title: Antibody design: beyond the natural limits.
abstract: Dissection of antibody-antigen interactions requires a knowledge of antibody structure, the ability to model accurately the conformation of antibody-combining sites, and an understanding of the energetic factors governing the interactions. When this understanding has reached the point where the molecular shape and chemical character of a combining site necessary to define a particular specificity and binding requirement can be designed, the antibody repertoire will have been extended 'beyond the natural limits'.
authors.affiliation: School of Biology and Biochemistry, University of Bath, UK.
authors.forename: A R
authors.initials: AR
authors.lastname: Rees
authors.forename: D
authors.initials: D
authors.lastname: Staunton
authors.forename: D M
authors.initials: DM
authors.lastname: Webster
authors.forename: S J
authors.initials: SJ
authors.lastname: Searle
authors.forename: A H
authors.initials: AH
authors.lastname: Henry
authors.forename: J T
authors.initials: JT
authors.lastname: Pedersen
mesh_terms: D000818:Animals; D000906:Antibodies / Q000737:chemistry* / Q000276:immunology; D000918:Antibody Specificity; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D015202:Protein Engineering
chemical_list: D000906:Antibodies