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@ARTICLE{Putko:276783,
      author       = {Putko, Paulina and Romero, Javier Agustin and Pantoja,
                      Christian F and Zweckstetter, Markus and Kazimierczuk,
                      Krzysztof and Zawadzka-Kazimierczuk, Anna},
      title        = {{U}sing temperature coefficients to support resonance
                      assignment of intrinsically disordered proteins.},
      journal      = {Journal of biomolecular NMR},
      volume       = {79},
      number       = {1},
      issn         = {0925-2738},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Science + Business Media B.V},
      reportid     = {DZNE-2025-00320},
      pages        = {59 - 65},
      year         = {2025},
      abstract     = {The resonance assignment of large intrinsically disordered
                      proteins (IDPs) is difficult due to the low dispersion of
                      chemical shifts (CSs). Luckily, CSs are often specific for
                      certain residue types, which makes the task easier. Our
                      recent work showed that the CS-based spin-system
                      classification can be improved by applying a linear
                      discriminant analysis (LDA). In this paper, we extend a set
                      of classification parameters by adding temperature
                      coefficients (TCs), i.e., rates of change of chemical shifts
                      with temperature. As demonstrated previously by other
                      groups, the TCs in IDPs depend on a residue type, although
                      the relation is often too complex to be predicted
                      theoretically. Thus, we propose an approach based on
                      experimental data; CSs and TCs values of residues assigned
                      using conventional methods serve as a training set for LDA,
                      which then classifies the remaining resonances. The method
                      is demonstrated on a large fragment (1-239) of highly
                      disordered protein Tau. We noticed that adding TCs to sets
                      of chemical shifts significantly improves the recognition
                      efficiency. For example, it allows distinguishing between
                      lysine and glutamic acid, as well as valine and isoleucine
                      residues based on H N , N, C α and C ' data. Moreover,
                      adding TCs to CSs of H N , N, C α , and C ' is more
                      beneficial than adding C β CSs. Our program for LDA
                      analysis is available at
                      https://github.com/gugumatz/LDA-Temp-Coeff .},
      keywords     = {Intrinsically Disordered Proteins: chemistry / Nuclear
                      Magnetic Resonance, Biomolecular: methods / Temperature /
                      Discriminant Analysis / Intrinsically disordered proteins
                      (Other) / Tau protein (Other) / Temperature coefficients
                      (Other) / Intrinsically Disordered Proteins (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {570},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39643821},
      doi          = {10.1007/s10858-024-00452-9},
      url          = {https://pub.dzne.de/record/276783},
}