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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.
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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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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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

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Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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2D NMR: Overview of Heteronuclear Correlation Techniques01:18

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Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
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¹H NMR: Complex Splitting01:13

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

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In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Quantitative Analysis of Multiplex H-Bonds.

Esther S Brielle1, Isaiah T Arkin2

  • 1The Alexander Grass Center for Bioengineering, Benin School of Computer Science and Engineering, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem 9190400, Israel.

Journal of the American Chemical Society
|July 22, 2020
PubMed
Summary
This summary is machine-generated.

Multiplex hydrogen bonds, involving three or more groups, are prevalent in transmembrane helices. These non-canonical bonds, particularly involving serine and threonine, are significantly stronger than single hydrogen bonds.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Spectroscopy

Background:

  • Hydrogen bonding is crucial for biomolecular structure and interactions.
  • Previous studies primarily focused on single hydrogen bonds, neglecting multiplex interactions.
  • The energetics of multiplex hydrogen bonds remain largely unexplored.

Purpose of the Study:

  • To investigate the prevalence and energetics of multiplex hydrogen bonds.
  • To characterize non-canonical hydrogen bonds involving serine and threonine residues in transmembrane helices.
  • To determine the contribution of these bonds to protein stability and flexibility.

Main Methods:

  • Isotope-edited Fourier-transform infrared (FTIR) spectroscopy.
  • Density Functional Theory (DFT) calculations.
  • Analysis of transmembrane helix sequences.

Main Results:

  • 92% of transmembrane helices exhibit at least one non-canonical hydrogen bond involving serine or threonine.
  • These bonds form between hydroxyl side chains and over-coordinated carbonyl oxygens (positions i-4, i-3, or i).
  • Bond enthalpies are up to 127% higher than canonical single hydrogen bonds.

Conclusions:

  • Multiplex hydrogen bonds involving serine and threonine are common in transmembrane helices.
  • These strong interactions stabilize residues in hydrophobic environments.
  • They provide flexibility, potentially crucial for protein function.