Correctly folded proteins make twice as many hydrophobic contacts

STEPHEN H. BRYANT, L. MARIO AMZEL

Research output: Contribution to journalArticle

Abstract

A novel statistical analysis of non‐bonded contacts in a set of known protein structures shows that the natural residue types fall into five or six groups distinguishable by nearest neighbor preference. The observed pattern of contact specificities clearly reflects residue hydrophobicity and charge. Its most striking feature is that residues in the hydrophobic group make about twice as many contacts with one another as would be expected on a random basis. A similar increase in hydrophobic contact frequency can be observed at the level of individual proteins. Native proteins make, on average, about twice as many hydrophobic contacts as corresponding misfolded proteins (1), generated by computer. On the basis of these observations increased hydrophobic contact frequency is proposed as a simple model of the hydrophobic effect.

Original languageEnglish (US)
Pages (from-to)46-52
Number of pages7
JournalInternational Journal of Peptide and Protein Research
Volume29
Issue number1
DOIs
StatePublished - Jan 1987

Keywords

  • hydrophobic effect
  • misfolded proteins
  • protein folding
  • residue contacts

ASJC Scopus subject areas

  • Biochemistry

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