Protein phosphorylation regulates many cellular processes by causing changes in protein
conformation. The prolyl isomerase PIN1 has been identified as a regulator of …

A significant fraction of every proteome is occupied by biologically active proteins that do not
form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and …

Intrinsically unstructured proteins (IUPs) are devoid of extensive structural order but often
display signs of local and limited residual structure. To explain their effective functioning, we …

Neuropathological hallmarks of Alzheimer's disease are neurofibrillary tangles composed of
tau and neuritic plaques comprising amyloid-β peptides (Aβ) derived from amyloid precursor …

Summary cis-trans isomerization of proteins phosphorylated by proline-directed kinases is
proposed to control numerous signaling molecules and is implicated in the pathogenesis of …

Molecular recognition lies at the heart of biological processes. At the molecular level the
biological activity of drugs corresponds to the binding of small molecules to macromolecular …

Classical studies show that for many proteins, the information required for specifying the
tertiary structure is contained in the amino acid sequence. Here, we attempt to define the …

The reversible phosphorylation of proteins on serine or threonine residues preceding
proline (Ser/Thr-Pro) is a major cellular signaling mechanism. Although it is proposed that …

Protein phosphorylation on certain serine or threonine residues preceding proline (Ser/Thr-
Pro) is a pivitol signaling mechanism in diverse cellular processes and its deregulation can …

Two strategies have been recently employed to push molecular simulation to long,
biologically relevant time scales: projection-based analysis of results from specialized …