Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

Ligand binding modulates the energy landscape of proteins, thus altering their folding and
allosteric conformational dynamics. To investigate such interplay, calmodulin has been a …

Numerous relatively short regions within intrinsically disordered proteins (IDPs) serve as
molecular recognition elements (MoREs). They fold into ordered structures upon binding to …

Determining the structures, kinetics, thermodynamics and mechanisms that underlie
conformational exchange processes in proteins remains extremely difficult. Only in …

In the past decade, a wealth of experimental data has demonstrated that a large fraction of
proteins, while functional, are intrinsically disordered at physiological conditions. Many …

Adenylate kinase (ADK) has been explored widely, through both experimental and
theoretical studies. However, still less is known about how the functional dynamics of ADK is …

Calmodulin (CaM) is found to have the capability to bind multiple targets. Investigations on
the association mechanism of CaM to its targets are crucial for understanding protein …

The double-well model is usually used to describe the conformational transition between
two states of a protein. Since conformational changes usually occur within a relatively large …

Highlights•Key interaction features due to metal binding in metalloproteins were
discussed.•Progress on molecular simulations of metalloprotein folding with diverse models …