Robust Quantitative Modeling of Peptide Binding Affinities for MHC Molecules Using Physical-Chemical Descriptors. Ivanciuc, O. & Braun, W. Prot.~Pep.~Lett., 14:903--916, 2007.
abstract   bibtex   
Major histocompatibility complex (MHC) molecules bind short peptides resulting from intracellular processing of foreign and self proteins, and present them on the cell surface for recognition by T-cell receptors. We propose a new robust approach to quantitatively model the binding affinities of MHC molecules by quantitative structure-activity relationships (QSAR) that use the physical-chemical amino acid descriptors E-1-E-5. These QSAR models are robust, sequence-based, and can be used as a fast and reliable filter to predict the MHC binding affinity for large protein databases.
@article{Ivanciuc:2007aa,
	Abstract = {Major histocompatibility complex (MHC) molecules bind short peptides resulting from intracellular processing of foreign and self proteins, and present them on the cell surface for recognition by T-cell receptors. We propose a new robust approach to quantitatively model the binding affinities of MHC molecules by quantitative structure-activity relationships (QSAR) that use the physical-chemical amino acid descriptors E-1-E-5. These QSAR models are robust, sequence-based, and can be used as a fast and reliable filter to predict the MHC binding affinity for large protein databases.},
	Author = {Ivanciuc, Ovidiu and Braun, Werner},
	Date-Added = {2008-05-01 17:08:12 -0400},
	Date-Modified = {2008-05-01 17:10:11 -0400},
	Journal = {Prot.~Pep.~Lett.},
	Keywords = {qsar; filter; major histocompatibility complex; peptide binding affinity; quantitative structure-activity relationships; amino acid descriptors},
	Pages = {903--916},
	Timescited = {0},
	Title = {Robust Quantitative Modeling of Peptide Binding Affinities for {MHC} Molecules Using Physical-Chemical Descriptors},
	Volume = {14},
	Year = {2007}}

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