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  2. Hydrogen bond - Wikipedia

    en.wikipedia.org/wiki/Hydrogen_bond

    In a discrete water molecule, there are two hydrogen atoms and one oxygen atom. The simplest case is a pair of water molecules with one hydrogen bond between them, which is called the water dimer and is often used as a model system. When more molecules are present, as is the case with liquid water, more bonds are possible because the oxygen of ...

  3. Molecular recognition - Wikipedia

    en.wikipedia.org/wiki/Molecular_recognition

    A recent study based on molecular simulations and compliance constants describes molecular recognition as a phenomenon of organisation. Even for small molecules like carbohydrates, the recognition process can not be predicted or designed even assuming that each individual hydrogen bond's strength is exactly known. [26]

  4. Antigen-antibody interaction - Wikipedia

    en.wikipedia.org/wiki/Antigen-antibody_interaction

    The antigens and antibodies combine by a process called agglutination. It is the fundamental reaction in the body by which the body is protected from complex foreign molecules, such as pathogens and their chemical toxins. In the blood, the antigens are specifically and with high affinity bound by antibodies to form an antigen-antibody complex.

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The β pleated sheet is a structure that forms with the backbone bending over itself to form the hydrogen bonds (as displayed in the figure to the left). The hydrogen bonds are between the amide hydrogen and carbonyl oxygen of the peptide bond. There exists anti-parallel β pleated sheets and parallel β pleated sheets where the stability of ...

  6. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    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 ...

  7. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    It is formed as result of various attractive forces like hydrogen bonding, disulfide bridges, hydrophobic interactions, hydrophilic interactions, van der Waals force etc. When two or more polypeptide chains (either of identical or of different sequence) cluster to form a protein, quaternary structure of protein is formed.

  8. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons. It often, but not always, involves some chemical bonding.

  9. Molecule - Wikipedia

    en.wikipedia.org/wiki/Molecule

    The simplest of molecules is the hydrogen molecule-ion, H 2 +, and the simplest of all the chemical bonds is the one-electron bond. H 2 + is composed of two positively charged protons and one negatively charged electron , which means that the Schrödinger equation for the system can be solved more easily due to the lack of electron–electron ...