The long-held views on lock-and-key versus induced fit in binding arose from the notion that
a protein exists in a single, most stable conformation, dictated by its sequence. However, in …

It is difficult to overstate the importance of proteinprotein interactions in biological processes.
Some of these interactions and their roles are well known, for instance, the formation of …

A comparative analysis of the main-chain conformation of the L1, L2, L3, H1 and H2
hypervariable regions in 17 immunoglobulin structures that have been accurately …

Adeno-associated viruses (AAV) are ubiquitous in the human population (> 90% of adults
are seropositive) but have never been implicated as the cause of any disease. They were …

The binding of TCRs to their peptide-MHC ligands is characterized by a low affinity, slow
kinetics, and a high degree of cross-reactivity. Here, we report the results of a kinetic and …

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

Although affinity maturation constitutes an integral part of T-dependent humoral responses,
its structural basis is less well understood. We compared the physicochemical properties of …

Whereas antibodies have demonstrated the ability to mimic various compounds, classic
heavy/light‐chain antibodies may be limited in their applications. First, they tend not to bind …

In this study, we used in vitro protein evolution with ribosome and phage display to optimize
the affinity of a human IL-13-neutralizing antibody, a therapeutic candidate for the treatment …

Abstract The immunoglobulin G1 (IgG 1) κ antibodies HyHEL-5 and HyHEL-10 interact with
nonoverlapping epitopes on hen egg lysozyme (HEL); the HyHEL-5/HEL interface has two …