PUB - Publikationen an der Universität Bielefeld

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• [6]
  

  2018 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2931091

  Ihalainen, J. A., Gustavsson, E., Schröder, L., Donnini, S., Lehtivuori, H., Isaksson, L., Thöing, C., Modi, V., Berntsson, O., Stucki-Buchli, B., et al. (2018). Chromophore–Protein Interplay during the Phytochrome Photocycle Revealed by Step-Scan FTIR Spectroscopy. Journal of the American Chemical Society 140, 12396-12404.

  PUB | DOI | WoS | PubMed | Europe PMC
   
• [5]
  

  2015 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2752305

  Thöing, C., Oldemeyer, S., and Kottke, T. (2015). Microsecond Deprotonation of Aspartic Acid and Response of the α/β Subdomain Precede C-Terminal Signaling in the Blue Light Sensor Plant Cryptochrome. Journal of the American Chemical Society 137, 5990-5999.

  PUB | DOI | WoS | PubMed | Europe PMC
   
• [4]
  

  2014 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2664510

  Spexard, M., Thöing, C., Beel, B., Mittag, M., and Kottke, T. (2014). Response of the Sensory Animal-like Cryptochrome aCRY to Blue and Red Light As Revealed by Infrared Difference Spectroscopy. Biochemistry 53, 1041-1050.

  PUB | DOI | WoS | PubMed | Europe PMC
   
• [3]
  

  2013 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2564098

  Thöing, C., Pfeifer, A., Kakorin, S., and Kottke, T. (2013). Protonated triplet-excited flavin resolved by step-scan FTIR spectroscopy: implications for photosensory LOV domains. Physical chemistry chemical physics : PCCP 15, 5916-5926.

  PUB | DOI | WoS | PubMed | Europe PMC
   
• [2]
  

  2011 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2373405

  Spexard, M., Immeln, D., Thöing, C., and Kottke, T. (2011). Infrared spectrum and absorption coefficient of the cofactor flavin in water. VIBRATIONAL SPECTROSCOPY 57, 282-287.

  PUB | DOI | WoS
   
• [1]
  

  2011 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2317316

  Thoms, S., Hofhuis, J., Thöing, C., Gartner, J., and Niemann, H. (2011). The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization. Journal of Structural Biology 175, 362-371.

  PUB | DOI | WoS | PubMed | Europe PMC