New PDF release: Advances in Immunology

By Frank J. Dixon (Eds.)

ISBN-10: 0120224437

ISBN-13: 9780120224432

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Extra info for Advances in Immunology

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1986b), hydrophobic (carbon) or hydrophilic (noncarbon) atoms, and side-chain or main-chain atoms. 4 A) probe sphere. Exposed sidechain area is expressed as a percentage for hydrophobic (carbon), hydrophilic (noncarbon), or all side-chain atom surface area, exposed in the context of the protein structure, calculated from the total side-chain surface area in the absence of neighboring protein residues (Shrake and Rupley, 1973). [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.

1986). , 1988) and unpublished results (E. A. Padlan, E. W. Silverton, S. Sheriff, G. H. Cohen, S. Smith-Gill, and D. R. Davies) from X-ray diffraction studies of these antibodies in antibody-lysozyme complexes (H. M. Geysen and S. J. Smith-Gill, unpublished results). Although preliminary, the peptide mapping results identified the unpublished HyHELlO site and correctly suggested the involvement of Trp and Arg in the complex. , 1982). In principle, the characterization of critical residues, originally studied by peptide mapping and comprehensive single-residue substitution in peptides (see Sections IV and V), can be done in the context of the native protein fold, using cloning and site-directed mutation methods.

Cohen, S. Smith-Gill, and D. R. Davies) from X-ray diffraction studies of these antibodies in antibody-lysozyme complexes (H. M. Geysen and S. J. Smith-Gill, unpublished results). Although preliminary, the peptide mapping results identified the unpublished HyHELlO site and correctly suggested the involvement of Trp and Arg in the complex. , 1982). In principle, the characterization of critical residues, originally studied by peptide mapping and comprehensive single-residue substitution in peptides (see Sections IV and V), can be done in the context of the native protein fold, using cloning and site-directed mutation methods.

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Advances in Immunology by Frank J. Dixon (Eds.)


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