January 3, 2025, Filed Under: 2008, PublicationsEffects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model. Citation: O’Brien, E. P. ; Ziv, G. ; Haran, G. ; Brooks, B. R. ; Thirumalai, D. Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model. Proc Natl Acad Sci U S A 105, 13403-8. Download effects-of-denaturants-and-osmolytes-on-proteins-are-accurately-predicted-by-the-molecular-transfer-model.pdf939 KB Last updated on 08/18/2017 PubMed DOI
January 3, 2025, Filed Under: 2008, PublicationsFactors governing helix formation in peptides confined to carbon nanotubes. Citation: O’Brien, E. P. ; Stan, G. ; Thirumalai, D. ; Brooks, B. R. Factors governing helix formation in peptides confined to carbon nanotubes. Nano Lett 8 3702-8. Download factors-governing-helix-formation-in-peptides-confined-to-carbon-nanotubes.pdf2.03 MB Last updated on 08/18/2017 PubMed DOI
January 3, 2025, Filed Under: 2008, PublicationsForce-dependent hopping rates of RNA hairpins can be estimated from accurate measurement of the folding landscapes. Citation: Hyeon, C. ; Morrison, G. ; Thirumalai, D. Force-dependent hopping rates of RNA hairpins can be estimated from accurate measurement of the folding landscapes. Proc Natl Acad Sci U S A 105, 9604-9. Download force-dependent-hopping-rates-of-rna-hairpins-can-be-estimated-from-accurate-measurement-of-the-folding-landscapes.pdf754 KB Last updated on 08/18/2017 PubMed DOI
January 3, 2025, Filed Under: 2008, PublicationsInteractions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability. Citation: Vaitheeswaran, S. ; Thirumalai, D. Interactions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability. Proc Natl Acad Sci U S A 105, 17636-41. Download interactions-between-amino-acid-side-chains-in-cylindrical-hydrophobic-nanopores-with-applications-to-peptide-stability.pdf971 KB Last updated on 08/18/2017 PubMed DOI
January 3, 2025, Filed Under: 2008, PublicationsProbing the mechanisms of fibril formation using lattice models. Citation: Li, M. S. ; Klimov, D. K. ; Straub, J. E. ; Thirumalai, D. Probing the mechanisms of fibril formation using lattice models. J Chem Phys 129, 175101. Download probing-the-mechanisms-of-fibril-formation-using-lattice-models.pdf912 KB Last updated on 08/18/2017 PubMed DOI
January 3, 2025, Filed Under: 2008, PublicationsRelative stability of helices determines the folding landscape of adenine riboswitch aptamers. Citation: Lin, J. – C. ; Thirumalai, D. Relative stability of helices determines the folding landscape of adenine riboswitch aptamers. J Am Chem Soc 130, 14080-1. Download Citation relative-stability-of-helices-determines-the-folding-landscape-of-adenine-riboswitch-aptamers.pdf534 KB Last updated on 08/18/2017 PubMed DOI
January 2, 2025, Filed Under: 2008, PublicationsRole of internal chain dynamics on the rupture kinetic of adhesive contacts. Citation: Barsegov, V. ; Morrison, G. ; Thirumalai, D. Role of internal chain dynamics on the rupture kinetic of adhesive contacts. Phys Rev Lett 100, 248102. Download role-of-internal-chain-dynamics-on-the-rupture-kinetics-of-adhesive-contacts.pdf385 KB Last updated on 08/18/2017 PubMed DOI
January 2, 2025, Filed Under: 2008, PublicationsUrea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Citation: Hua, L. ; Zhou, R. ; Thirumalai, D. ; Berne, B. J. Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc Natl Acad Sci U S A 105, 16928-33. Download Citation urea-denaturation-by-stronger-dispersion-interactions-with-proteins-than-water-implies-a-2-stage-unfolding.pdf1.12 MB Last updated on 08/18/2017 PubMed DOI
January 2, 2025, Filed Under: 2008, PublicationsMinimal models for proteins and RNA from folding to function. Citation: Pincus, D. L. ; Cho, S. S. ; Hyeon, C. ; Thirumalai, D. Minimal models for proteins and RNA from folding to function. Prog Mol Biol Transl Sci 84, 203-50. Download minimal-models-for-protein-and-rna-from-folding-to-function.pdf1.87 MB Last updated on 08/18/2017 PubMed DOI
January 2, 2025, Filed Under: 2008, PublicationsEstimations of the size of nucleation regions in globular proteins. Citation: Chen, J. ; Bryngelson, J. D. ; Thirumalai, D. Estimations of the size of nucleation regions in globular proteins. J Phys Chem B 112, 16115-20. Download estimations-of-the-size-of-nucleation-regions-in-globular-proteins.pdf259 KB Last updated on 08/18/2017 PubMed DOI
