Cryo-electron microscopy (cryo-EM) is rapidly becoming an attractive method in the field of
structural biology. With the exploding popularity of cryo-EM, sample preparation must evolve …

Microbial rhodopsins are a family of photoactive retinylidene proteins widespread
throughout the microbial world. They are notable for their diversity of function, using …

G-protein-coupled receptors comprise the largest family of mammalian transmembrane
receptors. They mediate numerous cellular pathways by coupling with downstream …

Light-driven proton-pum** rhodopsins are widely distributed in many microorganisms.
They convert sunlight energy into proton gradients that serve as energy source of the cell …

Molecular machines, such as polymerases, ribosomes, or proteasomes, fulfill complex tasks
requiring the thermal energy of their environment. They achieve this by restricting random …

Single-particle cryogenic electron microscopy (cryo-EM) allows reconstruction of high-
resolution structures of proteins in different conformations. Protein function often involves …

The atomic structure of the light-driven ion pump bacteriorhodopsin and the surrounding
lipid matrix was determined by X-ray diffraction of crystals grown in cubic lipid phase. In the …

The aquaporins (AQPs) are a family of small membrane-spanning proteins (monomer size∼
30 kDa) that are expressed at plasma membranes in many cells types involved in fluid …

An effective environmental force constant is introduced to quantify the molecular resilience
(or its opposite,“softness”) of a protein structure and relate it to biological function and …

In protein and RNA macromolecules, only a limited number of different side‐chain chemical
groups are available to function as catalysts. The myriad of enzyme‐catalyzed reactions …