporates disciplines such as Supramolecular chemistry, Fiber diffraction, Carbon-13 NMR, Structural motif and Crystallite in addition to Solid-state nuclear magnetic resonance. His work investigates the relationship between Peptide and topics such as Amylin that intersect with problems in Transmission electron microscopy and Protein folding. His research in Protein structure intersects with topics in Side chain and Stereochemistry.
His primary scientific interests are in Solid-state nuclear magnetic resonance, Crystallography, Fibril, Nuclear magnetic resonance and Nuclear magnetic resonance spectroscopy. The Solid-state nuclear magnetic resonance study combines topics in areas such as Carbon-13 NMR, Homonuclear molecule, Analytical chemistry, Magic angle spinning and Chemical shift. His studies in Crystallography integrate themes in fields like Protein structure, Beta sheet, Side chain and Intermolecular force.
Robert Tycko focuses mostly in the field of Fibril, narrowing it down to topics relating to Peptide and, in certain cases, Stereochemistry. As part of the same scientific family, Robert Tycko usually focuses on Nuclear magnetic resonance, concentrating on Polarization and intersecting with Spin polarization and Microwave. His work deals with themes such as Alzheimer's disease, Amyloid fibril and Biochemistry, which intersect with Biophysics.
Robert Tycko mainly focuses on Solid-state nuclear magnetic resonance, Fibril, Biophysics, Crystallography and Molecule. His Solid-state nuclear magnetic resonance research incorporates themes from Carbon-13 NMR, Nuclear magnetic resonance spectroscopy, Analytical chemistry, Protein structure and Chemical shift. Robert Tycko usually deals with Protein structure and limits it to topics linked to Side chain and Monomer.
His work carried out in the field of Fibril brings together such families of science as Amino acid, Amyloid fibril, Cryo-electron microscopy and Peptide. His Biophysics research includes elements of Alzheimer's disease, Amyloid β, Phosphorylation and Amyloid. His Crystallography research includes themes of Lattice, Pathogenesis and Intermolecular force.
Robert Tycko spends much of his time researching Fibril, Solid-state nuclear magnetic resonance, Crystallography, Biophysics and Peptide. His study in Fibril is interdisciplinary in nature, drawing from both Hydrophobic effect and Phosphorylation. His Solid-state nuclear magnetic resonance study integrates concerns from other disciplines, such as Nuclear magnetic resonance spectroscopy and Carbon-13 NMR.
Within one scientific family, he focuses on topics pertaining to Chemical shift under Crystallography, and may sometimes address concerns connected to Protein structure, Metastability and Lattice. The Biophysics study which covers Biochemistry that intersects with Amyloid fibril. His Peptide study incorporates themes from Racemic mixture and Self-healing hydrogels.
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.
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Aneta T. Petkova;Yoshitaka Ishii;John J. Balbach;Oleg N. Antzutkin.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Aneta T. Petkova;Richard D. Leapman;Zhihong Guo;Wai Ming Yau.
Science (2005)
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Masato Kato;Tina W. Han;Shanhai Xie;Kevin Shi.
Cell (2012)
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils†
Aneta T. Petkova;Wai-Ming Yau;Robert Tycko.
Biochemistry (2006)
Conducting films of C60 and C70 by alkali-metal doping
R. C. Haddon;A. F. Hebard;M. J. Rosseinsky;D. W. Murphy.
Nature (1991)
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
Anant K. Paravastu;Richard D. Leapman;Wai-Ming Yau;Robert Tycko.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue
Jun-Xia Lu;Wei Qiang;Wai-Ming Yau;Charles D. Schwieters.
Cell (2013)
Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR†
John J. Balbach;Yoshitaka Ishii;Oleg N. Antzutkin;Richard D. Leapman.
Biochemistry (2000)
New Phases of C60 Synthesized at High Pressure
Y. Iwasa;T. Arima;R. M. Fleming;T. Siegrist.
Science (1994)
Molecular structure of amyloid fibrils: insights from solid-state NMR
Robert Tycko.
Quarterly Reviews of Biophysics (2006)
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