The Hydrogen bond

Recent developments in theory and experiments
  • 1.11 MB
  • English

distributor, American Elsevier Pub. Co
ID Numbers
Open LibraryOL7529705M
ISBN 10044410805X
ISBN 139780444108050

The Hydrogen Bond and the Water Molecule offers a synthesis of what is known and currently being researched on the topic of hydrogen bonds and water molecules. The most simple water molecular, H2O, is a fascinating but poorly understood molecule. This contrast with the book's subtitle: "Outline of a Comprehensive Hydrogen Bond Theory".

A more appropriate subtitle would have been: "A Structural Chemist Viewpoint" or "Structure-Property Correlations". Actually, a general theory of chemical bonding, which also includes H-bonding, already exists: this is the Quantum Theory of Atoms in Cited by: Hydrogen Bond (Books in Chemistry S.) Hardcover – December 1, by A.L.

McClellan George C. Pimentel (Author)Author: A.L. McClellan George C. Pimentel. Hydrogen Bonding covers the papers presented at the Symposium on Hydrogen Bonding, held at Ljubljana on July 29 to August 3, The book focuses on the developments, processes, approaches, methodologies, and reactions involved in hydrogen Edition: 1.

The Hydrogen Bond and the Water Molecule offers a synthesis of what is known and currently being researched on the topic of hydrogen bonds and water molecules. The most simple water molecular, H2O, is a fascinating but poorly understood molecule.

Its unique ability to attract an exceptionally large number of hydrogen bonds induces the formation of a dense "hydrogen bond network" The Hydrogen bond book has the. An easy-to-read supplement to the often brief descriptions of hydrogen bonding found in most undergraduate chemistry and molecular biology textbooks, An Introduction to Hydrogen Bonding 5/5(1).

hydrogen bond. between an electronegative atom and a hydrogen atom attached to a second, relatively electronegative atom. It is best considered as an electrostatic interaction, heightened by the small size of hydrogen, which permits proximity of the interacting dipoles or charges.

Intramolecular Hydrogen Bond Energy in Polyhydroxy Systems: A Critical Comparison of Molecular Tailoring and Isodesmic Approaches. The Journal of Physical Chemistry A(28), Cited by: Hydrogen bonding confers rigidity to the protein structure and specificity to intermolecular interactions.

The accepted (and most frequently observed) geometry for a hydrogen bond is a distance of less than Å ( Å) between hydrogen and the acceptor and a donor‐hydrogen Cited by: hydrogen bond.

exists when a hydrogen atom is bonded to two or more other atoms. Since the hydrogen atom has only one orbital (1s) at sufficiently low energy, hydrogen bonds are mainly electrostatic.

in nature but covalent and repulsive orbital-orbital interactions are also present. The. Hydrogen bond (H-bond) effects are well known: it makes sea water liquid, joins cellulose microfibrils in sequoia trees, shapes DNA into chromosomes, and polypeptide chains into wool, hair, muscles, or enzymes.

However, its very nature is much less known and we may still wonder why O-HO energies range from less than 1 to more than 30 kcal/mol without evident reason.

The hydrogen bond has only 5% or so of the strength of a covalent bond. However, when many hydrogen bonds can form between two molecules (or parts of the same molecule), the resulting union can be sufficiently strong as to be quite stable.

Multiple hydrogen bonds. hold the two strands of the DNA double helix together. A hydrogen bond results when this strong partial positive charge attracts a lone pair of electrons on another atom, which becomes the hydrogen bond acceptor. An electronegative atom such as fluorine, oxygen, or nitrogen is a hydrogen bond acceptor, regardless of whether it is bonded to a hydrogen atom or not.

hydrogen bond acceptor and the hydrogen itself can be as short as Å, well below the sum of the atomic radii (e.g. Å for hydrogen and ~Å for oxygen and nitrogen). You know that the Lennard-Jones potential rises with 1/r12 if we get closer than the Van der Vaals radii. The only way these atoms can get closer to one another is if File Size: KB.

Hydrogen Bond. Hydrogen bonds are an important contributor to the stability of proteins and to the specificity of protein–protein and protein–ligand interactions.

From: Hematology (Seventh Edition), This bond is called the hydrogen bond. As a result of hydrogen bonding, a hydrogen atom links the two electronegative atoms simultaneously, one by a covalent bond and the other by a hydrogen bond.

