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  2. 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]

  3. Hydrogen bond - Wikipedia

    en.wikipedia.org/wiki/Hydrogen_bond

    A single hydrogen atom can participate in two hydrogen bonds. This type of bonding is called "bifurcated" (split in two or "two-forked"). It can exist, for instance, in complex organic molecules. [46] It has been suggested that a bifurcated hydrogen atom is an essential step in water reorientation. [47]

  4. Molecular self-assembly - Wikipedia

    en.wikipedia.org/wiki/Molecular_self-assembly

    Molecular self-assembly is a key concept in supramolecular chemistry. [6] [7] [8] This is because assembly of molecules in such systems is directed through non-covalent interactions (e.g., hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi-stacking interactions, and/or electrostatic) as well as electromagnetic interactions.

  5. 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.

  6. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Proteins have two types of well-classified, frequently occurring elements of local structure defined by a particular pattern of hydrogen bonds along the backbone: alpha helix and beta sheet. Their number and arrangement is called the secondary structure of the protein.

  7. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Protein–protein_interaction

    The contacts between the two proteins are shown as coloured patches. 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 ...

  8. Nucleic acid secondary structure - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_secondary...

    Some DNA- or RNA-binding enzymes can recognize specific base pairing patterns that identify particular regulatory regions of genes. Hydrogen bonding is the chemical mechanism that underlies the base-pairing rules described above. Appropriate geometrical correspondence of hydrogen bond donors and acceptors allows only the "right" pairs to form ...

  9. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    A covalent bond forming H 2 (right) where two hydrogen atoms share the two electrons. A covalent bond is a chemical bond that involves the sharing of electrons to form electron pairs between atoms. These electron pairs are known as shared pairs or bonding pairs.