When Szent-Györgyi called water the “matrix of life”, 1 he was echoing an old sentiment.
Paracelsus in the 16th century said that “water was the matrix of the world and of all its …

Protein-bound internal water molecules are essential features of the structure and function of
microbial rhodopsins. Besides structural stabilization, they act as proton conductors and …

Much progress has been made in our understanding of water molecule reactions on
surfaces, proton solvation in gas-phase water clusters, and proton transfer through liquids …

With recent advances in X-ray crystallography of membrane proteins promising many new
high-resolution structures, molecular dynamics simulations will become increasingly …

Networks of internal water molecules are thought to provide proton transfer pathways in
many enzymatic and photosynthetic reactions. Extremely broad absorption continua …

Microbial rhodopsins have been intensively researched for the last three decades. Since the
discovery of bacteriorhodopsin, the scope of microbial rhodopsins has been considerably …

Self-assembly of proteins often gives rise to interesting quasi-stable structures that serve
important biological purposes. Insulin hexamer is such an assembly. While monomer is the …

Molecular oxygen acts as the terminal electron sink in the respiratory chains of aerobic
organisms. Cytochrome c oxidase in the inner membrane of mitochondria and the plasma …

Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins, found in
microorganisms belonging to all kingdoms of life, with new members being constantly …

The functional mechanism of the light-driven proton pump protein bacteriorhodopsin
depends on the location of water molecules in the active site at various stages of the …