Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Do all backbone polar groups in proteins form hydrogen bonds?

Patrick J Fleming1, George D Rose

  • 1T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.

Protein Science : a Publication of the Protein Society
|June 7, 2005
PubMed
Summary

Intrapeptide hydrogen bonds are crucial for protein stability, contrary to some small molecule evidence. Breaking these bonds is energetically costly, making unsatisfied hydrogen bonds rare in protein structures.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The master molecule that built biology: How water shaped the chemistry of life.

Protein science : a publication of the Protein Society·2026
Same author

50 years in the shadow of the Ramachandran plot.

Protein science : a publication of the Protein Society·2025
Same author

FIBOS: R and python packages for analyzing protein packing and structure.

Bioinformatics (Oxford, England)·2025
Same author

Anti-microbial cetylpyridinium chloride suppresses mast cell function by targeting tyrosine phosphorylation of Syk kinase.

Journal of immunotoxicology·2025
Same author

The Iconic α-Helix: From Pauling to the Present.

Methods in molecular biology (Clifton, N.J.)·2024
Same author

Antimicrobial cetylpyridinium chloride suppresses mast cell function by targeting tyrosine phosphorylation of Syk kinase.

bioRxiv : the preprint server for biology·2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Chemistry

Background:

  • Intrapeptide hydrogen bonds are proposed to stabilize protein tertiary structures.
  • Small molecule studies suggest intrapeptide hydrogen bonds are less favorable than peptide-water interactions.
  • The energetic cost of unsatisfied hydrogen bonds is a critical factor in protein folding.

Purpose of the Study:

  • To resolve the apparent paradox regarding the role of intrapeptide hydrogen bonds in protein stability.
  • To investigate the energetic cost of unsatisfied hydrogen bonds in protein conformations.
  • To establish a rule for evaluating protein structures based on hydrogen bond energetics.

Main Methods:

  • Review of existing experimental and theoretical evidence from proteins, peptides, and small molecules.

Related Experiment Videos

  • Analysis of the energetic cost of breaking hydrogen bonds.
  • Evaluation of the likelihood of unsatisfied hydrogen bonds in protein conformations.

    • Main Results:

    • Evidence from proteins supports stabilization by intrapeptide hydrogen bonds.
    • Evidence from small molecules suggests these bonds are less favorable than solvent interactions.
    • Both experiment and theory indicate that breaking a hydrogen bond costs 5-6 kcal/mol.
    • The energetic penalty makes unsatisfied hydrogen bonds highly improbable in proteins.

    Conclusions:

    • Intrapeptide hydrogen bonds play a significant role in stabilizing folded protein structures.
    • The high energetic cost of unsatisfied hydrogen bonds is a key determinant of protein conformation.
    • This understanding provides a robust framework for analyzing protein structures.