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@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},
}