Literature DB >> 16473903

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

Changbong Hyeon1, D Thirumalai.   

Abstract

Nanomanipulation of individual RNA molecules, using laser optical tweezers, has made it possible to infer the major features of their energy landscape. Time-dependent mechanical unfolding trajectories, measured at a constant stretching force (f(S)) of simple RNA structures (hairpins and three-helix junctions) sandwiched between RNA/DNA hybrid handles show that they unfold in a reversible all-or-none manner. To provide a molecular interpretation of the experiments we use a general coarse-grained off-lattice Gō-like model, in which each nucleotide is represented using three interaction sites. Using the coarse-grained model we have explored forced-unfolding of RNA hairpin as a function of f(S) and the loading rate (r(f)). The simulations and theoretical analysis have been done both with and without the handles that are explicitly modeled by semiflexible polymer chains. The mechanisms and timescales for denaturation by temperature jump and mechanical unfolding are vastly different. The directed perturbation of the native state by f(S) results in a sequential unfolding of the hairpin starting from their ends, whereas thermal denaturation occurs stochastically. From the dependence of the unfolding rates on r(f) and f(S) we show that the position of the unfolding transition state is not a constant but moves dramatically as either r(f) or f(S) is changed. The transition-state movements are interpreted by adopting the Hammond postulate for forced-unfolding. Forced-unfolding simulations of RNA, with handles attached to the two ends, show that the value of the unfolding force increases (especially at high pulling speeds) as the length of the handles increases. The pathways for refolding of RNA from stretched initial conformation, upon quenching f(S) to the quench force f(Q), are highly heterogeneous. The refolding times, upon force-quench, are at least an order-of-magnitude greater than those obtained by temperature-quench. The long f(Q)-dependent refolding times starting from fully stretched states are analyzed using a model that accounts for the microscopic steps in the rate-limiting step, which involves the trans to gauche transitions of the dihedral angles in the GAAA tetraloop. The simulations with explicit molecular model for the handles show that the dynamics of force-quench refolding is strongly dependent on the interplay of their contour length and persistence length and the RNA persistence length. Using the generality of our results, we also make a number of precise experimentally testable predictions.

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Year:  2006        PMID: 16473903      PMCID: PMC1440726          DOI: 10.1529/biophysj.105.078030

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  46 in total

1.  Solution structure of Cobalt(III)hexammine complexed to the GAAA tetraloop, and metal-ion binding to G.A mismatches.

Authors:  S Rüdisser; I Tinoco
Journal:  J Mol Biol       Date:  2000-02-04       Impact factor: 5.469

2.  Kinetics from nonequilibrium single-molecule pulling experiments.

Authors:  Gerhard Hummer; Attila Szabo
Journal:  Biophys J       Date:  2003-07       Impact factor: 4.033

Review 3.  Force as a useful variable in reactions: unfolding RNA.

Authors:  Ignacio Tinoco
Journal:  Annu Rev Biophys Biomol Struct       Date:  2004

4.  Pulling-speed-dependent force-extension profiles for semiflexible chains.

Authors:  Nam-Kyung Lee; D Thirumalai
Journal:  Biophys J       Date:  2004-05       Impact factor: 4.033

5.  Relaxation dynamics of semiflexible polymers.

Authors:  Y Bohbot-Raviv; W Z Zhao; M Feingold; C H Wiggins; R Granek
Journal:  Phys Rev Lett       Date:  2004-03-03       Impact factor: 9.161

6.  The secondary structure of RNA under tension.

Authors:  M Müller; F Krzakala; M Mézard
Journal:  Eur Phys J E Soft Matter       Date:  2002-09       Impact factor: 1.890

Review 7.  RNA and protein folding: common themes and variations.

Authors:  D Thirumalai; Changbong Hyeon
Journal:  Biochemistry       Date:  2005-04-05       Impact factor: 3.162

8.  Parameters for the Description of Transition States.

Authors:  J E Leffler
Journal:  Science       Date:  1953-03-27       Impact factor: 47.728

9.  Simple model of protein folding kinetics.

Authors:  R Zwanzig
Journal:  Proc Natl Acad Sci U S A       Date:  1995-10-10       Impact factor: 11.205

10.  Folding and stability of a tryptophan-containing mutant of ubiquitin.

Authors:  S Khorasanizadeh; I D Peters; T R Butt; H Roder
Journal:  Biochemistry       Date:  1993-07-13       Impact factor: 3.162

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  35 in total

1.  Effects of pH on proteins: predictions for ensemble and single-molecule pulling experiments.

Authors:  Edward P O'Brien; Bernard R Brooks; D Thirumalai
Journal:  J Am Chem Soc       Date:  2011-12-27       Impact factor: 15.419

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

Authors:  Greg Morrison; Changbong Hyeon; Michael Hinczewski; D Thirumalai
Journal:  Phys Rev Lett       Date:  2011-03-29       Impact factor: 9.161

3.  Force-dependent switch in protein unfolding pathways and transition-state movements.

Authors:  Pavel I Zhuravlev; Michael Hinczewski; Shaon Chakrabarti; Susan Marqusee; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2016-01-27       Impact factor: 11.205

Review 4.  Determination of thermodynamics and kinetics of RNA reactions by force.

Authors:  Ignacio Tinoco; Pan T X Li; Carlos Bustamante
Journal:  Q Rev Biophys       Date:  2006-10-16       Impact factor: 5.318

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

Authors:  Changbong Hyeon; D Thirumalai
Journal:  Biophys J       Date:  2006-10-06       Impact factor: 4.033

6.  Extracting kinetics from single-molecule force spectroscopy: nanopore unzipping of DNA hairpins.

Authors:  Olga K Dudko; Jérôme Mathé; Attila Szabo; Amit Meller; Gerhard Hummer
Journal:  Biophys J       Date:  2007-03-23       Impact factor: 4.033

7.  Force unfolding kinetics of RNA using optical tweezers. II. Modeling experiments.

Authors:  M Manosas; J-D Wen; P T X Li; S B Smith; C Bustamante; I Tinoco; F Ritort
Journal:  Biophys J       Date:  2007-02-09       Impact factor: 4.033

8.  Single-molecule mechanical unfolding and folding of a pseudoknot in human telomerase RNA.

Authors:  Gang Chen; Jin-Der Wen; Ignacio Tinoco
Journal:  RNA       Date:  2007-10-24       Impact factor: 4.942

9.  Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy.

Authors:  Kirstin A Walther; Frauke Gräter; Lorna Dougan; Carmen L Badilla; Bruce J Berne; Julio M Fernandez
Journal:  Proc Natl Acad Sci U S A       Date:  2007-04-30       Impact factor: 11.205

10.  Crowding effects on the mechanical stability and unfolding pathways of ubiquitin.

Authors:  David L Pincus; D Thirumalai
Journal:  J Phys Chem B       Date:  2009-01-08       Impact factor: 2.991

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