With the numerous detailed molecular descriptions of antibody-antigen interfaces, the
structural study of these molecular interactions has evolved from an attempt to understand …

Motivation: Empirical models for the prediction of how changes in sequence alter protein–
protein binding kinetics and thermodynamics can garner insights into many aspects of …

HLAMatchmaker is a structurally based matching program. Each HLA antigen is viewed as a
string of epitopes represented by short sequences (triplets) involving polymorphic amino …

Using site‐directed mutagenesis, x‐ray crystallograpby, micro‐calorimetric, equilibrium
sedimentation and surface plasmon resonance detection techniques, we have examined the …

We present an analysis of the water molecules immobilized at the protein–protein interfaces
of 115 homodimeric proteins and 46 protein–protein complexes, and compare them with …

The structure of the hemagglutinin (HA) of a mutant influenza virus that escapes
neutralization by a monoclonal antibody shows that the mutation causes changes in HA …

Alanine scanning mutagenesis, double mutant cycles, and X-ray crystallography were used
to characterize the interface between the anti-hen egg white lysozyme (HEL) antibody D1. 3 …

Abstract Antibodies HyHEL8, HyHEL10, and HyHEL26 (HH8, HH10, and HH26,
respectively) recognize highly overlapping epitopes on hen egg-white lysozyme (HEL) with …

Antigen-dependent activation of T lymphocytes requires T cell receptor (TCR)-mediated
recognition of specific peptides, together with the MHC molecules to which they are bound …

Dimers of CH3 domains from human IgG1 were used to study the effect of mutations
constructed at a domain− domain interface upon domain dissociation and …