TY  - JOUR
A1  - Pfeil, Wolfgang
T1  - Partly folded proteins (Minireview)
Y1  - 1998
SN  - 0320-9725
ER  - 
TY  - JOUR
A1  - Jung, Christiane
A1  - Pfeil, Wolfgang
A1  - Köpke, Karla
A1  - Schulze, Heike
A1  - Ristau, Otto
T1  - Conformational states and substates of cytochrome P450cam - insight in protein dynamics and folding
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Schubert, Dieter
A1  - Schluckebier, Gerd
A1  - Backmann, Jan
A1  - Granzien, Joachim
A1  - Kisker, Caroline
A1  - Choe, Hui-Woog
A1  - Hahn, Ulrich
A1  - Pfeil, Wolfgang
A1  - Saenger, Wolfram
T1  - X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59Tyr in ribonuclease T1
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Pfeil, Wolfgang
T1  - Thermodynamische Untersuchungen an Proteinen
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Pfeil, Wolfgang
A1  - Gesierich, Ulrike
A1  - Sterner, Reinhard
T1  - The 4Fe-4S ferredoxin from thermotoga maritima is extremely thermostable
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Pfeil, Wolfgang
T1  - Native-like intermediates in protein folding
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Damaschun, Gregor
A1  - Damaschun, Hilde
A1  - Gast, Klaus
A1  - Misselwitz, Rolf
A1  - Müller, Jürgen J.
A1  - Pfeil, Wolfgang
A1  - Zirwer, Dietrich
T1  - Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast
Y1  - 1993
ER  - 
TY  - BOOK
A1  - Pfeil, Wolfgang
T1  - Protein stability and folding : a collecton of thermodynamic data ; Supplement 1
Y1  - 2001
SN  - 3-540-42168-8
PB  - Springer
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Koroljova, Olga V.
A1  - Stepanova, Elena V.
A1  - Binukov, Vladimir I.
A1  - Timofeev, Vladimir P.
A1  - Pfeil, Wolfgang
T1  - Temperature-induced changes in copper centers and protein conformation of two fungal laccases from Coriolus hirsutus and Coriolus zonatus
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Freiberg, Alexander
A1  - Machner, M. P.
A1  - Pfeil, Wolfgang
A1  - Schubert, W. D.
A1  - Heinz, Dirk W.
A1  - Seckler, Robert
T1  - Folding and stability of the leucine-rich repeat domain of internalin B from Listeria monocytogenes
N2  - 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
Y1  - 2004
SN  - 0022-2836
ER  -