scholarly journals Wide-Angle X-Ray Solution Scattering for Protein-Ligand Binding: Multivariate Curve Resolution with Bayesian Confidence Intervals

2013 ◽  
Vol 104 (4) ◽  
pp. 873-883 ◽  
Author(s):  
David D.L. Minh ◽  
Lee Makowski
2014 ◽  
Vol 229 ◽  
pp. 114-122 ◽  
Author(s):  
Wellington H. Cassinelli ◽  
Leandro Martins ◽  
Aline R. Passos ◽  
Sandra H. Pulcinelli ◽  
Celso V. Santilli ◽  
...  

2014 ◽  
Vol 840 ◽  
pp. 20-27 ◽  
Author(s):  
Alexey Voronov ◽  
Atsushi Urakawa ◽  
Wouter van Beek ◽  
Nikolaos E. Tsakoumis ◽  
Hermann Emerich ◽  
...  

2007 ◽  
Vol 12 (7) ◽  
pp. 994-998 ◽  
Author(s):  
Diane J. Rodi ◽  
Suneeta Mandava ◽  
David B. Gore ◽  
Lee Makowski ◽  
Robert F. Fischetti

Small-molecule ligands that change the structure of a protein are likely to affect its function, whereas those causing no structural change are less likely to be functional. Wide-angle x-ray scattering (WAXS) can be easily carried out on proteins and small molecules in solution in the absence of chemical tags or derivatives. The authors demonstrate that WAXS is a sensitive probe of ligand binding to proteins in solution and can distinguish between nonfunctional and productive binding. Furthermore, similar ligand-binding modes translate into similar scattering patterns. This approach has high potential as a novel, generic, low-throughput assay for functional ligand binding. ( Journal of Biomolecular Screening 2007:994-998)


Author(s):  
L. T. Germinario ◽  
J. Blackwell ◽  
J. Frank

This report describes the use of digital correlation and averaging methods 1,2 for the reconstruction of high dose electron micrographs of the chitin-protein complex from Megarhyssa ovipositor. Electron microscopy of uranyl acetate stained insect cuticle has demonstrated a hexagonal array of unstained chitin monofibrils, 2.4−3.0 nm in diameter, in a stained protein matrix3,4. Optical diffraction Indicated a hexagonal lattice with a = 5.1-8.3 nm3 A particularly well ordered complex is found in the ovipositor of the ichneumon fly Megarhyssa: the small angle x-ray data gives a = 7.25 nm, and the wide angle pattern shows that the protein consists of subunits arranged in a 61 helix, with an axial repeat of 3.06 nm5.


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