Metabolic functions, such as the supply of cells with energy, the catalysis of metabolic transformation by enzymes, the transport of substances into the extracellular space or through membranes and communication based on a feedback control system via signalling chains, are fundamental processes in an organism.
Such conformational changes are important in biological functions such as enzymatic catalysis, cellular transport, and signaling [ 4, 5].
The focus of these efforts has progressed from the interior of proteins to their surface and the design of functions, such as binding or catalysis.
GPI- anchored enzymes, receptors, binding proteins, and structural proteins are known to be involved in a number of different physiological processes and functions, such as catalysis, signal transduction, cell adhesion, and complement regulation (Table 6).
Other major fractions of proteins detected were those that perform housekeeping functions such as catalysis (enzymes) (22%) and transport (17%).
The tuning of the pKa of ionizable residues plays a critical role in various protein functions, such as ligand-binding, catalysis, and allostery.
To examine the coevolution of functionally important sites (FIS), we calculated the fraction of coevolved sites that are involved in important molecular functions such as catalysis, protein, ligand or metal binding, and post translational modifications (Tables 2 and 3).
The proteins regulating the cell cycle frequently adopt modular designs that use separate domains to carry out distinct and complementary functions, such as binding and catalysis.
It is now well established that proteins and nucleic acids undergo local and global conformational fluctuations to perform a variety of cellular functions such as signal transduction, transport, and catalysis.
Such movements are required in order to encompass function, such as enzyme catalysis or ligand binding, as well as site-to-site communication within the globular protein fold or between protein subunits [75].
