Literature DB >> 1856868

Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA.

D A Pearlman1, P A Kollman.   

Abstract

A recently suggested method for refinement of structural data obtained from two-dimensional nuclear magnetic resonance experiments using molecular dynamics (MD) is explored. In this method, the time-averaged values of the appropriate internal co-ordinates of the molecule, calculated from the MD trajectory, are driven by restraints towards the experimental target values. This contrasts with most refinement procedures currently in use, where restraints are applied based on the instantaneous values of the appropriate co-ordinates. Both refinement methods are applied to the EcoRI restriction site DNA hexamer d(GAATTC)2, using target nuclear Overhauser enhancement distances derived from a one nanosecond unrestrained MD simulation of this structure. The resulting refined structures are compared to the results of the unrestrained MD trajectory, which serves as our "experimental" data. We show that although both methods can yield an average structure with the correct gross morphology, the new method allows both a much more realistic picture of inherent flexibility, and reproduces fine conformational detail better, such as sequence dependency. We also analyze the very long MD trajectory generated here (longer than any previously reported for a DNA oligomer), and find that significantly shorter simulations, typical of those frequently performed, may not yield acceptably reliable values for certain structural parameters.

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Year:  1991        PMID: 1856868     DOI: 10.1016/0022-2836(91)90024-z

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  41 in total

1.  Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal.

Authors:  Joanna Makowska; Adam Liwo; Wioletta Zmudzińska; Agnieszka Lewandowska; Lech Chmurzyński; Harold A Scheraga
Journal:  Biopolymers       Date:  2011-12-09       Impact factor: 2.505

2.  Alpha/gamma transitions in the B-DNA backbone.

Authors:  Péter Várnai; Dragana Djuranovic; Richard Lavery; Brigitte Hartmann
Journal:  Nucleic Acids Res       Date:  2002-12-15       Impact factor: 16.971

3.  Dynamic properties of salmon calcitonin bound to sodium dodecyl sulfate micelles: a restrained molecular dynamics study from NMR data.

Authors:  M A Castiglione Morelli; A Pastore; A Motta
Journal:  J Biomol NMR       Date:  1992-07       Impact factor: 2.835

4.  Molecular dynamics simulation using weak-coupling NOE distance restraining.

Authors:  A P Nanzer; T Huber; A E Torda; W F van Gunsteren
Journal:  J Biomol NMR       Date:  1996-10       Impact factor: 2.835

5.  Automated detection of problem restraints in NMR data sets using the FINGAR genetic algorithm method.

Authors:  D A Pearlman
Journal:  J Biomol NMR       Date:  1999-04       Impact factor: 2.835

6.  Methods of NMR structure refinement: molecular dynamics simulations improve the agreement with measured NMR data of a C-terminal peptide of GCN4-p1.

Authors:  Jozica Dolenc; John H Missimer; Michel O Steinmetz; Wilfred F van Gunsteren
Journal:  J Biomol NMR       Date:  2010-06-04       Impact factor: 2.835

7.  FINGAR: A new genetic algorithm-based method for fitting NMR data.

Authors:  D A Pearlman
Journal:  J Biomol NMR       Date:  1996-07       Impact factor: 2.835

8.  Further evidence for the absence of polyproline II stretch in the XAO peptide.

Authors:  Joanna Makowska; Sylwia Rodziewicz-Motowidlo; Katarzyna Baginska; Mariusz Makowski; Jorge A Vila; Adam Liwo; Lech Chmurzynski; Harold A Scheraga
Journal:  Biophys J       Date:  2007-02-02       Impact factor: 4.033

9.  Sensitivity of NMR internucleotide distances to B-DNA conformation: underlying mechanics.

Authors:  A Lefebvre; S Fermandjian; B Hartmann
Journal:  Nucleic Acids Res       Date:  1997-10-01       Impact factor: 16.971

10.  Using NMR and molecular dynamics to link structure and dynamics effects of the universal base 8-aza, 7-deaza, N8 linked adenosine analog.

Authors:  Alexander M Spring-Connell; Marina G Evich; Harald Debelak; Frank Seela; Markus W Germann
Journal:  Nucleic Acids Res       Date:  2016-08-26       Impact factor: 16.971

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