ArticleBiophysical journal2010
Order statistics theory of unfolding of multimeric proteins.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Strength, deformability and toughness of uncrosslinked fibrin fibers from theoretical reconstruction of stress-strain curves.Acta biomaterialia · 2021Article
- TensorCalculator: exploring the evolution of mechanical stress in the CCMV capsid.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- SOP-GPU: influence of solvent-induced hydrodynamic interactions on dynamic structural transitions in protein assemblies.Journal of computational chemistry · 2016Article
- Computing Average Passive Forces in Sarcomeres in Length-Ramp Simulations.PLoS computational biology · 2016Article
- -1 Programmed Ribosomal Frameshifting as a Force-Dependent Process.Progress in molecular biology and translational science · 2016Review
- Structural transitions and energy landscape for Cowpea Chlorotic Mottle Virus capsid mechanics from nanomanipulation in vitro and in silico.Biophysical journal · 2013Article
- Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism.The Journal of biological chemistry · 2013Article
- Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Biophysical journal · 2013Article
- Mechanism of fibrin(ogen) forced unfolding.Structure (London, England : 1993) · 2011Article
- Dissociation of bimolecular αIIbβ3-fibrinogen complex under a constant tensile force.Biophysical journal · 2011Article
- Titin-based tension in the cardiac sarcomere: molecular origin and physiological adaptations.Progress in biophysics and molecular biologyReview
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3 authors.
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Abstract
Dynamic force spectroscopy has become indispensable for the exploration of the mechanical properties of proteins. In force-ramp experiments, performed by utilizing a time-dependent pulling force, the peak forces for unfolding transitions in a multimeric protein (D)(N) are used to map the free energy landscape for unfolding for a protein domain D. We show that theoretical modeling of unfolding transitions based on combining the observed first (f(1)), second (f(2)), …, N(th) (f(N)) unfolding forces for a protein tandem of fixed length N, and pooling the force data for tandems of different length, n(1) <n(2) < … <N, leads to an inaccurate estimation of the distribution of unfolding forces for the protein D, ψ(D)(f). This problem can be overcome by using Order statistics theory, which, in conjunction with analytically tractable models, can be used to resolve the molecular characteristics that determine the unfolding micromechanics. We present a simple method of estimation of the parent distribution, ψ(D)(f), based on analyzing the force data for a tandem (D)(n) of arbitrary length n. Order statistics theory is exemplified through a detailed analysis and modeling of the unfolding forces obtained from pulling simulations of the monomer and oligomers of the all-β-sheet WW domain.
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