Affiliation: University of Bayreuth
- Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structurePhilipp Neudecker
Lehrstuhl für Biopolymere, Universitaet Bayreuth, Universitatsstrasse 30, 95440 Bayreuth, Germany
Biochem J 376:97-107. 2003....
- Solution structure, dynamics, and hydrodynamics of the calcium-bound cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric two EF-hand assembly with a regulatory functionPhilipp Neudecker
Lehrstuhl für Biopolymere, Universitat Bayreuth, D 95440 Bayreuth, Germany
J Mol Biol 336:1141-57. 2004..Together with the close structural homology to calmodulin and the hydrophobic ligand binding groove this transition suggests a regulatory function for Bet v 4...
- Solution structure of human proguanylin: the role of a hormone prosequenceThomas Lauber
Lehrstuhl für Biopolymere, Universitat Bayreuth, Universitatstrasse 30, 95447 Bayreuth, Germany
J Biol Chem 278:24118-24. 2003....
- A novel approach for investigation of specific and cross-reactive IgE epitopes on Bet v 1 and homologous food allergens in individual patientsDiana Mittag
Allergy Unit, Department of Dermatology, University Hospital Zurich, Switzerland
Mol Immunol 43:268-78. 2006..Moreover, patterns of IgE reactivity may be patient-specific. The aim of our study was to compare specific and cross-reactive IgE epitopes and epitope patterns between individual patients. We used Bet v 1-related food allergy as a model...
- Sequence-specific 1H, 13C and 15N resonance assignments of Ara h 6, an allergenic 2S albumin from peanutKatrin Lehmann
J Biomol NMR 29:93-4. 2004
- High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2Katrin Lehmann
Lehrstuhl Biopolymere, Universität Bayreuth 30, Universitaetsstrasse 30, 95440, Bayreuth, Germany
Protein Expr Purif 31:250-9. 2003..It could be shown that recombinant Ara h 2, thus overexpressed and purified, and the allergen isolated from peanuts are identical as judged from immunoblotting, analytical HPLC, and circular dichroism spectra...
- Sequence-specific 1H, 13C and 15N resonance assignments of SAM22, an allergenic stress-induced protein from soy beanPhilipp Neudecker
J Biomol NMR 26:191-2. 2003
- Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domainPhilipp Neudecker
Department of Medical Genetics, University of Toronto, ON, Canada
J Biomol NMR 34:129-35. 2006....
- Abp1p and Fyn SH3 domains fold through similar low-populated intermediate statesDmitry M Korzhnev
Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada, M5S 1A8
Biochemistry 45:10175-83. 2006....
- Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopyPhilipp Neudecker
Departments of Medical Genetics and Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8
J Mol Biol 363:958-76. 2006....
- Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopyPhilipp Neudecker
Department of Medical Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8
Proc Natl Acad Sci U S A 104:15717-22. 2007..The results further support the notion that on-pathway intermediates can be stabilized by nonnative contacts...
- Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do?D Flemming Hansen
Department of Medical Genetics, University of Toronto, Toronto, Ontario, Canada, M5S 1A8
J Am Chem Soc 130:2667-75. 2008..The accuracy of the extracted chemical shifts opens up the possibility of obtaining quantitative structural information of invisible states of the sort that is now available from chemical shifts recorded on ground states of proteins...
- Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingArash Zarrine-Afsar
Department of Biochemistry, University of Toronto, Toronto, ON, Canada
Proc Natl Acad Sci U S A 105:9999-10004. 2008..Moreover, we show that a coarse-grained model with a simple consideration of hydrophobicity is sufficient for the accurate prediction of kinetically important nonnative interactions...