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2011

January 5, 2025, Filed Under: 2011

Capturing the essence of folding and functions of biomolecules using coarse-grained models.

Citation:

Hyeon, C. ; Thirumalai, D. Capturing the essence of folding and functions of biomolecules using coarse-grained models. Nat Commun 2 487.

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capturing-the-essence-of-folding-and-functions-of-biomolecules-using-coarse-grained-models.pdf1.41 MB

Last updated on 08/17/2017

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January 5, 2025, Filed Under: 2011

Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins.

Citation:

Liu, Z. ; Reddy, G. ; O’Brien, E. P. ; Thirumalai, D. Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins. Proc Natl Acad Sci U S A 108, 7787-92.

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collapse-kinetics-and-chevron-plots-from-simulations-of-denaturant-dependent-folding-of-globular-proteins.pdf1.06 MB

Last updated on 08/17/2017

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January 5, 2025, Filed Under: 2011

Compaction and tensile forces determine the accuracy of folding landscape parameters from single molecule pulling experiments.

Citation:

Morrison, G. ; Hyeon, C. ; Hinczewski, M. ; Thirumalai, D. Compaction and tensile forces determine the accuracy of folding landscape parameters from single molecule pulling experiments. Phys Rev Lett 106, 138102.

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compaction-and-tensile-forces-determine-the-accuracy-of-folding-landscape-parameters-from-single-molecule-pulling-experiments.pdf726 KB

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January 5, 2025, Filed Under: 2011

Crowding promotes the switch from hairpin to pseudoknot conformation in human telomerase RNA.

Citation:

Denesyuk, N. A. ; Thirumalai, D. Crowding promotes the switch from hairpin to pseudoknot conformation in human telomerase RNA. J Am Chem Soc 133, 11858-61.

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crowding-promotes-the-switch-from-hairpin-to-pseudoknot-conformation-in-human-telomerase-rna.pdf1.95 MB

Last updated on 08/17/2017

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January 5, 2025, Filed Under: 2011

Entropic stabilization of proteins by TMAO.

Citation:

Cho, S. S. ; Reddy, G. ; Straub, J. E. ; Thirumalai, D. Entropic stabilization of proteins by TMAO. J Phys Chem B 115, 13401-7.

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entropic-stabilization-of-proteins-by-tmao.pdf3.59 MB

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January 5, 2025, Filed Under: 2011

Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide.

Citation:

O’Brien, E. P. ; Straub, J. E. ; Brooks, B. R. ; Thirumalai, D. Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide. J Phys Chem Lett 2 1171-1177.

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influence-of-nanoparticle-size-and-shape-on-oligomer-formation-of-an-amyloidogenic-peptide.pdf2.93 MB

Last updated on 08/17/2017

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January 5, 2025, Filed Under: 2011

Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped.

Citation:

Xia, F. ; Thirumalai, D. ; Gräter, F. Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped. Proc Natl Acad Sci U S A 108, 6963-8.

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minimum-energy-compact-structures-in-force-quench-polyubiquitin-folding-are-domain-swapped.pdf1.11 MB

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January 5, 2025, Filed Under: 2011

Toward a molecular theory of early and late events in monomer to amyloid fibril formation.

Citation:

Straub, J. E. ; Thirumalai, D. Toward a molecular theory of early and late events in monomer to amyloid fibril formation. Annu Rev Phys Chem 62, 437-63.

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toward-a-molecular-theory-of-early-and-late-events-in-monomer-to-amyloid-fibril-formation.pdf1.95 MB

Last updated on 08/17/2017

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January 5, 2025, Filed Under: 2011

Folding of human telomerase RNA pseudoknot using ion-jump and temperature-quench simulations.

Citation:

Biyun, S. ; Cho, S. S. ; Thirumalai, D. Folding of human telomerase RNA pseudoknot using ion-jump and temperature-quench simulations. J Am Chem Soc 133, 20634-43.

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folding-of-human-telomerase-rna-pseudoknot-using-ion-jump-and-temperature-quench-simulations.pdf4.52 MB

Last updated on 08/17/2017

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