Publications of the Schuler Group
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Publications
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2016
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Consistent view of polypeptide chain expansion in chemical denaturants from multiple experimental methods. Journal of the American Chemical Society, 138(36):11714-11726.
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Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment. Journal of the American Chemical Society, 138(36):11702-11713.
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Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. Proceedings of the National Academy of Sciences of the United States of America, 113(37):E5389-E5398.
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Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins. Annual Review of Biophysics, 45:207-231.
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Soluble oligomers of the pore-forming toxin cytolysin a from escherichia coli are off-pathway products of pore assembly. Journal of Biological Chemistry, 291(11):5652-5663.
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Erratum: The assembly dynamics of the cytolytic pore toxin ClyA. Nature Communications, 7:10650.
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2015
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Excited-state annihilation reduces power dependence of single-molecule FRET experiments. Physical Chemistry Chemical Physics (PCCP), 17(48):32304-32315.
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Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations. Journal of Chemical Theory and Computation, 11(11):5543-5553.
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Editorial overview: Biophysical and molecular biological methods: Structure, dynamics, and single molecules. Current Opinion in Structural Biology, 34:iv-vi.
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Gas-Phase FRET Efficiency Measurements To Probe the Conformation of Mass-Selected Proteins. Analytical Chemistry, 87(15):7559-7565.
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Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells. Nature Methods, 12(8):773-779.
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Quantitative interpretation of FRET experiments via molecular simulation: force field and validation. Biophysical Journal, 108(11):2721-2731.
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Temperature-cycle microscopy reveals single-molecule conformational heterogeneity. Physical Chemistry Chemical Physics (PCCP), 17(9):6532-6544.
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Transient misfolding dominates multidomain protein folding. Nature Communications, 6(8861):online.
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The assembly dynamics of the cytolytic pore toxin ClyA. Nature Communications, 6:6198.
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2014
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Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy. Biophysical Journal, 107(12):2882-2893.
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Characterization of variants of the pore-forming toxin ClyA from Escherichia coli controlled by a redox switch. Biochemistry, 53(40):6357-6369.
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Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein. Proceedings of the National Academy of Sciences of the United States of America, 111(37):13355-13360.
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Temperature-dependent solvation modulates the dimensions of disordered proteins. Proceedings of the National Academy of Sciences of the United States of America, 111(14):5213-5218.
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Cryogenic colocalization microscopy for nanometer-distance measurements. ChemPhysChem, 15(4):763-770.
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Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments. Proceedings of the National Academy of Sciences of the United States of America, 111(13):4874-4879.
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Experimental and computational study of BODIPY dye-labeled cavitand dynamics. Journal of the American Chemical Society, 136(6):2441-2449.
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Single-molecule studies of intrinsically disordered proteins. Chemical Reviews, 114(6):3281-3317.
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