The conditions for hydrogen bonding are: The molecule must contain a highly electronegative atom linked to the hydrogen atom. The energy of hydrogen bonds, which is usually in the range of \(\ \text{kcal/mol}\) (\(\ \text{kJ/mol}\)), results from the electrostatic interaction and also from the orbital interaction of the antibonding σ*(XH) MO of the molecule acting as the hydrogen donor and the non-bonding lone electron pair MO n Y of the hydrogen acceptor.

The Hydrogen Bond and the Water Molecule offers a synthesis of what is known and currently being researched on the topic of hydrogen bonds and water molecules. The most simple water molecular, H2O, is a fascinating but poorly understood molecule.

In the second part of the book the role played by the dense H-bond network developed by H2O.

Description The Hydrogen bond FB2

Their –O–H groups form hydrogen-bonds with water molecules to form stabilizing interactions. As the length of the hydrocarbon chain increases, the non-polar hydrocarbon part of the molecule starts to become more important and the solubility decreases.

The donor in a hydrogen bond is the atom to which the hydrogen atom participating in the hydrogen bond is covalently bonded, and is usually a strongly electronegative atom such as N,O, or F. The hydrogen acceptor is the neighboring electronegative ion or molecule, and must posses a lone electron pair in order to form a hydrogen bond.

Hydrogen bonds are weak attractions, with a binding strength less than one-tenth that of a normal covalent bond. However, hydrogen bonds are of extraordinary importance; without them all wooden structures would collapse, cement would crumble, oceans would vaporize, and all living things would disintegrate into random dispersions of inert matter.

Hydrogen bonds have about a tenth of the strength of an average covalent bond, and are being constantly broken and reformed in liquid water.

If you liken the covalent bond between the oxygen and hydrogen to a stable marriage, the hydrogen bond has "just good friends" status. Water as a "perfect" example of hydrogen bonding. Finally, the book examines experimental and theoretical studies on the nature and control of excited-state hydrogen transfer in various systems.

Hydrogen Bonding and Transfer in the Excited State is an essential overview of this increasingly important field of study, surveying the entire field over 2 volumes, 40 chapters and pages.

Figure 3: Hydrogen bonding angles for a phosphate binding protein are close to optimal in the phosphate-bound structure but distorted with arsenate.

(A), A close-up view of the short hydrogen bond between oxygen of a bound phosphate and the carboxylate of aspartate. The binding angles are close to the canonical optimal values. The hydrogen bond. [George C Pimentel; Aubrey L McClellan] Home. WorldCat Home About WorldCat Help. Search. Search for Library Items Search for Lists Search for Contacts Search for a Library.

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Create # A series of chemistry books\/span>\n \u00A0\u00A0\u00A0\n schema. Hydrogen bonds and friction forces between fibres in paper are the dominating of them [6,7,8].

Polar water molecules play the key role in formation of hydrogen bonds between fibres in paper [9,10]. In papermaking, all technological operations take place in water, whose consumption amounts to ca. 5 to 15 m 3 per ton of paper produced [2,11,12 Cited by: A hydrogen bond is an interaction between a proton donor group D-H and a proton acceptor atom A, the D-H A interaction being called as a hydrogen bond.

Generally, a hydrogen bond can be characterized as a proton shared by two lone electron pairs. Hydrogen bond energies range from about kcal/mol for strong bonds, kcal/mol forFile Size: KB.

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A hydrogen bond is an intermolecular attractive force in which a hydrogen atom that is covalently bonded to a small, highly electronegative atom is attracted to a lone pair of electrons on an atom in a neighboring molecule.

Hydrogen bonds are very strong compared to other dipole interactions. The strength of a typical hydrogen bond is about 5% of that of a covalent bond. Linus Pauling credits T.S. Moore and T.F. Winmill with the first mentioning of the hydrogen bond () in his book, The Nature of the Chemical Bond.

That bond wasn't used for water though. 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 molecule.

In other words, hydrogen bonds always include hydrogen that is already part of a polar molecule. hydrogen bonding in peptide links The linking of atoms in two peptide links by the hydrogen bonds they can form.

The links may be part of the same polypeptide chain that has doubled back on itself, or they may belong to different chains. Encyclopædia Britannica, Inc.Hydrogen bonds may form between atoms within a molecule or between two separate molecules. A hydrogen bond is weaker than an ionic bond or a covalent bond, but stronger than van der Waals forces.

Hydrogen bonds play an important role in biochemistry and produce many of the unique properties of water.A hydrogen bond is a low kind type of dipole-dipole bond that exists between an electronegative molecule and a hydrogen molecule bonded to another electronegative molecule.

This type of bond always involves a hydrogen atom. That explains the name. Hydrogen bonds can occur between molecules (intermolecularly), or within different parts of a single molecule (intramolecularly).