This motif is critical in stabilizing distinct conformations of the activation loop to form a platform for binding to the protein substrate.

An E3 ubiquitin ligase targets specific protein substrates for degradation by the proteasome.

SIRT1 deacetylates protein substrates, thus altering their activity or function.

The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates.

The reason for this result is that the denaturing agents unfold the protein substrates and make them more accessible to the protease.

The apical section contains a large number of hydrophobic binding sites for unfolded protein substrates.

This molecule is not based on a peptide and has no obvious structural similarity to a protein substrate.

It contains twelve doses of ethylene dihydride with a protein substrate.

Caspases are activated in apoptotic cells and cleave intracellular protein substrates.

A new class of peptide-derived inhibitors, based on sequence homology with the protein substrate, can be developed.