Proteins that self-assemble into polyhedral shell-like structures are useful molecular
containers both in nature and in the laboratory. Here we review efforts to repurpose diverse …

Self-assembly is a ubiquitous process in synthetic and biological systems, broadly defined
as the spontaneous organization of multiple subunits (macromolecules, particles, etc.) into …

Recent advances in computational methods have enabled the predictive design of self-
assembling protein nanomaterials with atomic-level accuracy. These design strategies focus …

The hepatitis B virus capsid represents a promising therapeutic target. Experiments suggest
the capsid must be flexible to function; however, capsid structure and dynamics have not …

Defining mechanisms of direct-acting antivirals facilitates drug development and our
understanding of virus function. Heteroaryldihydropyrimidines (HAPs) inappropriately …

Understanding capsid assembly is important because of its role in virus lifecycles and in
applications to drug discovery and nanomaterial development. Many virus capsids are …

Neutralizing antibodies (NAbs) are traditionally thought to inhibit virus infection by
preventing virion entry into target cells. In addition, antibodies can engage Fc receptors …

Flaviviruses assemble initially in an immature, noninfectious state and undergo extensive
conformational rearrangements to generate mature virus. Previous cryo-electron microscopy …

Highlights•The recent progress in the design of self-assembling protein complexes is
reviewed.•Methodological advancements have enabled design of assemblies with atomic …

Virus capsids, the protective protein shells of viruses with typical dimensions in the
nanometer range, are a challenge to analyze. Analytical techniques need to characterize the …