Improving enzyme thermostability The Thermococcus litoralis Glutamate Dehydrogenase Model

摘要

The identification of the structural determinants that confer thermostability to a protein remains a major unsolved problem in molecular biology. Trends commonly associated with elevated thermostability in proteins include relatively small solvent-exposed surface area (Chan et al., 1995), decreased length of surface loops (Russel et al., 1994), increased packing density that reduces cavities in the hydrophobic core (Russell et al., 1994; Britton et al., 1995), optimizaton of hydrophobic interactions (Spassov et al., 1995), extended ionpair networks (Yip et al., 1995; Chan et al., 1995; Korndorfer et al., 1995; Henning et al., 1995) and hydrogen bonds between charged-neutral residues (Tanner et al., 1995). Overall these characteristics lead to decreased flexibility of the polypeptide chain, a required feature that compensates for increased thermal fluctuations at high temperatures (Vihinen, 1987).