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Theoretical Chemistry Accounts

, Volume 106, Issue 1–2, pp 121–127 | Cite as

Stabilization centers and protein stability

  • Á. Simon
  • Z. Dosztányi
  • C. Magyar
  • G. Szirtes
  • É. Rajnavölgyi
  • I. Simon
Regular article

Abstract.

The well-balanced stability of protein structures allows large-scale fluctuations, which are indispensable in many biochemical functions, ensures the long-term persistence of the equilibrium structure and it regulates the degradation of proteins to provide amino acids for biosynthesis. This balance is studied in the present work with two sets of proteins by analyzing stabilization centers, defined as certain clusters of residues involved in cooperative long-range interactions. One data set contains 56 proteins, which belong to 16 families of homologous proteins, derived from organisms of various physiological temperatures. The other set is composed of 31 major histocompatibility complex (MHC)–peptide complexes, which represent peptide transporters complexed with peptide ligands that apparently contribute to the stabilization of the MHC proteins themselves. We show here that stabilization centers, which had been identified as special clusters of residues that protect the protein structure, evolved to serve also as regulators of function – related degradation of useless protein as part of protein housekeeping.

Key words: Protein thermostability Major histocompatibility complex protein Protein stability 

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Copyright information

© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • Á. Simon
    • 2
  • Z. Dosztányi
    • 2
  • C. Magyar
    • 2
  • G. Szirtes
    • 2
  • É. Rajnavölgyi
    • 3
  • I. Simon
    • 1
  1. 1. e-mail: simon@enzim.hu; Tel.: +36-1-4669276; Fax: +36-1-4665465XX
  2. 2. Institute of Enzymology, BRC, Hungarian Academy of Sciences, P.O. Box 7, 1518 Budapest, HungaryHU
  3. 3. Department of Immunology, Eötvös Loránd University, Jávorka S. u. 14, 2131 Göd, HungaryHU

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