PINE-SPARKY.2 for automated NMR-based protein structure research.
 

PINE-SPARKY.2 for automated NMR-based protein structure research.

Related Articles PINE-SPARKY.2 for automated NMR-based protein structure research.

Bioinformatics. 2017 Dec 21;:

Authors: Lee W, Markley JL

Abstract
Summary: NMR (nuclear magnetic resonance) spectroscopy, along with X-ray crystallography and Cryo-EM, is one of the three major tools that enable the determination of atomic-level structural models of biological macromolecules. Of these, NMR has the unique ability to follow important processes in solution, including conformational changes, internal dynamics and protein-ligand interactions. As a means for facilitating the handling and analysis of spectra involved in these types of NMR studies, we have developed PINE-SPARKY.2, a software package that integrates and automates discrete tasks that previously required interaction with separate software packages. The graphical user interface of PINE-SPARKY.2 simplifies chemical shift assignment and verification, automated detection of secondary structural elements, predictions of flexibility and hydrophobic cores, and calculation of three-dimensional structural models.
Availability: PINE-SPARKY.2 is available in the latest version of NMRFAM-SPARKY from the National Magnetic Resonance Facility at Madison (http://pine.nmrfam.wisc.edu/download_packages.html), the NMRbox Project (https://nmrbox.org), and to subscribers to the SBGrid (https://sbgrid.org). For a detailed description of the program, see http://www.nmrfam.wisc.edu/pine-sparky2.htm.
Contact: whlee@nmrfam.wisc.edu or markley@nmrfam.wisc.edu.
Supplementary information: Supplementary data are available at Bioinformatics online.


PMID: 29281006 [PubMed - as supplied by publisher]



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