The structure determination of protein− protein complexes is a rather tedious and lengthy
process, by both NMR and X-ray crystallography. Several methods based on docking to …

A very fast empirical method is presented for structure‐based protein pKa prediction and
rationalization. The desolvation effects and intra‐protein interactions, which cause variations …

We use single silicon nitride nanopores to study folded, partially folded, and unfolded single
proteins by measuring their excluded volumes. The DNA-calibrated translocation signals of …

We present a new computational method of docking pairs of proteins by using spherical
polar Fourier correlations to accelerate the search for candidate low‐energy conformations …

With molecular dynamics protein dynamics can be simulated in atomic detail. Current
computers are not fast enough to probe all available conformations, but fluctuations around …

The bacterial phosphotransferase system (PTS) couples phosphoryl transfer, via a series of
bimolecular protein–protein interactions, to sugar transport across the membrane. The …

Many biological macromolecular interactions proceed via lowly-populated, highly transient
species that arise from rare excursions between the minimum free energy configuration and …

Diverse proteins with similar structures are grouped into families of homologs and analogs, if
their sequence similarity is higher or lower, respectively, than 20%–30%. It was suggested …

The interaction between the∼ 30 kDa N-terminal domain of enzyme I (EIN) and the∼ 9.5
kDa histidine-containing phosphocarrier protein HPr of the Escherichia coli …

The practical exploitation of the vast numbers of sequences in the genome sequence
databases is crucially dependent on the ability to identify the function of each sequence …