Role of cation-π interactions to the stability of thermophilic proteins

M. Michael Gromiha, Shali Thomas, C. Santhosh

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

Elucidating the factors responsible for exhibiting extreme thermal stability of thermophilic proteins is very important for an understanding of the mechanism of protein stability, as well as to design stable proteins. In this work, we have analyzed the influence of cation-π interactions to enhance the stability from mesophilic to thermophilic proteins. The favorable residue pairs forming such a system of interactions have been brought out. We found that the Tyr has a greater number of such interactions with Lys in thermophilic proteins. Specifically, the same Lys would experience a greater number of cation-π interactions with several Tyr residues in thermophiles. On the other hand, the influence of Phe in making cation-π interactions is higher in mesophiles than in thermophiles. Further, a network of cation-π interactions are maintained by Lys in thermophiles, whereas Arg plays a major role in mesophilic proteins. Moreover, atoms that have a substantial positive charge in both Lys and Arg make a more significant contribution for cation-π interactions, than do cationic group atoms.

Original languageEnglish
Pages (from-to)355-362
Number of pages8
JournalPreparative Biochemistry and Biotechnology
Volume32
Issue number4
DOIs
Publication statusPublished - 25-11-2002

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Protein Stability
Cations
Proteins
Extreme Heat
Atoms
Thermodynamic stability

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry

Cite this

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Role of cation-π interactions to the stability of thermophilic proteins. / Gromiha, M. Michael; Thomas, Shali; Santhosh, C.

In: Preparative Biochemistry and Biotechnology, Vol. 32, No. 4, 25.11.2002, p. 355-362.

Research output: Contribution to journalArticle

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