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Articles by Robert Tycko
Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions
Get full text access Log in, subscribe or purchase for full access. References 1. Boeynaems, S. ∙ Alberti, S. ... Protein phase separation: A new phase in cell biology Trends Cell Biol. 2018; 28:420-435 2. Dignon, G.L. ∙ Best, R.B. ∙ Mittal, J. Biomolecular phase separation: From molecular driving forces to macroscopic properties Annu. Rev. Phys. Chem. 2020; 71:53-75 3. Su, Q. ∙ Mehta, S. ∙ Zhang, J. Liquid-liquid phase separation: Orchestrating cell signaling through time and space Mol. Cell.
Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions
Abstract Solutions of the intrinsically disordered, low-complexity domain of the FUS protein (FUS-LC) undergo liquid-liquid phase separation (LLPS) below temperatures TLLPS in the 20-40° C range.
Experimental Evidence for Millisecond--Timescale Structural Evolution Following the Microsecond--Timescale Folding of a Small Protein
Prior work has shown that small proteins can fold (i.e., convert from unstructured to structured states) within 10μs. Here we use time-resolved solid state nuclear magnetic resonance (ssNMR) methods to show that full folding of the 35-residue villin headpiece subdomain (HP35) requires a slow annealing process that has not been previously detected.
Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Phys. Chem. B 2024, 128, 7 Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Phys. Chem. B 2024, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering - Nature Communications
Abstract Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely instigators of neurodegeneration in Alzheimer’s disease. We report results of time-resolved solid state nuclear magnetic resonance (ssNMR) and light scattering experiments on 40-residue amyloid-β (Aβ40) that provide structural information for oligomers that form on time scales from 0.7 ms to 1.0 h after initiation of self-assembly by a rapid pH drop.
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase
Calmodulin (CaM) mediates a wide range of biological responses to changes in intracellular Ca2+ concentrations through its calcium-dependent binding affinities to numerous target proteins. Binding of two Ca2+ ions to each of the two four-helix-bundle domains of CaM results in major conformational changes that create a potential binding site for the CaM binding domain of a target protein, which also undergoes major conformational changes to form the complex with CaM.
Effects of an HIV-1 maturation inhibitor on the structure and dynamics of CA-SP1 junction helices in virus-like particles
Evidence of magnetism in Earth’s oldest minerals suggests a strong magnetic field around 4 billion years ago. Image credit: Julie Mansy (photographer), Rory D. Cottrell (University of Rochester, Rochester, NY), and John A. Tarduno (University of Rochester, Rochester, NY).
Coexisting Order and Disorder Within a Common 40-Residue Amyloid-β Fibril Structure in Alzheimer's Disease Brain Tissue
U. Ghosh, W. Yau and R. Tycko, Chem. Commun., 2018, Accepted Manuscript , DOI: 10.1039/C8CC01967C If you are not the author of this article and you wish to reproduce material from it in a third party non-RSC publication you must formally request permission using RightsLink. Go to our Instructions for using RightsLink page for details.
Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies
The HIV-1 capsid protein (CA) forms the capsid shell that encloses RNA within a mature HIV-1 virion. Previous studies by electron microscopy have shown that the capsid shell is primarily a triangular lattice of CA hexamers, with variable curvature that destroys the ideal symmetry of a planar lattice. The mature CA lattice depends on CA dimerization, which occurs through interactions between helix 9 segments of the C-terminal domain (CTD) of CA.
Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments
We present the results of solid state nuclear magnetic resonance (NMR) experiments on HIV-1 capsid protein (CA) assemblies with three different morphologies, namely wild-type CA (WT-CA) tubes with 35-60 nm diameters, planar sheets formed by the Arg18-Leu mutant (R18L-CA), and R18L-CA spheres with 20-100 nm diameters. The experiments are intended to elucidate molecular structural variations that underlie these variations in CA assembly morphology.
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