Do all backbone polar groups in proteins form hydrogen bonds?

Patrick J. Fleming, George D. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

Evidence from proteins and peptides supports the conclusion that intrapeptide hydrogen bonds stabilize the folded form of proteins. Paradoxically, evidence from small molecules supports the opposite conclusion, that intrapeptide hydrogen bonds are less favorable than peptide-water hydrogen bonds. A related issue - often lost in this debate about comparing peptide-peptide to peptide-water hydrogen bonds - involves the energetic cost of an unsatisfied hydrogen bond. Here, experiment and theory agree that breaking a hydrogen bond costs between 5 and 6 kcal/mol. Accordingly, the likelihood of finding an unsatisfied hydrogen bond in a protein is insignificant. This realization establishes a powerful rule for evaluating protein conformations.

Original languageEnglish (US)
Pages (from-to)1911-1917
Number of pages7
JournalProtein Science
Volume14
Issue number7
DOIs
StatePublished - Jul 2005

Keywords

  • Hydrogen bond satisfaction
  • Protein folding
  • Protein hydrogen bonds
  • Protein stability

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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