Conjugation of NMR and SAXS for Flexible and Multidomain Protein Structure Determination: From Sample Preparation to Model Refinement

Publication date: Available online 21 August 2019Source: Progress in Biophysics and Molecular BiologyAuthor(s): P. Rodríguez-ZamoraAbstractExperimental information from small angle X-ray scattering (SAXS) is conjugated with nuclear magnetic resonance (NMR) spectroscopy data for the improvement of protein structure determination, particularly for flexible, multidomain or intrinsically disordered proteins. Individually, each of these techniques presents capabilities and limitations: NMR excels in local information, providing atomic resolution, but is limited by protein size, whereas SAXS yields a global envelope of the protein with lower resolution, but revealing domain positions. Different conjugation methodologies use the complementarity of both techniques’ independent constraints to achieve comprehensive protein structure determination and resolve dynamics at a moderate computational expense.
Source: Progress in Biophysics and Molecular Biology - Category: Molecular Biology Source Type: research