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Hydrogen bonding stabilizes globular proteins

J K Myers1, C N Pace

  • 1Department of Medical Biochemistry, Texas A & M University, College Station 77843-1114, USA.

Biophysical Journal
|October 1, 1996
PubMed
Summary
This summary is machine-generated.

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Intramolecular hydrogen bonds are crucial for protein structure. Experimental evidence strongly indicates that these hydrogen bonds significantly stabilize globular proteins, contributing favorably to their overall stability.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Intramolecular hydrogen bonds are vital for globular protein structure and stability.
  • The net contribution of these bonds to protein stability remains a subject of debate between experimental and theoretical studies.

Purpose of the Study:

  • To investigate the quantitative contribution of intramolecular hydrogen bonds to the conformational stability of globular proteins.
  • To reconcile conflicting findings from experimental and theoretical approaches regarding protein stabilization by hydrogen bonds.

Main Methods:

  • Utilized experimental measurements of the change in conformational stability (delta (delta G)) upon mutation of hydrogen-bonding residues.
  • Applied corrections to experimental data to account for variations in side-chain hydrophobicity and conformational entropy.

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Main Results:

  • Mutational studies suggest an initial stabilization of 1.0 kcal/mol per hydrogen bond.
  • After correcting for hydrophobicity and entropy, the estimated stabilization increased to 2.2 kcal/mol per hydrogen bond.
  • Experimental findings consistently support a stabilizing role for intramolecular hydrogen bonds.

Conclusions:

  • Intramolecular hydrogen bonds provide a significant net favorable contribution to the stability of globular proteins.
  • Experimental evidence compellingly demonstrates that hydrogen bonding enhances protein stability.