@article{PopovaHundertmarkSeckleretal.2011,
  author    = {Popova, Antoaneta V. and Hundertmark, Michaela and Seckler, Robert and Hincha, Dirk K.},
  title     = {Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes},
  series = {Biochimica et biophysica acta : Biomembranes},
  volume    = {1808},
  journal   = {Biochimica et biophysica acta : Biomembranes},
  number    = {7},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2736},
  doi       = {10.1016/j.bbamem.2011.03.009},
  pages     = {1879 -- 1887},
  year      = {2011},
  abstract  = {Dehydration stress-related late embryogenesis abundant (LEA) proteins have been found in plants, invertebrates and bacteria. Most LEA proteins are unstructured in solution, but some fold into amphipathic a-helices during drying. The Pfam LEA_4 (Group 3) protein LEA7 from the higher plant Arabidopsis thaliana was predicted to be 87\% alpha-helical, while CD spectroscopy showed it to be largely unstructured in solution and only 35\% alpha-helical in the dry state. However, the dry protein contained 15\% beta-sheets. FTIR spectroscopy revealed the (beta-sheets to be largely due to aggregation. beta-Sheet content was reduced and alpha-helix content increased when LEA7 was dried in the presence of liposomes with secondary structure apparently influenced by lipid composition. Secondary structure was also affected by the presence of membranes in the fully hydrated state. A temperature-induced increase in the flexibility of the dry protein was also only observed in the presence of membranes. Functional interactions of LEA7 with membranes in the dry state were indicated by its influence on the thermotropic phase transitions of the lipids and interactions with the lipid headgroup phosphates.},
  language  = {en}
}
@article{HoeferDiLellaDahmanietal.2019,
  author    = {H{\"o}fer, C. T. and Di Lella, S. and Dahmani, Ismail and Jungnick, N. and Bordag, N. and Bobone, Sara and Huang, Q. and Keller, S. and Herrmann, A. and Chiantia, Salvatore},
  title     = {Structural determinants of the interaction between influenza A virus matrix protein M1 and lipid membranes},
  series = {Biochimica et biophysica acta : Biomembranes},
  volume    = {1861},
  journal   = {Biochimica et biophysica acta : Biomembranes},
  number    = {6},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2736},
  doi       = {10.1016/j.bbamem.2019.03.013},
  pages     = {1123 -- 1134},
  year      = {2019},
  abstract  = {Influenza A virus is a pathogen responsible for severe seasonal epidemics threatening human and animal populations every year. One of the ten major proteins encoded by the viral genome, the matrix protein M1, is abundantly produced in infected cells and plays a structural role in determining the morphology of the virus. During assembly of new viral particles, M1 is recruited to the host cell membrane where it associates with lipids and other viral proteins. The structure of M1 is only partially known. In particular, structural details of M1 interactions with the cellular plasma membrane as well as M1 protein interactions and multimerization have not been clarified, yet. In this work, we employed a set of complementary experimental and theoretical tools to tackle these issues. Using raster image correlation, surface plasmon resonance and circular dichroism spectroscopies, we quantified membrane association and oligomerization of full-length M1 and of different genetically engineered M1 constructs (i.e., N- and C-terminally truncated constructs and a mutant of the polybasic region, residues 95-105). Furthermore, we report novel information on structural changes in M1 occurring upon binding to membranes. Our experimental results are corroborated by an all-atom model of the full-length M1 protein bound to a negatively charged lipid bilayer.},
  language  = {en}
}
@article{HundertmarkPopovaRauschetal.2012,
  author    = {Hundertmark, Michaela and Popova, Antoaneta V. and Rausch, Saskia and Seckler, Robert and Hincha, Dirk K.},
  title     = {Influence of drying on the secondary structure of intrinsically disordered and globular proteins},
  series = {Biochemical and biophysical research communications},
  volume    = {417},
  journal   = {Biochemical and biophysical research communications},
  number    = {1},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0006-291X},
  doi       = {10.1016/j.bbrc.2011.11.067},
  pages     = {122 -- 128},
  year      = {2012},
  abstract  = {Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.},
  language  = {en}
}