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Hydrogen Bonds

Hydrogen 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...

Hydrogen Bonds

Hydrogen 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...

Noncovalent Attractions in Biomolecules

Noncovalent 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,...

Noncovalent Attractions in Biomolecules

Noncovalent 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,...

Intermolecular Forces

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...

Introduction to Chemical Bonds

Introduction to Chemical Bonds

Chemical Bonds
The electrons of the outermost energy level determine the energetic stability of the atom and its tendency to form chemical bonds with other atoms. The innermost electron shell has a maximum capacity of two electrons, but the next two electron shells can each have a maximum of eight electrons. This is known as the octet rule, which states that, with the exception of the innermost shell, atoms are most stable energetically when they have eight electrons in their valence shell, the...

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Related Experiment Video

Updated: Jul 3, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Bethe approximation for the hydrogen-bonding self-avoiding walk in a solvent.

D P Foster¹, M Aniambossou

¹Laboratoire de Physique Théorique et Modélisation CNRS UMR 8089, Université de Cergy-Pontoise, 2 ave A Chauvin 95302 Cergy-Pontoise cedex, France.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics

|July 23, 2008

Summary

This summary is machine-generated.

This study models protein secondary structure formation using a hydrogen-bonding model on a square lattice. It incorporates solvent quality effects within the Bethe approximation framework to understand protein folding dynamics.

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Area of Science:

Biophysics
Computational Biology
Protein Science

Background:

Protein secondary structure formation is crucial for protein function.
Understanding the role of solvent quality in protein folding is essential.
Lattice models provide simplified frameworks for studying complex biophysical phenomena.

Purpose of the Study:

To investigate protein secondary structure formation using a square-lattice hydrogen-bonding model.
To extend the model by incorporating the effects of solvent quality.
To analyze the model within the Bethe approximation.

Main Methods:

Development of a square-lattice hydrogen-bonding model.
Inclusion of solvent quality parameters into the model.
Application of the Bethe approximation for theoretical analysis.

Main Results:

The study provides insights into how solvent quality influences protein secondary structure formation.
The Bethe approximation offers a tractable method for analyzing the lattice model.
Model predictions can be compared with experimental data on protein folding.

Conclusions:

The hydrogen-bonding lattice model, extended with solvent quality, offers a valuable theoretical tool for studying protein folding.
The Bethe approximation is suitable for analyzing such models.
Further refinements could enhance the model's predictive power for diverse protein systems.