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2006

January 2, 2025, Filed Under: 2006, Publications

Determination of network of residues that regulate allostery in protein families using sequence analysis.

Citation:

Dima, R. I. ; Thirumalai, D. Determination of network of residues that regulate allostery in protein families using sequence analysis. Protein Sci 15, 258-68.

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determination-of-network-of-residues-that-regulate-allostery-in-protein-families-using-sequence-analysis.pdf511 KB

Last updated on 01/03/2018

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January 2, 2025, Filed Under: 2006, Publications

Dynamic transition in tRNA is solvent induced.

Citation:

Caliskan, G. ; Briber, R. M. ; Thirumalai, D. ; Garcia-Sakai, V. ; Woodson, S. A. ; Sokolov, A. P. Dynamic transition in tRNA is solvent induced. J Am Chem Soc 128, 32-3.

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January 2, 2025, Filed Under: 2006, Publications

Effect of finite size on cooperativity and rates of protein folding.

Citation:

Kouza, M. ; Li, M. S. ; O’Brien, E. P. ; Hu, C. – K. ; Thirumalai, D. Effect of finite size on cooperativity and rates of protein folding. J Phys Chem A 110, 671-6.

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effect-of-finite-size-on-cooperativity-and-rates-of-protein-folding.pdf204 KB

Last updated on 01/03/2018

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January 2, 2025, Filed Under: 2006, Publications

Forced-unfolding and force-quench refolding of RNA hairpins.

Citation:

Hyeon, C. ; Thirumalai, D. Forced-unfolding and force-quench refolding of RNA hairpins. Biophys J 90, 3410-27.

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forced-unfolding-and-force-quench-refolding-of-rna-hairpins.pdf555 KB

Last updated on 01/03/2018

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January 2, 2025, Filed Under: 2006, Publications

Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions.

Citation:

Li, M. S. ; Hu, C. – K. ; Klimov, D. K. ; Thirumalai, D. Multiple stepwise refolding of immunoglobulin domain I27 upon force quench depends on initial conditions. Proc Natl Acad Sci U S A 103, 93-8.

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multiple-stepwise-refolding-of-immunoglobulin-domain-i27-upon-force-quench-depends-on-initial-conditions.pdf482 KB

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January 2, 2025, Filed Under: 2006, Publications

Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces.

Citation:

Cheung, M. S. ; Thirumalai, D. Nanopore-protein interactions dramatically alter stability and yield of the native state in restricted spaces. J Mol Biol 357, 632-43.

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January 2, 2025, Filed Under: 2006, Publications

Counterion charge density determines the position and plasticity of RNA folding transition states.

Citation:

Koculi, E. ; Thirumalai, D. ; Woodson, S. A. Counterion charge density determines the position and plasticity of RNA folding transition states. J Mol Biol 359, 446-54.

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January 2, 2025, Filed Under: 2006, Publications

Hydrophobic and ionic interactions in nanosized water droplets.

Citation:

Vaitheeswaran, S. ; Thirumalai, D. Hydrophobic and ionic interactions in nanosized water droplets. J Am Chem Soc 128, 13490-6.

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hydrophobic-and-ionic-interactions-in-nanosized-water-droplets.pdf301 KB

Last updated on 01/03/2018

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January 2, 2025, Filed Under: 2006, Publications

Kinetics of interior loop formation in semiflexible chains.

Citation:

Hyeon, C. ; Thirumalai, D. Kinetics of interior loop formation in semiflexible chains. J Chem Phys 124, 104905.

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kinetics-of-interior-loop-formation-in-semiflexible-chains.pdf590 KB

Last updated on 01/03/2018

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January 2, 2025, Filed Under: 2006, Publications

Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations.

Citation:

Zheng, W. ; Brooks, B. R. ; Thirumalai, D. Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc Natl Acad Sci U S A 103, 7664-9.

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low-frequency-normal-modes-that-describe-allosteric-transitions-in-biological-nanomachines-are-robust-to-sequence-variations.pdf2.41 MB

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