Non-Arrhenius kinetics for the loop closure of a DNA hairpin.

Intramolecular chain diffusion is an elementary process in the conformational fluctuations of the DNA hairpin-loop. We have studied the temperature and viscosity dependence of a model DNA hairpin-loop by FRET (fluorescence resonance energy transfer) fluctuation spectroscopy (FRETfs). Apparent thermo...

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Main Authors: Wallace, M, Ying, L, Balasubramanian, S, Klenerman, D
Format: Journal article
Language:English
Published: 2001
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author Wallace, M
Ying, L
Balasubramanian, S
Klenerman, D
author_facet Wallace, M
Ying, L
Balasubramanian, S
Klenerman, D
author_sort Wallace, M
collection OXFORD
description Intramolecular chain diffusion is an elementary process in the conformational fluctuations of the DNA hairpin-loop. We have studied the temperature and viscosity dependence of a model DNA hairpin-loop by FRET (fluorescence resonance energy transfer) fluctuation spectroscopy (FRETfs). Apparent thermodynamic parameters were obtained by analyzing the correlation amplitude through a two-state model and are consistent with steady-state fluorescence measurements. The kinetics of closing the loop show non-Arrhenius behavior, in agreement with theoretical prediction and other experimental measurements on peptide folding. The fluctuation rates show a fractional power dependence (beta = 0.83) on the solution viscosity. A much slower intrachain diffusion coefficient in comparison to that of polypeptides was derived based on the first passage time theory of SSS [Szabo, A., Schulten, K. and Schulten, Z. (1980) J. Chem. Phys. 72, 4350-4357], suggesting that intrachain interactions, especially stacking interaction in the loop, might increase the roughness of the free energy surface of the DNA hairpin-loop.
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spelling oxford-uuid:cb67410d-56d6-47a9-b8b7-cca2820672e32022-03-27T07:14:36ZNon-Arrhenius kinetics for the loop closure of a DNA hairpin.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cb67410d-56d6-47a9-b8b7-cca2820672e3EnglishSymplectic Elements at Oxford2001Wallace, MYing, LBalasubramanian, SKlenerman, DIntramolecular chain diffusion is an elementary process in the conformational fluctuations of the DNA hairpin-loop. We have studied the temperature and viscosity dependence of a model DNA hairpin-loop by FRET (fluorescence resonance energy transfer) fluctuation spectroscopy (FRETfs). Apparent thermodynamic parameters were obtained by analyzing the correlation amplitude through a two-state model and are consistent with steady-state fluorescence measurements. The kinetics of closing the loop show non-Arrhenius behavior, in agreement with theoretical prediction and other experimental measurements on peptide folding. The fluctuation rates show a fractional power dependence (beta = 0.83) on the solution viscosity. A much slower intrachain diffusion coefficient in comparison to that of polypeptides was derived based on the first passage time theory of SSS [Szabo, A., Schulten, K. and Schulten, Z. (1980) J. Chem. Phys. 72, 4350-4357], suggesting that intrachain interactions, especially stacking interaction in the loop, might increase the roughness of the free energy surface of the DNA hairpin-loop.
spellingShingle Wallace, M
Ying, L
Balasubramanian, S
Klenerman, D
Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title_full Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title_fullStr Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title_full_unstemmed Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title_short Non-Arrhenius kinetics for the loop closure of a DNA hairpin.
title_sort non arrhenius kinetics for the loop closure of a dna hairpin
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