Literature DB >> 26745403

Classic Analysis of Biopolymer Dynamics Is Model Free.

R Bryn Fenwick1, H Jane Dyson2.   

Abstract

Early analysis of biopolymer dynamics relied on a variety of motional models that were difficult to distinguish and sometimes gave contradictory results. The Lipari-Szabo model-free approach (documented in a 1980 article in Biophysical Journal, as well as in two more comprehensive 1982 articles in the Journal of the American Chemical Society, provided a simple formalism that allowed investigators to understand fluorescence and NMR experimental data without having to specify a motional model. Although the model-free method is not universally applicable (for example, its assumption of a uniform correlation time for overall molecular tumbling can be problematic for biomolecules containing areas of disorder), it remains the most popular and widely used technique for analyzing molecular motion.
Copyright © 2016 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2016        PMID: 26745403      PMCID: PMC4805862          DOI: 10.1016/j.bpj.2015.11.022

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


  15 in total

1.  Probing substates in sperm whale myoglobin using high-pressure crystallography.

Authors:  Paul Urayama; George N Phillips; Sol M Gruner
Journal:  Structure       Date:  2002-01       Impact factor: 5.006

2.  Residual dipolar couplings and some specific models for motional averaging.

Authors:  Michaël Deschamps; Iain D Campbell; Jonathan Boyd
Journal:  J Magn Reson       Date:  2005-01       Impact factor: 2.229

3.  A theory of fluorescence polarization decay in membranes.

Authors:  K Kinosita; S Kawato; A Ikegami
Journal:  Biophys J       Date:  1977-12       Impact factor: 4.033

Review 4.  Integrative, dynamic structural biology at atomic resolution--it's about time.

Authors:  Henry van den Bedem; James S Fraser
Journal:  Nat Methods       Date:  2015-04       Impact factor: 28.547

5.  Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.

Authors:  G M Clore; P C Driscoll; P T Wingfield; A M Gronenborn
Journal:  Biochemistry       Date:  1990-08-14       Impact factor: 3.162

6.  On the wobbling-in-cone analysis of fluorescence anisotropy decay.

Authors:  K Kinosita; A Ikegami; S Kawato
Journal:  Biophys J       Date:  1982-02       Impact factor: 4.033

7.  Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes.

Authors:  G Lipari; A Szabo
Journal:  Biophys J       Date:  1980-06       Impact factor: 4.033

8.  Theory for nuclear magnetic relaxation of probes in anisotropic systems: application of cholesterol in phospholipid vesicles.

Authors:  J R Brainard; A Szabo
Journal:  Biochemistry       Date:  1981-08-04       Impact factor: 3.162

9.  Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.

Authors:  L E Kay; D A Torchia; A Bax
Journal:  Biochemistry       Date:  1989-11-14       Impact factor: 3.162

10.  Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme.

Authors:  A M Mandel; M Akke; A G Palmer
Journal:  J Mol Biol       Date:  1995-02-10       Impact factor: 5.469

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