Hydrogen bonding in globular proteins

Douglas F. Sticke, Leonard G. Presta, Ken A. Dill, George D. Rose

Research output: Contribution to journalArticle

Abstract

A global census of the hydrogen bonds in 42 X-ray-elucidated proteins was taken and the following demographic trends identified: (1) Most hydrogen bonds are local, i.e. between partners that are close in sequence, the primary exception being hydrogen-bonded ion pairs. (2) Most hydrogen bonds are between backbone atoms in the protein, an average of 68%. (3) All proteins studied have extensive hydrogen-bonded secondary structure, an average of 82%. (4) Almost all backbone hydrogen bonds are within single elements of secondary structure. An approximate rule of thirds applies: slightly more than one-third (37%) form i → i → 3 hydrogen bonds, almost one-third (32%) form → i → 4 hydrogen bonds, and slightly less than one-third (26%) reside in paired strands of β-sheet. The remaining 5% are not wholly within an individual helix, turn or sheet. (5) Side-chain to backbone hydrogen bonds are clustered at helix-capping positions. (6) An extensive nerwork of hydrogen bonds is present in helices. (7) To a close approximation, the total number of hydrogen bonds is a simple function of a protein'e helix and sheet content. (8) A unique quantity, termed the reduced number of hydrogen bonds, is defined as the maximum number of hydrogen bonds possible when every donor: acceptor pair is constrained to be 1:1. This quantity scales linearly with chain length, with 0·71 reduced hydrogen bond per residue. Implications of these results for pathways of protein folding are discussed.

Original languageEnglish (US)
Pages (from-to)1143-1159
Number of pages17
JournalJournal of molecular biology
Volume226
Issue number4
DOIs
StatePublished - May 20 1992
Externally publishedYes

Keywords

  • H-bonding
  • helix capping
  • hydrogen bonding
  • protein folding
  • protein secondary structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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