Proteins are complex biological macromolecules performing a great variety of functions in
the living systems. In order to get insight into the atomic structures and the time evolution of …

In nature, proteins most often exist as complexes, with many of these consisting of identical
subunits. Understanding of the energetics governing the folding and misfolding of such …

Recent structural studies and analyses of microbial genomes have consolidated the
understanding of the structural and functional versatility of coiled‐coil domains in proteins …

The effect of mutations on protein structures is usually rather localized and minor. Finding a
mutation that can single-handedly change the fold and/or topology of a protein structure is a …

Conformational transitions play a central role in regulating protein function. Structure-based
models with multiple basins have been used to understand the mechanisms governing …

In the current work we study, via molecular simulations and experiments, the folding and
stability of proteins from the tertiary motif of 4-α-helical bundles, a recurrent motif consisting …

Recurrent protein folding motifs include various types of helical bundles formed by α-helices
that supercoil around each other. While specific patterns of amino acid residues (heptad …

Quantifying convergence and sufficient sampling of macromolecular molecular dynamics
simulations is more often than not a source of controversy (and of various ad hoc solutions) …

This study aims to the investigation of the advantages of designing new proteins presume
upon a 'bias' sequence of amino acids, based on the reversed sequence of parent proteins …

It has been proposed that certain type II restriction enzymes (REs), such as EcoRV, track the
helical pitch of DNA as they diffuse along DNA, a so-called rotation-coupled sliding. As of …