12 edition of Hydrogen bonding in biological structures found in the catalog.
Includes bibliographical references (p. -546 and index.
|Statement||G.A. Jeffrey, W. Saenger.|
|LC Classifications||QP517.H93 J44 1991|
|The Physical Object|
|Pagination||xiv, 569 p. :|
|Number of Pages||569|
|LC Control Number||90026529|
Hydrogen bonding refers to the formation of Hydrogen bonds, which are a special class of attractive intermolecular forces that arise due to the dipole-dipole interaction between a hydrogen atom that is bonded to a highly electronegative atom and another highly electronegative atom while lies in the vicinity of the hydrogen atom. The weak or non-conventional hydrogen bond has been the subject of intense scrutiny over recent years. Although the existence of this type of hydrogen bond was suggested many years ago, research has traditionally focused on the stronger and more well-known forms of hydrogen bonds.
Hydrogen bonding in water results in the crystal structure of ice, making it less dense than water and able to float. chloroform (CHCl 3): Hydrogen bonding occurs between hydrogen of one molecule and carbon of another molecule. ammonia (NH 3): Hydrogen bonds form between hydrogen of one molecule and nitrogen of another. In the case of ammonia. This chapter reviews the weak hydrogen bond in supramolecular chemistry by focusing on the relevance of these interactions in the analysis, design, and synthesis of the structures of molecular assemblies, most notably crystals. Supramolecular chemistry signifies chemistry beyond the molecule and deals with implications of the fact that molecules can recognise one another via intermolecular.
2. Secondary Structure. Secondary Structure refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D are two types of secondary structures observed in proteins. One type is the alpha (α) helix structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. Hydrogen bonds can form between different molecules and they do not always have to include a water molecule. Hydrogen atoms in polar bonds within any molecule can form bonds with other adjacent molecules. For example, hydrogen bonds hold together two long strands of DNA to give the DNA molecule its characteristic double-stranded structure.
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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 Bonding in Biological Structures is Cited by: Hydrogen Bonding in Biological Structures is informative and eminently usable. It is, in a sense, a Rosetta stone that unlocks a wealth of information from the language of crystallography and makes it accessible to all scientists.
(From a book review of Kenneth M. Harmon, Science ). 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 Bonding in Biological Structuresis. 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 Bonding in Biological Structures is. Hydrogen Bonding in Biological Structures George A. Jeffrey When writing a book on as vast a subject as Hydrogen Bonding, a major problem is to circumscribe the subject matter.
a detailed knowledge of the H-bond is required. That the bulk of the literature concerning experimental and theoretical aspects of H-bonds is inaccessible to biologists is a fact.
The authors have therefore provided the biological community with an invaluable. Amides contain N-H bonds; hydrogen bonds involving amides are crucial influences in the structure of proteins.
Large biological molecules like proteins consists of s of atoms, which interact through "intramolecular" ion-ion, London dispersion, dipole-dipole, and hydrogen bonding to create a unique 3D structure.
Biological Chemistry Book: Biochemistry Online (Jakubowski) 4: Protein Structure where D is a hydrogen bond donor (like NH) and A is a hydrogen bond acceptor, (like C=O), (determined by analysis of X ray crystallographic structures).
Of all H bonds to C=O, 43% are to water, 11% to side chains, and 46% to main chain NH's. Of all H bonds. For students and researchers interested in supramolecular chemistry, biological structure and recognition, and other sophisticated concepts and methodologies, it provides a careful selection of key references from the vast hydrogen bonding literature.
An Amazon Book with Buzz: "Sweet Sorrow" by David Nicholls Reviews: 3. In biology, intramolecular hydrogen bonding is partly responsible for the secondary, tertiary, and quaternary structures of proteins and nucleic acids.
The hydrogen bonds help the proteins and nucleic acids form and maintain specific shapes. Van der Waals Interactions. 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. II Hydrogen Bonding in Small Biological Molecules.- 13 Hydrogen Bonding in Carbohydrates.- Sugar Alcohols (Alditols) as Model Cooperative Hydrogen-Bonded Structures.- Influence of Hydrogen Bonding on Configuration and Conformation in Cyclic Monosaccharides.- Rules to Describe Hydrogen-Bonding Patterns in Monosaccharides.- Description 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.
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‐acceptor angle of between 90° and ° (°).
An easy-to-read supplement to the often brief descriptions of hydrogen bonding found in most undergraduate chemistry and molecular biology textbooks, An 5/5(1). Most hydrogen bonds are weak attractions with a binding strength about one-tenth of that of a normal covalent bond.
Nevertheless, they are very important. Without them, all wooden structures would collapse, cement would crumble, oceans would Hydrogen bonds range from the very strong, comparable with covalent bonds, to the very weak, comparable.
Hydrogen-bond formation modifies the electronic structure of the molecules involved. In very strong hydrogen bonds, the covalent X-H bond may be so much lengthened that it is barely distinguished from the HA hydrogen bond, as shown in Part IB, Chap.
7, Table The hydrogen atom in a hydrogen bond is shared by two electronegative atoms such as oxygen or nitrogen.) Hydrogen bonds are responsible for specific base-pair formation in the DNA double helix and a major factor to the stability of the DNA double helix structure.
A hydrogen bond (often informally abbreviated H-bond) is a partial intermolecular bonding interaction between a lone pair on an electron rich donor atom, particularly the second-row elements nitrogen (N), oxygen (O), or fluorine (F), and the antibonding molecular orbital of a bond between hydrogen (H) and a more electronegative atom or group.
Hydrogen bonding, interaction involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons; such a bond is weaker than an ionic bond or covalent bond but stronger than van der Waals en bonds can exist between atoms in different molecules or in parts of the same molecule.
One atom of the pair (the donor), generally a fluorine, nitrogen, or. In proteins, hydrogen-bonding patterns are key signatures of secondary structure elements. The same hydrogen-bonding patterns that occur between backbone atoms in adjacent strands in β-sheets in a single protein chain can serve to ‘zip’ together two proteins that interact via extended strands – see the example in Figure 4d.Each groove is lined by potential hydrogen-bond donor and acceptor atoms that enable specific interactions with proteins (see Figure ).
In the minor groove, N-3 of adenine or guanine and O-2 of thymine or cytosine can serve as hydrogen acceptors, and the amino group attached to C-2 of guanine can be a hydrogen donor.
In the major groove, N.Water-Involved Hydrogen Bonds in Dimeric Supramolecular Structures of Magnesium and Zinc Phthalocyaninato Complexes. ACS Omega4 (2), DOI: /acsomega.8b