@article{Pfeil1998,
  author    = {Pfeil, Wolfgang},
  title     = {Partly folded proteins (Minireview)},
  issn      = {0320-9725},
  year      = {1998},
  language  = {en}
}
@article{JungPfeilKoepkeetal.1994,
  author    = {Jung, Christiane and Pfeil, Wolfgang and K{\"o}pke, Karla and Schulze, Heike and Ristau, Otto},
  title     = {Conformational states and substates of cytochrome P450cam - insight in protein dynamics and folding},
  year      = {1994},
  language  = {en}
}
@article{SchubertSchluckebierBackmannetal.1994,
  author    = {Schubert, Dieter and Schluckebier, Gerd and Backmann, Jan and Granzien, Joachim and Kisker, Caroline and Choe, Hui-Woog and Hahn, Ulrich and Pfeil, Wolfgang and Saenger, Wolfram},
  title     = {X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59Tyr in ribonuclease T1},
  year      = {1994},
  language  = {en}
}
@article{Pfeil1996,
  author    = {Pfeil, Wolfgang},
  title     = {Thermodynamische Untersuchungen an Proteinen},
  year      = {1996},
  language  = {de}
}
@article{PfeilGesierichSterner1996,
  author    = {Pfeil, Wolfgang and Gesierich, Ulrike and Sterner, Reinhard},
  title     = {The 4Fe-4S ferredoxin from thermotoga maritima is extremely thermostable},
  year      = {1996},
  language  = {en}
}
@article{Pfeil1994,
  author    = {Pfeil, Wolfgang},
  title     = {Native-like intermediates in protein folding},
  year      = {1994},
  language  = {en}
}
@article{DamaschunDamaschunGastetal.1993,
  author    = {Damaschun, Gregor and Damaschun, Hilde and Gast, Klaus and Misselwitz, Rolf and M{\"u}ller, J{\"u}rgen J. and Pfeil, Wolfgang and Zirwer, Dietrich},
  title     = {Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast},
  year      = {1993},
  language  = {en}
}
@book{Pfeil2001,
  author    = {Pfeil, Wolfgang},
  title     = {Protein stability and folding : a collecton of thermodynamic data ; Supplement 1},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {3-540-42168-8},
  pages     = {XIV, 521 S.},
  year      = {2001},
  language  = {en}
}
@article{KoroljovaStepanovaBinukovetal.2001,
  author    = {Koroljova, Olga V. and Stepanova, Elena V. and Binukov, Vladimir I. and Timofeev, Vladimir P. and Pfeil, Wolfgang},
  title     = {Temperature-induced changes in copper centers and protein conformation of two fungal laccases from Coriolus hirsutus and Coriolus zonatus},
  year      = {2001},
  language  = {en}
}
@article{FreibergMachnerPfeiletal.2004,
  author    = {Freiberg, Alexander and Machner, M. P. and Pfeil, Wolfgang and Schubert, W. D. and Heinz, Dirk W. and Seckler, Robert},
  title     = {Folding and stability of the leucine-rich repeat domain of internalin B from Listeria monocytogenes},
  issn      = {0022-2836},
  year      = {2004},
  abstract  = {Internalin B (InlB), a surface protein of the human pathogen Listeria monocytogenes, promotes invasion into various host cell types by inducing phagocytosis of the entire bacterium. The N-terminal half of InlB (residues 36-321, InlB(321)), which is sufficient for this process, contains a central leucine-rich repeat (LRR) domain that is flanked by a small a-helical cap 2 and an immunoglobulin (Ig)-like domain. Here we investigated the variant lacking the Ig-like domain (lnlB(248)). The circular dichroism spectra of both protein variants in the far ultraviolet region are very similar, with a characteristic minimum found at similar to200 nm, possibly resulting from the high 3(10)-helical content in the LRR domain. Upon addition of chemical denaturants, both variants unfold in single transitions with unusually high cooperativity that are fully reversible and best described by two-state equilibria. The free energies of GdmCl-induced unfolding determined from transitions at 20degreesC are 9.9(+/- 0.8)kcal/mol for InlB(321) and 5.4(+/- 0.4) kcal/mol for InlB(248). InlB(321) is also more stable against thermal denaturation, as observed by scanning calorimetry. This suggests, that the Ig-like domain, which presumably does not directly interact with the host cell receptor during bacterial invasion, plays a critical role for the in vivo stability of InlB. (C) 2004 Elsevier Ltd. All rights reserved},
  language  = {en}
}