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

ABSTRACT: We establish a framework for assessing whether the transition state location of a biopolymer, which can be inferred from single molecule pulling experiments, corresponds to the ensemble of structures that have equal probability of reaching either the folded or unfolded states (P(fold)=0.5). Using results for the forced unfolding of a RNA hairpin, an exactly soluble model, and an analytic theory, we show that P(fold) is solely determined by s, an experimentally measurable molecular tensegrity parameter, which is a ratio of the tensile force and a compaction force that stabilizes the folded state. Applications to folding landscapes of DNA hairpins and a leucine zipper with two barriers provide a structural interpretation of single molecule experimental data. Our theory can be used to assess whether molecular extension is a good reaction coordinate using measured free energy profiles.

SUBMITTER: Morrison G

PROVIDER: S-EPMC3571105 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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

Morrison Greg G Hyeon Changbong C Hinczewski Michael M Thirumalai D D

Physical review letters 20110329 13

We establish a framework for assessing whether the transition state location of a biopolymer, which can be inferred from single molecule pulling experiments, corresponds to the ensemble of structures that have equal probability of reaching either the folded or unfolded states (P(fold)=0.5). Using results for the forced unfolding of a RNA hairpin, an exactly soluble model, and an analytic theory, we show that P(fold) is solely determined by s, an experimentally measurable molecular tensegrity par ...[more]

PMID: 21517423

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