By Frank J. Dixon (Eds.)
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Adapted from Geysen et al. ] ANTIBODY BINDING TO PROTEIN ANTIGENS 35 temperature factor minima correspond to reactivities with at most one antiserum and titers of less than 500. The peak in reactivity near hexapeptide 54 falls in a local mobility minimum, but this region remains more mobile than the global minima near hexapeptides 27 and 102. The packing density profile (inverted), although more serrated, resembles the overall mobility profile; the major differences are an additional minimum near hexapeptide 13, and a shift in C-terminal peak.
In addition, proteins with both solved threedimensional structures and defined epitopes are often highly conserved among different species and may thus produce limited immunological responses in experimental animals. It is axiomatic that an understanding of complex systems, whether the interactions of atoms or macromolecules, depends on the ability to ask the specific experimental questions that address a single, unknown 28 ELIZABETH D. GETZOFF ET A L . variable. In much of immunology, experiments involve complex systems containing many different variables, which can be difficult to define and impossible to eliminate.
Raster color graphics images of opposing sides of the solid external molecular surface of MHr show t h a t the most highly reactive surface regions form superassemblies (three-dimensional clusters) that wrap around one side (left view) of the protein and almost connect on the other side (right view). The four whelices are oriented vertically, with the two-iron active site near the top. [Adapted from Geysen et al. ] FIG. 10. Stereochemistry, mechanism, and critical residues of MHr site 4-9. (A) The spatial relationship and interactions of critical side chains for MHr site 4-9, Ile-Pro-Glu-Pro-Tyr-Val,of the N-terminal loop are viewed in a slice through the MHr atomic model (isolated by clipping planes) as displayed on computer graphics.