Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs …
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at …
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions …
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the …
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other …
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand …
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications …
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, …
Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell …
Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical …
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures …
Protein kinases are able to govern large-scale cellular changes in response to complex arrays of stimuli, and much effort has been directed at uncovering …