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Hydrogen bonding in globular proteins.

D F Stickle1, L G Presta, K A Dill

  • 1Department of Biological Chemistry, Pennsylvania State University College of Medicine, Hershey 17033.

Journal of Molecular Biology
|August 20, 1992
PubMed
Summary
This summary is machine-generated.

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This study analyzed hydrogen bonds in 42 proteins, finding most are local and involve backbone atoms. Protein structure, particularly helix and sheet content, dictates the total number of hydrogen bonds.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Hydrogen bonds are crucial for protein structure and function.
  • Understanding hydrogen bond distribution provides insights into protein folding pathways.

Purpose of the Study:

  • To conduct a global census of hydrogen bonds in proteins.
  • To identify demographic trends and patterns in hydrogen bond formation.
  • To explore the relationship between hydrogen bonds and protein secondary structure.

Main Methods:

  • Analysis of X-ray crystallographic data for 42 proteins.
  • Quantification of hydrogen bond types and locations.
  • Calculation of the reduced number of hydrogen bonds per residue.

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Main Results:

  • Most hydrogen bonds are local, primarily involving backbone atoms (68%).
  • Extensive hydrogen-bonded secondary structures (82%) are prevalent, mainly within helices and beta-sheets.
  • Hydrogen bond networks are extensive in helices, and their total number correlates with helix and sheet content.

Conclusions:

  • Hydrogen bond patterns are predictable based on protein secondary structure.
  • The reduced number of hydrogen bonds scales linearly with protein chain length.
  • These findings have implications for understanding protein folding mechanisms.