The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …

The study of molecular evolution at the level of protein-coding genes often entails comparing
large datasets of sequences to infer their evolutionary relationships. Despite the importance …

Background Normal mode analysis (NMA) using elastic network models is a reliable and
cost-effective computational method to characterise protein flexibility and by extension, their …

Biochemical activity and core stability are essential properties of proteins, maintained
usually by conserved amino acids. Structural dynamics emerged in recent years as another …

Even after a century of investigation, our understanding of how enzymes work remains far
from complete. In particular, several factors that enable enzymes to achieve high catalytic …

Motivation: The function of a protein depends not only on its structure but also on its
dynamics. This is at the basis of a large body of experimental and theoretical work on protein …

Proteins are intrinsically flexible molecules. The role of internal motions in a protein's
designated function is widely debated. The role of protein structure in enzyme catalysis is …

Proteins are usually described and classified according to amino acid sequence, structure or
function. Here, we develop a minimally biased scheme to compare and classify proteins …

RNA molecules are highly dynamic systems characterized by a complex interplay between
sequence, structure, dynamics, and function. Molecular simulations can potentially provide …

Understanding how local protein modifications, such as binding small-molecule ligands, can
trigger and regulate large-scale motions of large protein domains is a major open issue in …