@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}
}
@article{PfeilNoeltingJung1993,
  author    = {Pfeil, Wolfgang and N{\"o}lting, Bengt and Jung, Christiane},
  title     = {Thermodynmic properties of apocytochrome P450cam},
  year      = {1993},
  language  = {en}
}
@article{Pfeil1993,
  author    = {Pfeil, Wolfgang},
  title     = {Thermodynamics of apocytochrome b5 unfolding},
  year      = {1993},
  language  = {en}
}
@article{PfeilNoeltingJung1993,
  author    = {Pfeil, Wolfgang and N{\"o}lting, Bengt and Jung, Christiane},
  title     = {Apocytochrome P450cam is a native protein with some intermediate-like properties},
  year      = {1993},
  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{Pfeil1994,
  author    = {Pfeil, Wolfgang},
  title     = {Native-like intermediates in protein folding},
  year      = {1994},
  language  = {en}
}
@article{GastDamaschunDesmadriletal.1995,
  author    = {Gast, Klaus and Damaschun, Gregor and Desmadril, Michel and Minard, Philippe and M{\"u}ller-Frohne, Marlies and Pfeil, Wolfgang and Zirwer, Dietrich},
  title     = {Cold denaturation of yeast phosphoglycerate kinase : which domain is more stable?},
  year      = {1995},
  language  = {en}
}
@article{LaschZellmerPfeiletal.1995,
  author    = {Lasch, J{\"u}rgen and Zellmer, Sebastian and Pfeil, Wolfgang and Schubert, Rolf},
  title     = {Interaction of liposomes with the human skin lipid barrier : hSCLLs as model system - DSC of intact stratum corneum and in situ CLSM of human skin},
  year      = {1995},
  language  = {en}
}
@article{DudichZavylovPfeiletal.1995,
  author    = {Dudich, Igor V. and Zav`ylov, Vladimir and Pfeil, Wolfgang and Gaestel, Matthias and Zav`yalova, Galina A. and Denesyuk, Alexandr I. and Korpela, Timo},
  title     = {Dimer structure as a minimum cooperative subunit of small heat shock-proteins},
  year      = {1995},
  language  = {en}
}
@article{ZellmerPfeilLasch1995,
  author    = {Zellmer, Sebastian and Pfeil, Wolfgang and Lasch, J{\"u}rgen},
  title     = {Interaction of phosphatidylcholine liposomes with the human stratum corneum},
  year      = {1995},
  language  = {en}
}
@article{BurovaBernhardtPfeil1995,
  author    = {Burova, Tatjana V. and Bernhardt, Rita and Pfeil, Wolfgang},
  title     = {Conformational stability of holo and apo adrenodoxin : a scanning calorimetric study},
  year      = {1995},
  language  = {en}
}
@article{BurovaBeckertUhlmannetal.1996,
  author    = {Burova, Tatjana V. and Beckert, Vita and Uhlmann, Heike and Ristau, Otto and Bernhardt, Rita and Pfeil, Wolfgang},
  title     = {Conformational stability of adrenodoxin mutant proteins},
  year      = {1996},
  language  = {en}
}
@article{PfeilBurovaBeckertetal.1996,
  author    = {Pfeil, Wolfgang and Burova, Tatjana V. and Beckert, Vita and Uhlmann, Heike and Ristau, Otto and Bernhardt, Rita},
  title     = {Conformational stability of adrenodoxin mutant proteins},
  year      = {1996},
  language  = {en}
}
@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{Pfeil1996,
  author    = {Pfeil, Wolfgang},
  title     = {Thermodynamische Untersuchungen an Proteinen},
  year      = {1996},
  language  = {de}
}
@article{GesierichPfeil1996,
  author    = {Gesierich, Ulrike and Pfeil, Wolfgang},
  title     = {The conformational stability of - crystallin is rather low : calorimetric results},
  year      = {1996},
  language  = {en}
}
@article{SchwarzKisselePfeiletal.1997,
  author    = {Schwarz, D. and Kissele, P. and Pfeil, Wolfgang and Pisch, S. and Bornscheuer, U. and Schmid, Rolf D.},
  title     = {Evidence that nonbilayer phase probensity of the membrane is important for thr side chain cleavage of cytochrome P450SCC (CYP11A1)},
  year      = {1997},
  language  = {en}
}
@article{PfeilGesierichKleemannetal.1997,
  author    = {Pfeil, Wolfgang and Gesierich, Ulrike and Kleemann, G. R. and Sterner, Reinhard},
  title     = {Ferredoxin from the hyperthermophiele thermotoga maritima os stable beyond the boiling point of watter},
  year      = {1997},
  language  = {en}
}
@article{Pfeil1998,
  author    = {Pfeil, Wolfgang},
  title     = {Partly folded proteins (Minireview)},
  issn      = {0320-9725},
  year      = {1998},
  language  = {en}
}
@article{GoderBeckertPfeiletal.1998,
  author    = {Goder, V. and Beckert, Vita and Pfeil, Wolfgang and Bernhardt, Rita},
  title     = {Impact of the presequence of a mitochondrium targeted precursor, preadrenodoxin, on folding, catalytic activity and stability of the protein in vitro},
  year      = {1998},
  language  = {en}
}
@article{Pfeil1998,
  author    = {Pfeil, Wolfgang},
  title     = {Is the molten globule a third thermodynamic state of protein? : the exemplare of {\`a}-Lactalbumin},
  year      = {1998},
  language  = {en}
}
@article{RishiAnjumAhmadetal.1998,
  author    = {Rishi, Vikas and Anjum, Farah and Ahmad, Faizan and Pfeil, Wolfgang},
