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@ARTICLE{Yu:619633,
      author       = {Yu, Miao and Gruzinov, Andrey Yu. and Ruan, Hao and
                      Scheidt, Tom and Chowdhury, Aritra and Giofrè, Sabrina and
                      Mohammed, Ahmed S. A. and Caria, Joana and Sauter, Paul F.
                      and Svergun, Dmitri I. and Lemke, Edward A.},
      title        = {{A} genetically encoded anomalous {SAXS} ruler to probe the
                      dimensions of intrinsically disordered proteins},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {121},
      number       = {50},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2024-07772},
      pages        = {e2415220121},
      year         = {2024},
      abstract     = {Intrinsically disordered proteins (IDPs) adopt ensembles of
                      rapidly fluctuating heterogeneous conformations, influencing
                      their binding capabilities and supramolecular transitions.
                      The primary conformational descriptors for understanding IDP
                      ensembles—the radius of gyration (RG), measured by
                      small-angle X-ray scattering (SAXS), and the root mean
                      square (rms) end-to-end distance (RE), probed by fluorescent
                      resonance energy transfer (FRET)—are often reported to
                      produce inconsistent results regarding IDP expansion as a
                      function of denaturant concentration in the buffer. This
                      ongoing debate surrounding the FRET-SAXS discrepancy raises
                      questions about the overall reliability of either method for
                      quantitatively studying IDP properties. To address this
                      discrepancy, we introduce a genetically encoded anomalous
                      SAXS (ASAXS) ruler, enabling simultaneous and direct
                      measurements of RG and RE without assuming a specific
                      structural model. This ruler utilizes a genetically encoded
                      noncanonical amino acid with two bromine atoms, providing an
                      anomalous X-ray scattering signal for precise distance
                      measurements. Through this approach, we experimentally
                      demonstrate that the ratio between RE and RG varies under
                      different denaturing conditions, highlighting the intrinsic
                      properties of IDPs as the primary source of the observed
                      SAXS-FRET discrepancy rather than shortcomings in either of
                      the two established methods. The developed genetically
                      encoded ASAXS ruler emerges as a versatile tool for both
                      IDPs and folded proteins, providing a unified approach for
                      obtaining complementary and site-specific conformational
                      information in scattering experiments, thereby contributing
                      to a deeper understanding of protein functions.},
      cin          = {EMBL-User / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)432343117 - Eine genetisch kodierte ASAXS Methode
                      zur Messung der Eigenschaften von Intrinsisch ungeordneten
                      Proteinen (432343117) / DFG project 464588647 - SFB 1551:
                      Polymerkonzepte zum Verstehen zellulärer Funktionen
                      (464588647) / iNEXT-Discovery - Infrastructure for
                      transnational access and discovery in structural biology
                      (871037)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)432343117 /
                      G:(GEPRIS)464588647 / G:(EU-Grant)871037},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39642200},
      UT           = {WOS:001380520800016},
      doi          = {10.1073/pnas.2415220121},
      url          = {https://bib-pubdb1.desy.de/record/619633},
}