Interactions between hydrophobic side chains within α‐helices

Trevor P. Creamer, George D. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

The thermodynamic basis of helix stability in peptides and proteins is a topic of considerable interest. Accordingly, we have computed the interactions between side chains of all hydrophobic residue pairs and selected triples in a model helix, using Boltzmann‐weighted exhaustive modeling. Specifically, all possible pairs from the set Ala, Cys, His, Ile, Leu, Met, Phe, Trp, Tyr, and Val were modeled at spacings of (i, i + 2), (i, i + 3), and (i, i + 4) in the central turn of a model poly‐alanyl α‐helix. Significant interactions —both stabilizing and destabilizing —were found to occur at spacings of (i, i + 3) and (i, i + 4), particularly in side chains with rings (i.e., Phe, Tyr, Trp, and His). In addition, modeling of leucine triples in a helix showed that the free energy can exceed the sum of pairwise interactions in certain cases. Our calculated interaction values both rationalize recent experimental data and provide previously unavailable estimates of the constituent energies and entropies of interaction.

Original languageEnglish (US)
Pages (from-to)1305-1314
Number of pages10
JournalProtein Science
Volume4
Issue number7
DOIs
StatePublished - Jul 1995

Keywords

  • hydrophobicity
  • protein conformation
  • protein folding
  • secondary structure
  • α‐helix

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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