Rare Dissipative Transitions Punctuate the Initiation of Chemical Denaturation in Proteins.

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Rare Dissipative Transitions Punctuate the Initiation of Chemical Denaturation in Proteins.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

@en

Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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P1476

Rare Dissipative Transitions P ...... ical Denaturation in Proteins.

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P2093

Jeffrey K Weber

http://www.w3.org/2001/XMLSchema#string

Ruhong Zhou

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Seung-Gu Kang

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P2860

Entropy production fluctuation theorem and the nonequilibrium work relation for free energy differences

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Molecular simulation of ab initio protein folding for a millisecond folder NTL9(1-39)

Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine

CHARMM: the biomolecular simulation program

Verification of the Crooks fluctuation theorem and recovery of RNA folding free energies

Scalable molecular dynamics with NAMD

Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields.

Folding and unfolding single RNA molecules under tension.

Direct observation of the three-state folding of a single protein molecule.

P304

812-821

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P31

scholarly article

P356

10.1016/J.BPJ.2017.12.038

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P407

English

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P478

114

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P577

2018-02-01T00:00:00Z

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P698

29490243

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P932

5985007

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