2021/01/01 by Monica L. Fernández‐Quintero, Guy Georges, János Varga +1 · 1 citation
Medicine · Biochemistry, Genetics and Molecular Biology · #Monoclonal and Polyclonal Antibodies Research #Protein purification and stability #Glycosylation and Glycoproteins Research
paper · pdf · doi:10.1080/19420862.2021.1923122
openalex publication_date 2021/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
The rise of antibodies as a promising and rapidly growing class of biotherapeutic proteins has motivated numerous studies to characterize and understand antibody structures. In the past decades, the number of antibody crystal structures increased substantially, which revolutionized the atomistic understanding of antibody functions. Even though numerous static structures are known, various biophysical properties of antibodies (i.e., specificity, hydrophobicity and stability) are governed by their dynamic character. Additionally, the importance of high-quality structures in structure-function relationship studies has substantially increased. These structure-function relationship studies have also created a demand for precise homology models of antibody structures, which allow rational antibody design and engineering when no crystal structure is available. Here, we discuss various aspects and challenges in antibody design and extend the paradigm of describing antibodies with only a single static structure to characterizing them as dynamic ensembles in solution.