Peptidyl-prolyl cis/trans isomerase family (PPIase) is structurally divided into three
subfamilies, cyclophilins (Cyps), FK506-binding proteins (FKBPs), and parvulins. Pin1 …

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved
and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated …

A difference contact network analysis (dCNA) method is developed for delineating allosteric
mechanisms in proteins. The new method addresses limitations of conventional network …

Fully understanding the mechanism of allosteric regulation in biomolecules requires
separating and examining all of the involved factors. In enzyme catalysis, allosteric effector …

The incorporation of a guest, with different basic sites, into an organized system (host), such
as macrocycles, could stabilize, detect, or promote the formation of a certain protomer. In this …

Conspectus Recent advances have made all-atom molecular dynamics (MD) a powerful tool
to sample the conformational energy landscape. There are still however three major …

Pin1 belongs to the family of the peptidyl-prolyl cis-trans isomerase (PPIase), which is a
class of enzymes that catalyze the cis/trans isomerization of the Proline residue. Pin1 is …

Regulated hydrolysis of the phosphoinositide phosphatidylinositol (4, 5)-bis-phosphate to
diacylglycerol and inositol-1, 4, 5-P 3 defines a major eukaryotic pathway for translation of …

Proteins are inherently dynamic, and proper enzyme function relies on conformational
flexibility. In this study, we demonstrated how an active site residue changes an enzyme's …

Pin1 is an essential peptidyl-prolyl isomerase (PPIase) that catalyzes cis–trans prolyl
isomerization in proteins containing pSer/Thr-Pro motifs. It has an N-terminal WW domain …