Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

The prediction of protein three-dimensional structure from amino acid sequence has been a
grand challenge problem in computational biophysics for decades, owing to its intrinsic …

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 …

Cryogenic electron microscopy (cryo-EM) enables structure determination of
macromolecular objects and their assemblies. Although the techniques have been …

Cryo-electron microscopy (cryo-EM) of non-crystalline single particles is a biophysical
technique that can be used to determine the structure of biological macromolecules and …

Cryoelectron microscopy (Cryo-EM) has enabled structural determination of proteins larger
than about 50 kDa, including many intractable by any other method, but it has largely failed …

Modern vaccine design has sought a minimalization approach, moving to the isolation of
antigens from pathogens that invoke a strong neutralizing immune response. This approach …

The design of protein–protein interfaces using physics-based design methods such as
Rosetta requires substantial computational resources and manual refinement by expert …

Variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) challenge
currently available COVID-19 vaccines and monoclonal antibody therapies due to structural …

Discrete protein assemblies ranging from hundreds of kilodaltons to hundreds of
megadaltons in size are a ubiquitous feature of biological systems and perform highly …