Noncovalent cross-links in context with other structural and functional elements of proteins

Éva Tüdos, András Fiser, Ágnes Simon, Zsuzsanna Dosztányi, Mónika Fuxreiter, Csaba Magyar, István Simon

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5 Scopus citations

Abstract

Proteins are heteropolymers with evolutionary selected native sequences of residues. These native sequences code for unique and stable 3D structures indispensable for biochemical activity and for proteolysis resistance, the latter which guarantees an appropriate lifetime for the protein in the protease rich cellular environment. Cross-links between residues close in space but far in the primary structure are required to maintain the folded structure of proteins. Some of these cross-links are covalent, most frequently disulfide bonds, but the majority of the cross-links are sets of cooperative noncovalent long-range interactions. In this paper we focus on special clusters of noncovalent long-range interactions: the Stabilization Centers (SCs). The relation between the SCs and secondary structural elements as well as the relation between SCs and functionally important regions of proteins are presented to show a detailed picture of these clusters, which are believed to be primarily responsible for major aspects of protein stability.

Original languageEnglish (US)
Pages (from-to)347-351
Number of pages5
JournalJournal of Chemical Information and Computer Sciences
Volume44
Issue number2
Publication statusPublished - Mar 1 2004

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ASJC Scopus subject areas

  • Chemistry(all)
  • Information Systems
  • Computer Science Applications
  • Computational Theory and Mathematics

Cite this

Tüdos, É., Fiser, A., Simon, Á., Dosztányi, Z., Fuxreiter, M., Magyar, C., & Simon, I. (2004). Noncovalent cross-links in context with other structural and functional elements of proteins. Journal of Chemical Information and Computer Sciences, 44(2), 347-351.