Increased usability, algorithmic improvements and incorporation of data mining for structure calculation of proteins with REDCRAFT software package

Background Traditional approaches to elucidation of protein structures by Nuclear Magnetic Resonance spectroscopy (NMR) rely on distance restraints also known as Nuclear Overhauser effects (NOEs). The use of NOEs as the primary source of structure determination by NMR spectroscopy is time consuming...

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Veröffentlicht in:	BMC bioinformatics Jg. 21; H. Suppl 9; S. 204 - 16
Hauptverfasser:	Cole, Casey, Parks, Caleb, Rachele, Julian, Valafar, Homayoun
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	London BioMed Central 03.12.2020 BioMed Central Ltd Springer Nature B.V BMC
Schlagworte:	Algorithms Analysis Bioinformatics Biomedical and Life Sciences Computational Biology/Bioinformatics Computer Appl. in Life Sciences Computer programs Couplings Data Mining Databases, Protein Documentation Folding Graphical user interface Interoperability Life Sciences Linux Magnetic resonance spectroscopy Magnetic Resonance Spectroscopy - methods Mathematical analysis Methods Microarrays Nef protein NMR NMR spectroscopy Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Peptides Protein Conformation Protein folding Proteins Proteins - chemistry Residual dipolar coupling (RDC) Residual dipolar coupling based residue assembly and filter tool (REDCRAFT) Secondary structure Software Software packages Software upgrading Spectroscopy Spectrum analysis Structure Usability User interface User-Computer Interface United States Residual dipolar coupling based residue assembly and filter tool (REDCRAFT) Secondary structure Data mining Protein folding Residual dipolar coupling (RDC)
ISSN:	1471-2105, 1471-2105
Online-Zugang:	Volltext
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