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2007

January 2, 2025, Filed Under: 2007, Publications

Intermediates and transition states in protein folding.

Citation:

Thirumalai, D. ; Klimov, D. K. Intermediates and transition states in protein folding. Methods Mol Biol 350, 277-303.

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January 2, 2025, Filed Under: 2007, Publications

Mechanical unfolding of RNA: from hairpins to structures with internal multiloops.

Citation:

Hyeon, C. ; Thirumalai, D. Mechanical unfolding of RNA: from hairpins to structures with internal multiloops. Biophys J 92, 731-43.

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mechanical-unfolding-of-rna-from-hairpins-to-structures-with-internal-multiloops.pdf1.64 MB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Charge density of divalent metal cations determines RNA stability.

Citation:

Koculi, E. ; Hyeon, C. ; Thirumalai, D. ; Woodson, S. A. Charge density of divalent metal cations determines RNA stability. J Am Chem Soc 129, 2676-82.

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charge-density-of-divalent-metal-cations-determines-rna-stability.pdf293 KB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein.

Citation:

Stan, G. ; Lorimer, G. H. ; Thirumalai, D. ; Brooks, B. R. Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein. Proc Natl Acad Sci U S A 104, 8803-8.

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coupling-between-allosteric-transitions-in-groel-and-assisted-folding-of-a-substrate-protein.pdf1.89 MB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism.

Citation:

O’Brien, E. P. ; Dima, R. I. ; Brooks, B. ; Thirumalai, D. Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism. J Am Chem Soc 129, 7346-53.

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interactions-between-hydrophobic-and-ionic-solutes-in-aqueous-guanidinium-chloride-and-urea-solutions-lessons-for-protein-denaturation-mechanism.pdf397 KB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism.

Citation:

Nguyen, P. H. ; Li, M. S. ; Stock, G. ; Straub, J. E. ; Thirumalai, D. Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism. Proc Natl Acad Sci U S A 104, 111-6.

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monomer-adds-to-preformed-structured-oligomers-of-a-beta-peptides-by-a-two-stage-dock-lock-mechanism.pdf2.01 MB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Allosteric communication in dihydrofolate reductase: signaling network and pathways for closed to occluded transition and back.

Citation:

Chen, J. ; Dima, R. I. ; Thirumalai, D. Allosteric communication in dihydrofolate reductase: signaling network and pathways for closed to occluded transition and back. J Mol Biol 374, 250-66.

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allosteric-communication-in-dihydrofolate-reductase-signaling-network-and-pathways-for-closed-to-occluded-transition-and-back.pdf2.59 MB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations.

Citation:

Zheng, W. ; Brooks, B. R. ; Thirumalai, D. Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. Biophys J 93, 2289-99.

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allosteric-transitions-in-the-chaperonin-groel-are-captured-by-a-dominant-normal-mode-that-is-most-robust-to-sequence-variations.pdf1.55 MB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Effects of crowding and confinement on the structures of the transition state ensemble in proteins.

Citation:

Cheung, M. S. ; Thirumalai, D. Effects of crowding and confinement on the structures of the transition state ensemble in proteins. J Phys Chem B 111, 8250-7.

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effects-of-crowding-and-confinement-on-the-structures-of-the-transition-state-ensemble-in-proteins.pdf745 KB

Last updated on 08/18/2017

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January 2, 2025, Filed Under: 2007, Publications

Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations.

Citation:

Mickler, M. ; Dima, R. I. ; Dietz, H. ; Hyeon, C. ; Thirumalai, D. ; Rief, M. Revealing the bifurcation in the unfolding pathways of GFP by using single-molecule experiments and simulations. Proc Natl Acad Sci U S A 104, 20268-73.

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revealing-the-bifurcation-in-the-unfolding-pathways-of-gfp-by-using-single-molecule-experiments-and-simulations.pdf1.08 MB

Last updated on 01/02/2018

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