---
res:
  bibo_abstract:
  - AlphaFold3 predicts highly accurate protein structures from sequence but tends
    to collapse to a single dominant conformation, even when the underlying structure
    is inherently heterogeneous. Moreover, its predictions are oblivious to experimental
    conditions that can alter local sequence conformation. In this work, we show that
    AlphaFold3 can be guided to match data obtained by nuclear magnetic resonance
    (NMR) spectroscopy, X-ray crystallography and cryogenic electron microscopy (cryo-EM)
    experiments and combinations thereof. Our approach can also incorporate data that
    explicitly report on dynamics, such as site-resolved order parameters. We demonstrate
    that this methodology generates compact structural ensembles whose ensemble-averaged
    observables agree with experiment, with fewer distance restraint violations than
    traditionally resolved NMR structures and with unmodeled alternate conformations
    uncovered in electron density. This methodology paves the way for experimentally
    aware predictive models that generate structural ensembles consistent with the
    measurements, potentially over multiple modalities, and that can be further refined
    toward thermodynamically grounded ensembles by incorporating energetics.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Sai A
      foaf_name: Maddipatla, Sai A
      foaf_surname: Maddipatla
      foaf_workInfoHomepage: http://www.librecat.org/personId=e957f5e5-91c9-11f0-a95f-e090f66ecb4d
  - foaf_Person:
      foaf_givenName: Nadav E
      foaf_name: Sellam, Nadav E
      foaf_surname: Sellam
      foaf_workInfoHomepage: http://www.librecat.org/personId=ef280fe0-91c9-11f0-a95f-8dea3f5bc513
  - foaf_Person:
      foaf_givenName: Meital I
      foaf_name: Bojan, Meital I
      foaf_surname: Bojan
      foaf_workInfoHomepage: http://www.librecat.org/personId=11d88cf5-91ca-11f0-a95f-edf9f08f47b7
  - foaf_Person:
      foaf_givenName: Vova
      foaf_name: Masalitin, Vova
      foaf_surname: Masalitin
      foaf_workInfoHomepage: http://www.librecat.org/personId=ff7958eb-91c9-11f0-a95f-f3bf65828cf6
  - foaf_Person:
      foaf_givenName: Sanketh
      foaf_name: Vedula, Sanketh
      foaf_surname: Vedula
  - foaf_Person:
      foaf_givenName: Paul
      foaf_name: Schanda, Paul
      foaf_surname: Schanda
      foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425
    orcid: 0000-0002-9350-7606
  - foaf_Person:
      foaf_givenName: Ailie
      foaf_name: Marx, Ailie
      foaf_surname: Marx
  - foaf_Person:
      foaf_givenName: Alexander
      foaf_name: Bronstein, Alexander
      foaf_surname: Bronstein
      foaf_workInfoHomepage: http://www.librecat.org/personId=58f3726e-7cba-11ef-ad8b-e6e8cb3904e6
    orcid: 0000-0001-9699-8730
  bibo_doi: 10.1038/s41587-026-03166-5
  dct_date: 2026^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/1087-0156
  - http://id.crossref.org/issn/1546-1696
  dct_language: eng
  dct_publisher: Springer Nature@
  dct_title: Experiment-guided AlphaFold3 resolves measurement-consistent protein
    ensembles@
  fabio_hasPubmedId: '42374114'
...