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Related Concept Videos

Hydrogen Bonds01:04

Hydrogen Bonds

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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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Hydrogen Bonds00:26

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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
Hydrogen Bonds Control the World!
Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Related Experiment Video

Updated: Dec 2, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

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Low barrier hydrogen bonds in protein structure and function.

M Trent Kemp1, Eric M Lewandowski1, Yu Chen1

  • 1Department of Molecular Medicine, University of South Florida Morsani College of Medicine, 12901 Bruce B. Downs Blvd, MDC 3522, Tampa, Florida 33612, United States.

Biochimica Et Biophysica Acta. Proteins and Proteomics
|November 5, 2020
PubMed
Summary
This summary is machine-generated.

Low-barrier hydrogen bonds (LBHBs) are debated in proteins. Experiments show LBHBs have stronger enthalpy than standard hydrogen bonds, offering insights into enzyme function and structure.

Keywords:
Enzyme catalysisLBHBNMR downfield shiftNeutron diffractionShort HBSub-angstrom resolution X-ray crystallography

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Low-barrier hydrogen bonds (LBHBs) are short hydrogen bonds (HBs) with equally shared hydrogen atoms, whose existence and role in protein catalysis remain debated.
  • Advancements in diffraction techniques have identified delocalized hydrogens in potential LBHBs, but short HBs do not always equate to LBHBs.

Purpose of the Study:

  • To investigate the energetic properties of LBHBs in proteins.
  • To explore the implications of LBHB characteristics for enzyme catalysis and protein structure.

Main Methods:

  • X-ray diffraction
  • Neutron diffraction
  • Experimental studies on ketosteroid isomerase (KSI)

Main Results:

  • Experimental evidence suggests LBHBs are significantly stronger than standard HBs in terms of enthalpy within the protein microenvironment.
  • This strength difference was not observed in free energy, highlighting a key aspect of the LBHB debate.

Conclusions:

  • The discrepancy between enthalpy and free energy of LBHBs provides critical insights into the ongoing debate.
  • The unique strength of LBHBs plays a significant role in the kinetics of enzyme function and protein structure, interacting with other molecular forces in a pre-organized environment.