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Intermolecular hydrogen bonding is responsible for the high boiling point of water (100 °C) compared to the other group 16 hydrides, which have little capability to hydrogen bond. Intramolecular hydrogen bonding is partly responsible for the secondary, tertiary, and quaternary structures of proteins and nucleic acids.
The hydrogen bond can be compared with the closely related dihydrogen bond, which is also an intermolecular bonding interaction involving hydrogen atoms. These structures have been known for some time, and well characterized by crystallography ; [ 56 ] however, an understanding of their relationship to the conventional hydrogen bond, ionic bond ...
Hydrogen bonds of the form A--H•••B occur when A and B are two highly electronegative atoms (usually N, O or F) such that A forms a highly polar covalent bond with H so that H has a partial positive charge, and B has a lone pair of electrons which is attracted to this partial positive charge and forms a hydrogen bond. [23]: 702 Hydrogen ...
It is not a covalent bond, but instead is classified as a strong non-covalent interaction. It is responsible for why water is a liquid at room temperature and not a gas (given water's low molecular weight). Most commonly, the strength of hydrogen bonds lies between 0–4 kcal/mol, but can sometimes be as strong as 40 kcal/mol [3] In solvents ...
A solid with extensive hydrogen bonding will be considered a molecular solid, yet strong hydrogen bonds can have a significant degree of covalent character. As noted above, covalent and ionic bonds form a continuum between shared and transferred electrons; covalent and weak bonds form a continuum between shared and unshared electrons.
The source of adhesive forces, according to the dispersive adhesion mechanism, is the weak interactions that occur between molecules close together. [2] These interactions include London dispersion forces, Keesom forces, Debye forces and hydrogen bonds. Individually, these attractions are not very strong, but when summed over the bulk of a ...
Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...
The bond length, or the minimum separating distance between two atoms participating in bond formation, is determined by their repulsive and attractive forces along the internuclear direction. [3] As the two atoms get closer and closer, the positively charged nuclei repel, creating a force that attempts to push the atoms apart.