A suite of Mathematica notebooks for the analysis of protein main chain 15N NMR relaxation data View Full Text


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Article Info

DATE

2006-12

AUTHORS

Leo Spyracopoulos

ABSTRACT

A suite of Mathematica notebooks has been designed to ease the analysis of protein main chain 15N NMR relaxation data collected at a single magnetic field strength. Individual notebooks were developed to perform the following tasks: nonlinear fitting of 15N-T1 and -T2 relaxation decays to a two parameter exponential decay, calculation of the principal components of the inertia tensor from protein structural coordinates, nonlinear optimization of the principal components and orientation of the axially symmetric rotational diffusion tensor, model-free analysis of 15N-T1, -T2, and {1H}-15N NOE data, and reduced spectral density analysis of the relaxation data. The principle features of the notebooks include use of a minimal number of input files, integrated notebook data management, ease of use, cross-platform compatibility, automatic visualization of results and generation of high-quality graphics, and output of analyses in text format. More... »

PAGES

215

References to SciGraph publications

  • 1995-04. Flexibility and function in HIV-1 protease in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1995-09. Spectral density function mapping using 15N relaxation data exclusively in JOURNAL OF BIOMOLECULAR NMR
  • 1995-07. Processing of heteronuclear NMR relaxation data with the new software DASHA in APPLIED MAGNETIC RESONANCE
  • 2003-01. The use of model selection in the model-free analysis of protein dynamics in JOURNAL OF BIOMOLECULAR NMR
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10858-006-9083-0

    DOI

    http://dx.doi.org/10.1007/s10858-006-9083-0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1014132530

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/17061025


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