Insights into biomolecular function from small-angle scattering.
Recent advances in neutron and X-ray sources and instrumentation, new and improved scattering techniques, and molecular biology techniques, which have permitted facile preparation of samples, have each led to new opportunities in using small-angle scattering to study the conformations and interactions of biological macromolecules in solution as a function of their properties. For example, new instrumentation on synchrotron sources has facilitated time-resolved studies that yield insights into protein folding. More powerful neutron sources, combined with molecular biology tools that isotopically label samples, have facilitated studies of biomolecular interactions, including those involving active enzymes.
Trewhella
J
J
Chemical Science and Technology Division, Los Alamos National Laboratory, NM 87545, USA. jtrewhella@lanl.gov
D001221:Aspartate Carbamoyltransferase / Q000737:chemistry; D002147:Calmodulin / Q000737:chemistry; D004247:DNA / Q000378:metabolism; D004815:Epidermal Growth Factor / Q000737:chemistry; D005170:Factor X / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D009502:Neutrons; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012542:Scattering, Radiation; D014961:X-Ray Diffraction
D002147:Calmodulin; D011506:Proteins; D004815:Epidermal Growth Factor; D005170:Factor X; D004247:DNA; D001221:Aspartate Carbamoyltransferase