Translational Friction Coefficient of Wormlike Chains

Yamakawa, Hiromi; Fujii, Masanori

doi:10.1021/ma60033a018

Cited by 509 publications

(364 citation statements)

References 5 publications

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“…(Yamakawa & Fujii, 1973) Hearst and Stockmayer (1962) first reported the sedimentation coefficient in relation to wormlike chain parameters, later refined by Yamakawa and Fujii (1973). The original relation given by Yamakawa and Fujii relating the sedimentation coefficient with persistence length was unfortunately misprinted; the correction was given by Freire and García de la Torre (1992): Yamakawa and Fujii (1973) …”

Section: Estimation Of Persistence Lengthmentioning

confidence: 99%

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A novel global hydrodynamic analysis of the molecular flexibility of the dietary fibre polysaccharide konjac glucomannan

et al. 2009

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Section: Estimation Of Persistence Lengthmentioning

confidence: 99%

“…Bushin-Bohdanecky method (Bushin, Tsvetkov, Lysenko & Emel'yanov, 1981;Bohdanecky, 1983) 2. Yamakawa-Fujii method (Yamakawa & Fujii, 1973) and 3. Combined analysis -HYDFIT (Ortega & García de la Torre, 2007) 1.…”

Section: Estimation Of Persistence Lengthmentioning

confidence: 99%

A novel global hydrodynamic analysis of the molecular flexibility of the dietary fibre polysaccharide konjac glucomannan

et al. 2009

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“…26 Kovacic determined from x-ray diffraction studies of oriented fibers of both B-DNA and A-RNA. 28 The hydrodynamic radius of A-RNA was assumed to be the same as that of B-DNA.…”

Section: B Analysis Of Fluorescence Depolarization Datamentioning

confidence: 99%

Torsion and bending of nucleic acids studied by subnanosecond time-resolved fluorescence depolarization of intercalated dyes

Millar

Robbins

Zewail

1982

The Journal of Chemical Physics

159

109

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Subnanosecond time-resolved fluorescence depolarization has been used to monitor the reorientation of ethidium bromide intercalated in native DNA, synthetic polynucleotide complexes, and in supercoiled plasmid DNA. The fluorescence polarization anisotropy was successfully analyzed with an elastic model of DNA dynamics, including both torsion and bending, which yielded an accurate value for the torsional rigidity of the different DNA samples. The dependence of the torsional rigidity on the base sequence, helical structure, and tertiary structure was experimentally observed. The magnitude of the polyelectrolyte contribution to the torsional rigidity of DNA was measured over a wide range of ionic strength, and compared with polyelectrolyte theories for the persistence length. We also observed a rapid initial reorientation of the intercalated ethidium which had a much smaller amplitude in RNA than in DNA.

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“…The frictional coefficient, f, was calculated for both dB1 and dB4 from the WLC dimensions, using a set of wellknown numerical equations, for the unperturbed worm-like chain. 6 Given the f values, s 0 and D 0 were …”

Section: Shape Modelingmentioning

confidence: 99%

Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. II. Hydrodynamic studies

et al. 2003

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Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. II. Hydrodynamic studies van Swieten, E; Friesen, RR; de Kruif, CG; Robillard, GT; Kruif, Cees G. de Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum.

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Translational Friction Coefficient of Wormlike Chains

Cited by 509 publications

References 5 publications

A novel global hydrodynamic analysis of the molecular flexibility of the dietary fibre polysaccharide konjac glucomannan

A novel global hydrodynamic analysis of the molecular flexibility of the dietary fibre polysaccharide konjac glucomannan

Torsion and bending of nucleic acids studied by subnanosecond time-resolved fluorescence depolarization of intercalated dyes

Size and shape of the repetitive domain of high molecular weight wheat gluten proteins. II. Hydrodynamic studies

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