Nature achieves differentiation of specific and nonspecific binding in molecular interactions
through precise control of biomolecules in space and time. Artificial systems such as …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

The recent availability of long equilibrium simulations of protein folding in atomistic detail for
more than 10 proteins allows us to identify the key interactions driving folding. We find that …

Single molecule and NMR measurements of protein dynamics increasingly uncover the
complexity of binding scenarios. Here, we describe an extended conformational selection …

Water is essential for life in many ways, and without it biomolecules might no longer truly be
biomolecules. In particular, water is important to the structure, stability, dynamics, and …

Protein folding and binding are analogous processes, in which the protein 'searches' for
favourable intramolecular or intermolecular interactions on a funnelled energy landscape …

The structure of a protein complex together with information about its affinity and other
thermodynamic characteristics provide a “frozen” view of the complex. This picture ignores …

Transient complexes are crucial for diverse biological processes such as biochemical
pathways and signaling cascades in the cell. Here, we give an overview of the transient …

The mutation and overexpression of the epidermal growth factor receptor (EGFR) are
associated with the development of a variety of cancers, making this prototypical …

Protein dynamics take place on many time and length scales. Coarse‐grained structure‐
based \bf(G\overlineo) models utilize the funneled energy landscape theory of protein …