Revealing protein structures: a new method for mapping antibody epitopes

A recent idea for determining the three-dimensional structure of a protein uses antibody recognition of surface structure and random peptide libraries to map antibody epitope combining sites. Antibodies that bind to the surface of the protein of interest can be used as "witnesses" to report the structure of the protein as follows: Proteins are composed of linear polypeptide chains that come together in complex spatial folding patterns to create the native protein structures and these folded structures form the binding sites for the antibodies. Short amino acid probe sequences, which bind to the active region of each antibody, can be selected from random sequence peptide libraries. These probe sequences can often be aligned to discontinuous regions of the one-dimensional target sequence of a protein. Such alignments indicate how pieces of the protein sequence must be folded together in space and thus provide valuable long-range constraints for solving the overall 3-D structur...

• Type: Conference
• Year: 2002
• Where: RECOMB
• Authors: Brendan Mumey, Brian W. Bailey, Edward A. Dratz
• Keywords: Computational Biology, Epitope Mapping Alignment, Mapping Alignment Problem, RECOMB 2002, Valuable Long-range Constraints