Differences in binding affinity among cell-cycle CDK and cyclin pairs.

The mammalian cell cycle is coordinated by primarily four cyclin-dependent kinases (CDKs), which are activated by a family of cyclin proteins to phosphorylate diverse protein effectors of cell growth and division. A wealth of qualitative protein interaction studies have supported a model in which different CDKs have specific cognate cyclin partners. However, there have been few quantitative measurements of binding kinetics and affinity to support our understanding of CDK-cyclin preferences and the structural origins of those preferences.

Prediction and confirmation of a switch-like region within the N-terminal domain of hSIRT1.

Many proteins display conformational changes resulting from allosteric regulation. Often only a few residues are crucial in conveying these structural and functional allosteric changes. These regions that undergo a significant change in structure upon receiving an input signal, such as molecular recognition, are defined as switch-like regions.