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@ARTICLE{Anthuparambil:617740,
      author       = {Anthuparambil, Nimmi Das and Timmermann, Sonja and Dargasz,
                      Michelle and Retzbach, Sebastian and Senft, Maximilian D.
                      and Begam, Nafisa and Ragulskaya, Anastasia and Paulus,
                      Michael and Zhang, Fajun and Westermeier, Fabian and Sprung,
                      Michael and Schreiber, Frank and Gutt, Christian},
      title        = {{S}alt induced slowdown of kinetics and dynamics during
                      thermal gelation of egg-yolk},
      journal      = {The journal of chemical physics},
      volume       = {161},
      number       = {5},
      issn         = {0021-9606},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {PUBDB-2024-07018},
      pages        = {055102},
      year         = {2024},
      note         = {DFG (Grant No. NFDI 40/1)},
      abstract     = {We investigated the effect of the NaCl concentration
                      (0.3–2M) on the structure and dynamics of hen egg yolk at
                      room temperature andduring thermal gelation at temperatures
                      in the range of 66–90 ○C utilizing low-dose x-ray photon
                      correlation spectroscopy in ultra-smallangle x-ray
                      scattering geometry. With an increase in the salt
                      concentration, we observe progressive structural and dynamic
                      changes at roomtemperature, indicating the disruption of
                      yolk components such as yolk-granules and yolk-plasma
                      proteins. Temperature- and salt-dependentstructural and
                      dynamic investigations suggest a delay in the gel formation
                      and aggregation of yolk low-density lipoproteins with
                      increasingionic strength. However, the time–temperature
                      superposition relationship observed in all samples suggests
                      an identical mechanism underlyingprotein
                      aggregation–gelation with a temperature-dependent reaction
                      rate. The sol–gel transition time extracted from kinetic
                      and dynamicinformation follows Arrhenius’s behavior, and
                      the activation energy (460 kJ/mol) is found to be
                      independent of the salt concentration.},
      cin          = {FS-PETRA-S / DOOR ; HAS-User},
      ddc          = {530},
      cid          = {I:(DE-H253)FS-PETRA-S-20210408 /
                      I:(DE-H253)HAS-User-20120731},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / 05K19PS1 - Instrumentierung, um die Dynamik von
                      biologischen Proben mit Korrelationsspektroskopie zu messen.
                      (BMBF-05K19PS1) / 05K20PSA - Verbundprojekt 05K2020 -
                      2019-06075 Protein-Dyn: Dynamik von Proteinen in Lösungen
                      auf multiplen Längen und Zeitskalen (Teilprojekt 1)
                      (BMBF-05K20PSA) / 05K22PS1 - Schnelle
                      Korrelationsspektroskopie an der ESRF-EBS (BMBF-05K22PS1) /
                      05K20VTA - Verbundprojekt 05K2020 - 2019-06075 Protein-Dyn:
                      Dynamik von Proteinen in Lösungen auf multiplen Längen und
                      Zeitskalen (Teilprojekt 2) (BMBF-05K20VTA) / FS-Proposal:
                      II-20210008 (II-20210008)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      G:(DE-Ds200)BMBF-05K19PS1 / G:(DE-Ds200)BMBF-05K20PSA /
                      G:(DE-Ds200)BMBF-05K22PS1 / G:(DE-Ds200)BMBF-05K20VTA /
                      G:(DE-H253)II-20210008},
      experiment   = {EXP:(DE-H253)P-P10-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39105556},
      UT           = {WOS:001297911300003},
      doi          = {10.1063/5.0219004},
      url          = {https://bib-pubdb1.desy.de/record/617740},
}