Related Experiment Video
Updated: Jul 12, 2026
11:37
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Molecular interactions and hydrogen bond tunneling dynamics: some new perspectives
Science (New York, N.Y.)
|March 12, 1993
Summary
New spectroscopic tools reveal complex quantum tunneling in hydrogen-bonded systems. These studies provide detailed intermolecular potential energy surfaces for water and ammonia complexes.
Area of Science:
- Physical Chemistry
- Spectroscopy
- Quantum Dynamics
Background:
- Advancements in tunable far-infrared lasers and high-resolution spectroscopy enable detailed studies of weakly bound clusters.
- Understanding intermolecular forces and quantum tunneling is crucial for hydrogen-bonded systems.
Purpose of the Study:
- To explore the impact of advanced spectroscopic probes on understanding intermolecular forces.
- To investigate complex quantum tunneling dynamics in hydrogen-bonded systems.
- To derive intermolecular potential energy surfaces from experimental data.
Main Methods:
- Utilizing tunable far-infrared laser spectroscopy.
- Applying high-resolution spectroscopic techniques to weakly bound clusters.
- Inverting spectroscopic data to determine potential energy surfaces.
Main Results:
- Detailed analysis of interactions in water-hydrophobe complexes, the water trimer, and the ammonia dimer.
- Successful inversion of spectroscopic data to yield intermolecular potential energy surfaces.
- Investigations into nonpairwise additivity of intermolecular forces.
Conclusions:
- Far-infrared spectroscopy provides powerful insights into intermolecular forces and quantum dynamics.
- The derived potential energy surfaces enhance the understanding of hydrogen-bonded systems.
- Spectroscopic methods are key to elucidating complex molecular interactions.
More Related Videos
Related Concept Videos
02:35Noncovalent Attractions in Biomolecules
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.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
02:35Noncovalent Attractions in Biomolecules
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.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
00:26Hydrogen Bonds
Hydrogen BondsHydrogen 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...
01:04Hydrogen Bonds
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...
02:04Protein-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
01:24Van der Waals Interactions
Atoms and molecules interact with each other through intermolecular forces. These electrostatic forces arise from attractive or repulsive interactions between particles with permanent, partial, or temporary charges. The intermolecular forces between neutral atoms and molecules are ion–dipole, dipole–dipole, and dispersion forces, collectively known as van der Waals forces.Polar molecules have a partial positive charge on one end and a partial negative charge on the other end of the molecule,...