Protein Structure Theory Group
INSTITUTE OF BIOCHEMISTRY - CHARITÉ HUMBOLDT UNIVERSITY BERLIN
INSTITUTE OF BIOCHEMISTRY - CHARITÉ HUMBOLDT UNIVERSITY BERLIN
It is our goal to describe the time-resolved digestion of model peptides by the proteasome via simple mathematical models. The model parameter values gathered this way can be used for comparing different types of proteasomes, especially for the comparison immuno- vs. constitutive proteasome. Our main focus of attentien are differences in cut sites and processing speed of various peptide fragments.
My goal is to provide computational tools to predict the efficiency of individual steps in the MHC-I antigen processing and presentation pathway. Currently this is realized for the transport of peptides into the ER by TAP and binding of peptides to MHC-I molecules, implemented at www.mhc-pathway.net. In the future I hope to add predictions of proteasomal cleavage.
Peters, B., Janek, K., Kuckelkorn, U. and Holzhütter, H.-G. Assessment of proteasomal cleavage probabilities from kinetic analysis of time-dependent product formation. J. Mol. Biol. 318, 847-862 (2002) [abstract]
Peters, B. and Holzhütter, H.-G. In vitro phototoxicity testing: Development and validation of a new concentration response analysis software and biostatistical analyes relates to the use of various prediction models. ATLA 30, 415-432 (2002) [abstract]
Peters B, Tong W, Sidney J, Sette A and Weng Z. Examining the Independent Binding Assumption for Binding of Peptide Epitopes to MHC-I Molecules. Bioinformatics, accepted for publication.
Peters B, Bulik S, Tampe R, van Endert PM, and Holzhütter HG. Identifying MHC-I epitopes by predicting the TAP transport efficiency of epitope precursors. Submitted to J Immunol.
Last modified: Wed May 07 13:34:32 CET 2003