Improving Enzyme Thermostability

The Thermococcus litoralis Glutamate Dehydrogenase Model
  • Costantino Vetriani
  • Dennis L. Maeder
  • Nicola J. Tolliday
  • Horst H. Klump
  • Kitty S. P. Yip
  • David W. Rice
  • Frank T. Robb
Chapter

Abstract

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 (Russel et al., 1994; Britton et al., 1995), optimization of hydrophobic interactions (Spassov et al., 1995), extended ion-pair networks (Yip et al., 1995; Chan et al., 1995; Korndörfer 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).

Keywords

Optimal Growth Temperature Protein Thermostability Marine Biotechnology Increase Packing Density gdhA Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Costantino Vetriani
    • 1
  • Dennis L. Maeder
    • 1
    • 2
  • Nicola J. Tolliday
    • 1
  • Horst H. Klump
    • 2
  • Kitty S. P. Yip
    • 3
  • David W. Rice
    • 3
  • Frank T. Robb
    • 1
  1. 1.Center of Marine Biotechnology Columbus CenterUniversity of Maryland Biotechnology InstituteBaltimoreUSA
  2. 2.Department of BiochemistryUniversity of Cape TownRondeboschSouth Africa
  3. 3.Krebs InstituteUniversity of SheffieldUK

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