Conjugation of NMR and SAXS for flexible and multidomain protein structure determination: From sample preparation to model refinement

Experimental 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 tec...

Full description

Saved in:
Bibliographic Details
Published in:Progress in biophysics and molecular biology 2020-01, Vol.150, p.140-144
Main Author: Rodríguez-Zamora, P.
Format: Article
Language:English
Subjects:
Algorithms
Computer Simulation
Conjugation methods
Hybrid modeling
Intrinsically Disordered Proteins - chemistry
Magnetic Resonance Spectroscopy - methods
Models, Molecular
NMR
Protein Conformation
Protein structure
SAXS
Scattering, Small Angle
X-Ray Diffraction - methods
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Experimental 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.
ISSN:0079-6107
1873-1732
DOI:10.1016/j.pbiomolbio.2019.08.009