January 5, 2025, Filed Under: 2014Sequence-dependent folding landscapes of adenine riboswitch aptamers. Citation: Lin, J. – C. ; Hyeon, C. ; Thirumalai, D. Sequence-dependent folding landscapes of adenine riboswitch aptamers. Phys Chem Chem Phys 16, 6376-82. Download Citation sequence-dependent-folding-landscapes-of-adenine-riboswitch-apatamers.pdf2.03 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Transmembrane fragment structures of amyloid precursor protein depend on membrane surface curvature. Citation: Dominguez, L. ; Meredith, S. C. ; Straub, J. E. ; Thirumalai, D. Transmembrane fragment structures of amyloid precursor protein depend on membrane surface curvature. J Am Chem Soc 136, 854-7. Download Citation transmembrane-fragment-structures-of-amyloid-precursor-protein-depend-on-membrane-surface-curvature.pdf1.2 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Dynamical transition and heterogeneous hydration dynamics in RNA. Citation: Yoon, J. ; Lin, J. – C. ; Hyeon, C. ; Thirumalai, D. Dynamical transition and heterogeneous hydration dynamics in RNA. J Phys Chem B 118, 7910-9. Download Citation dynamical-transition-and-heterogeneous-hydration-dynamics-in-rna.pdf2.25 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Entropy and enthalpy of interaction between amino acid side chains in nanopores. Citation: Vaitheeswaran, S. ; Thirumalai, D. Entropy and enthalpy of interaction between amino acid side chains in nanopores. J Chem Phys 141, 22D523. Download Citation entropy-and-enthalpy-of-interaction-between-amino-acid-side-chains-in-nanopores.pdf881 KB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Evidence of disorder in biological molecules from single molecule pulling experiments. Citation: Hyeon, C. ; Hinczewski, M. ; Thirumalai, D. Evidence of disorder in biological molecules from single molecule pulling experiments. Phys Rev Lett 112, 138101. Download Citation evidence-of-disorder-in-biological-molecules-from-single-molecule-pulling-experiments.pdf355 KB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Membrane-Protein Interactions Are Key to Understanding Amyloid Formation. Citation: Straub, J. E. ; Thirumalai, D. Membrane-Protein Interactions Are Key to Understanding Amyloid Formation. J Phys Chem Lett 5 633-5. Download Citation membrane-protein-interactions-are-key-to-understanding-amyloid-formation.pdf317 KB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes. Citation: Chakrabarti, S. ; Hinczewski, M. ; Thirumalai, D. Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes. Proc Natl Acad Sci U S A 111, 9048-53. Download Citation plasticity-of-hydrogen-bond-networks-regulates-mechanochemistry-of-cell-adhesion-complexes.pdf1.25 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins. Citation: Zhuravlev, P. I. ; Reddy, G. ; Straub, J. E. ; Thirumalai, D. Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins. J Mol Biol 426, 2653-66. Download Citation propensity-to-form-amyloid-fibrils-is-encoded-as-excitations-in-the-free-energy-landscape-of-monomeric-proteins.pdf1.67 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments. Citation: Ramm, B. ; Stigler, J. ; Hinczewski, M. ; Thirumalai, D. ; Herrmann, H. ; Woehlke, G. ; Rief, M. Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments. Proc Natl Acad Sci U S A 111, 11359-64. Download Citation sequence-resolved-free-energy-profiles-of-stress-bearing-vimentin-intermediate-filaments.pdf4.43 MB Last updated on 08/17/2017 PubMed DOI
January 5, 2025, Filed Under: 2014Structural heterogeneity in transmembrane amyloid precursor protein homodimer is a consequence of environmental selection. Citation: Dominguez, L. ; Foster, L. ; Meredith, S. C. ; Straub, J. E. ; Thirumalai, D. Structural heterogeneity in transmembrane amyloid precursor protein homodimer is a consequence of environmental selection. J Am Chem Soc 136, 9619-26. Download Citation structural-heterogeneity-in-transmembrane-amyloid-precursor-protein-homodimer-is-a-consequence-of-environmental-selection.pdf4.18 MB Last updated on 08/17/2017 PubMed DOI
