% IMPORTANT: The following is UTF-8 encoded. This means that in the presence % of non-ASCII characters, it will not work with BibTeX 0.99 or older. % Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or % “biber”. @ARTICLE{Byer:491602, author = {Byer, Amanda S. and Pei, Xiaokun and Patterson, Michael G. and Ando, Nozomi}, title = {{S}mall-angle {X}-ray scattering studies of enzymes}, journal = {Current opinion in chemical biology}, volume = {72}, issn = {1367-5931}, address = {London}, publisher = {Current Biology Ltd.}, reportid = {PUBDB-2023-00294}, pages = {102232}, year = {2023}, abstract = {Enzyme function requires conformational changes to achieve substrate binding, domain rearrangements, and interactions with partner proteins, but these movements are difficult to observe. Small-angle X-ray scattering (SAXS) is a versatile structural technique that can probe such conformational changes under solution conditions that are physiologically relevant. Although it is generally considered a low-resolution structural technique, when used to study conformational changes as a function of time, ligand binding, or protein interactions, SAXS can provide rich insight into enzyme behavior, including subtle domain movements. In this perspective, we highlight recent uses of SAXS to probe structural enzyme changes upon ligand and partner-protein binding and discuss tools for signal deconvolution of complex protein solutions.}, cin = {EMBL-User}, ddc = {570}, cid = {I:(DE-H253)EMBL-User-20120814}, pnm = {6G3 - PETRA III (DESY) (POF4-6G3)}, pid = {G:(DE-HGF)POF4-6G3}, experiment = {EXP:(DE-H253)P-P12-20150101}, typ = {PUB:(DE-HGF)16}, pubmed = {36462455}, UT = {WOS:000919611900006}, doi = {10.1016/j.cbpa.2022.102232}, url = {https://bib-pubdb1.desy.de/record/491602}, }