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Hydrogen Bonds00:26

Hydrogen Bonds

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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.
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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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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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Stable molecules exist because covalent bonds hold the atoms together. The strength of a covalent bond is measured by the energy required to break it, that is, the energy necessary to separate the bonded atoms. Separating any pair of bonded atoms requires energy — the stronger a bond, the greater the energy required to break it.
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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding
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Increasing Enzyme Stability and Activity through Hydrogen Bond-Enhanced Halogen Bonds.

Anna-Carin C Carlsson1, Matthew R Scholfield1, Rhianon K Rowe1

  • 1Department of Biochemistry & Molecular Biology , Colorado State University , Fort Collins , Colorado 80523 , United States.

Biochemistry
|June 21, 2018
PubMed
Summary
This summary is machine-generated.

Engineered proteins with unnatural amino acids can improve stability and function. Replacing tyrosine with m-chlorotyrosine in T4 lysozyme created a synergistic halogen bond, enhancing protein stability and enzyme activity for therapeutic applications.

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Area of Science:

  • Biomolecular engineering
  • Protein engineering
  • Biocatalysis

Background:

  • Protein stability is crucial for biomolecular engineering and therapeutic design.
  • T4 lysozyme is a model enzyme used in protein studies.
  • Unnatural amino acids offer novel ways to modify protein properties.

Purpose of the Study:

  • To enhance the thermal stability and enzymatic activity of T4 lysozyme.
  • To investigate the role of halogen bonding in protein stabilization.
  • To explore the application of unnatural amino acids in protein design.

Main Methods:

  • Site-directed mutagenesis to incorporate m-chlorotyrosine (mClY) into T4 lysozyme.
  • Thermal stability assays (melting temperature and enthalpy).
  • Enzymatic activity assays at elevated temperatures.
  • Quantum chemical calculations to analyze bonding interactions.

Main Results:

  • mClY incorporation increased T4 lysozyme's melting temperature by ~1 °C and melting enthalpy by 3 kcal/mol.
  • Enzymatic activity at 40 °C was 15% higher compared to the wild-type enzyme.
  • A novel hydrogen bond-enhanced halogen bond (HeX-B) interaction was identified between mClY and glycine 28.
  • Larger halogens (bromine, iodine) did not confer similar stability or activity enhancements.

Conclusions:

  • Engineered halogen bonds, specifically HeX-B, can effectively stabilize enzymes and enhance their activity.
  • Unnatural amino acids like m-chlorotyrosine are valuable tools for designing more stable protein therapeutics.
  • This study demonstrates a new strategy for protein engineering using halogenated amino acids.