@article{FolikumahBehlLendlein2021,
  author    = {Folikumah, Makafui Y. and Behl, Marc and Lendlein, Andreas},
  title     = {Reaction behaviour of peptide-based single thiol-thioesters exchange reaction substrate in the presence of externally added thiols},
  series = {MRS communications / a publication of the Materials Research Society},
  volume    = {11},
  journal   = {MRS communications / a publication of the Materials Research Society},
  number    = {4},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {2159-6859},
  doi       = {10.1557/s43579-021-00041-z},
  pages     = {402 -- 410},
  year      = {2021},
  abstract  = {Identification of patterns in chemical reaction pathways aids in the effective design of molecules for specific applications. Here, we report on model reactions with a water-soluble single thiol-thioester exchange (TTE) reaction substrate, which was designed taking in view biological and medical applications. This substrate consists of the thio-depsipeptide, Ac-Pro-Leu-Gly-SLeu-Leu-Gly-NEtSH (TDP) and does not yield foul-smelling thiol exchange products when compared with aromatic thiol containing single TTE substrates. TDP generates an alpha,omega-dithiol crosslinker in situ in a 'pseudo intramolecular' TTE. Competitive intermolecular TTE of TDP with externally added "basic" thiols increased the crosslinker concentration whilst "acidic" thiols decreased its concentration. TDP could potentially enable in situ bioconjugation and crosslinking applications.},
  language  = {en}
}
@article{MitreiterOswaldStallmach2011,
  author    = {Mitreiter, Ivonne and Oswald, Sascha and Stallmach, Frank},
  title     = {Magnetic resonance measurements of iron turn-over in sands},
  series = {Grundwasser : Zeitschrift der Fachsektion Hydrogeologie in der Deutschen Gesellschaft f{\"u}r Geowissenschaften (FH-DGG)},
  volume    = {16},
  journal   = {Grundwasser : Zeitschrift der Fachsektion Hydrogeologie in der Deutschen Gesellschaft f{\"u}r Geowissenschaften (FH-DGG)},
  number    = {4},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1430-483X},
  doi       = {10.1007/s00767-011-0177-6},
  pages     = {269 -- 278},
  year      = {2011},
  abstract  = {In this study, Nuclear Magnetic Resonance (NMR), a non-destructive measurement technique, has been applied for investigation of iron turn-over processes. In non-invasive laboratory experiments, iron dissolution and precipitation reactions in saturated natural sands were observed spatially and temporally. These processes play an important role in groundwater with varying redox and pH conditions. Redox reactions turning Fe2+ into Fe3+ and Fe3+ into Fe2+ were detected in aqueous solution by the difference in magnetic relaxation times. Furthermore, the spatial distribution of the iron reduction reaction, the consumption and diffusive transfer to and from the reaction sites, was observed in a 1D set-up with natural sands. The achieved spatial resolution was less than one millimetre while repeating measurements every half an hour. It showed the system changing from diffusion-limited to reaction-limited.},
  language  = {de}
}
@article{SowemimoKnoxBrownBorcherdsetal.2019,
  author    = {Sowemimo, Oluwakemi T. and Knox-Brown, Patrick and Borcherds, Wade and Rindfleisch, Tobias and Thalhammer, Anja and Daughdrill, Gary W.},
  title     = {Conserved Glycines Control Disorder and Function in the Cold-Regulated Protein, COR15A},
  series = {Biomolecules},
  volume    = {9},
  journal   = {Biomolecules},
  number    = {3},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2218-273X},
  doi       = {10.3390/biom9030084},
  pages     = {17},
  year      = {2019},
  abstract  = {Cold-regulated (COR) 15A is an intrinsically disordered protein (IDP) from Arabidopsis thaliana important for freezing tolerance. During freezing-induced cellular dehydration, COR15A transitions from a disordered to mostly alpha-helical structure. We tested whether mutations that increase the helicity of COR15A also increase its protective function. Conserved glycine residues were identified and mutated to alanine. Nuclear magnetic resonance (NMR) spectroscopy was used to identify residue-specific changes in helicity for wildtype (WT) COR15A and the mutants. Circular dichroism (CD) spectroscopy was used to monitor the coil-helix transition in response to increasing concentrations of trifluoroethanol (TFE) and ethylene glycol. The impact of the COR15A mutants on the stability of model membranes during a freeze-thaw cycle was investigated by fluorescence spectroscopy. The results of these experiments showed the mutants had a higher content of alpha-helical structure and the increased alpha-helicity improved membrane stabilization during freezing. Comparison of the TFE- and ethylene glycol-induced coil-helix transitions support our conclusion that increasing the transient helicity of COR15A in aqueous solution increases its ability to stabilize membranes during freezing. Altogether, our results suggest the conserved glycine residues are important for maintaining the disordered structure of COR15A but are also compatible with the formation of alpha-helical structure during freezing induced dehydration.},
  language  = {en}
}