Analysis of the interactions of sulfur-containing amino acids in membrane proteins

José C. Gómez-Tamayo, Arnau Cordomí, Mireia Olivella, Eduardo Mayol, Daniel Fourmy, Leonardo Pardo

Research output: Contribution to journalArticleResearchpeer-review

20 Citations (Scopus)

Abstract

© 2016 The Protein Society The interactions of Met and Cys with other amino acid side chains have received little attention, in contrast to aromatic–aromatic, aromatic–aliphatic or/and aliphatic–aliphatic interactions. Precisely, these are the only amino acids that contain a sulfur atom, which is highly polarizable and, thus, likely to participate in strong Van der Waals interactions. Analysis of the interactions present in membrane protein crystal structures, together with the characterization of their strength in small-molecule model systems at the ab-initio level, predicts that Met–Met interactions are stronger than Met–Cys ≈ Met–Phe ≈ Cys–Phe interactions, stronger than Phe–Phe ≈ Phe–Leu interactions, stronger than the Met–Leu interaction, and stronger than Leu–Leu ≈ Cys–Leu interactions. These results show that sulfur-containing amino acids form stronger interactions than aromatic or aliphatic amino acids. Thus, these amino acids may provide additional driving forces for maintaining the 3D structure of membrane proteins and may provide functional specificity.
Original languageEnglish
Pages (from-to)1517-1524
JournalProtein Science
DOIs
Publication statusPublished - 1 Aug 2016

Keywords

  • membrane proteins
  • mining of crystal structures
  • sulfur-containing amino acids
  • van der Waals interactions

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