  title     = {Role of non-compatible osmolytes in the stabilization of proteins during heat stress},
  year      = {1998},
  language  = {en}
}
@book{Pfeil1998,
  author    = {Pfeil, Wolfgang},
  title     = {Protein stability and folding : a collection of thermodynamic data},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {3-540-63717-6},
  pages     = {XII, 656 S.: {\"u}berw. Tab., 7 Ill.},
  year      = {1998},
  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{BaxaCooperWeintraubetal.2001,
  author    = {Baxa, Ulrich and Cooper, Alan and Weintraub, N. and Pfeil, Wolfgang and Seckler, Robert},
  title     = {Enthalpic barriers to the hydrophobic binding of oligosaccharides to phage P22 tailspike protein},
  year      = {2001},
  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{Pfeil2002,
  author    = {Pfeil, Wolfgang},
  title     = {The influence of glycosylation on the thermal stability of ribonuclease},
  year      = {2002},
  language  = {en}
}
@article{RoskeSunnaPfeiletal.2004,
  author    = {Roske, Y. and Sunna, A. and Pfeil, Wolfgang and Heinemann, Udo},
  title     = {High-resolution crystal structures of Caldiceflulosiruptor strain Rt8B.4 carbohydrate-binding module CBM27-1 and its complex with mannohexaose},
  issn      = {0022-2836},
  year      = {2004},
  abstract  = {Carbohydrate-binding modules (CBMs) are the most common non-catalytic modules associated with enzymes active in plant cell-wall hydrolysis. Despite the large number of putative CBMs being identified by amino acid sequence alignments, only few representatives have been experimentally shown to have a carbohydrate-binding function. Caldicellulosiruptor strain Rt8B.4 Man26 is a thermostable modular glycoside hydrolase beta-mannanase which contains two non-catalytic modules in tandem at its N terminus. These modules were recently shown to function primarily as beta- mannan-binding modules and have accordingly been classified as members of a novel family of CBMs, family 27. The N- terminal CBM27 (CsCBM27-1) of Man26 from Caldicellulosiruptor Rt8B.4 displays high-binding affinity towards mannohexaose with a K-a of 1 x 10(7) M-1. Accordingly, the high-resolution crystal structures of CsCBM27-1 native and its mannohexaose complex were solved at 1.55 Angstrom and 1.06 Angstrom resolution, respectively. In the crystal, CsCBM27-1 shows the typical beta-sandwich jellyroll fold observed in other CBMs with a single metal ion bound, which was identified as calcium. The crystal structures reveal that the overall fold of CsCBM27-1 remains virtually unchanged upon sugar binding and that binding is mediated by three solvent-exposed tryptophan residues and few direct hydrogen bonds. Based on binding affinity and thermal unfolding experiments this structural calcium is shown to play a role in the thermal stability of CsCBM27-1 at high temperatures. The higher binding affinity of CsCBM27-1 to mannooligosaccharides when compared to other members of CBM family 27 might be explained by the different orientation of the residues forming the "aromatic platform" and by differences in the length of loops. Finally, evidence is presented, on the basis of fold similarities and the retention of the position of conserved motifs and a calcium ion, for the consolidation of related CBM families into a superfamily of CBMs. (C) 2004 Elsevier Ltd. All rights reserved},
  language  = {en}
}
@article{KrylovPfeilLisdat2004,
  author    = {Krylov, Andrey V. and Pfeil, Wolfgang and Lisdat, Fred},
  title     = {Denaturation and renaturation of cytochrome c immobilized on gold electrodes in DMSO-containing buffers},
  year      = {2004},
  abstract  = {Cytochrome c (cyt c) was immobilized on surface-modified gold electrodes using a self-assembling approach. The resulting cyt c electrode was studied using cyclic voltammetry. Compared to pure phosphate buffer, cyt c electrodes exhibited in DMSO-containing solutions lower oxidation and reduction peak currents, which originated from a decrease in the addressable electro-active amount of the surface-immobilized protein. This is associated with the process of protein denaturation. The denaturation kinetics can be described by a sum of two processes with time constants differing by more than one order of magnitude. The subsequent change of the aqueous/organic medium back to a pure aqueous buffer resulted in a shift of the formal potential to its initial value and a partial recovery of the peak current. This can be attributed to the renaturation of the cyt c. The extent of renaturation depended on the organic solvent/water ratio of the mixture used. The kinetics of protein renaturation were similar to those of the denaturation process. (C) 2004 Elsevier B.V. All rights reserved},
  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}
}