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  2. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...

  3. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    Pyruvate kinase, a protein with three domains (In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of ...

  4. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Polypeptide direction, NH 2 and COOH termini Small arrows on one or both of the termini, or letters. For β-strands, the direction of the arrow is sufficient. Today, the direction of the polypeptide chain is often indicated by a colour ramp. Disulfide bonds Interlocked SS symbol or a zigzag, like a stylized lightning stroke.

  5. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    [1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins . [ 4 ] Chains of fewer than twenty amino acids are called oligopeptides , and include dipeptides , tripeptides , and tetrapeptides .

  6. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and John Kendrew in 1958, for which they received a Nobel Prize in Chemistry A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes . [ 1 ]

  7. Molecular biophysics - Wikipedia

    en.wikipedia.org/wiki/Molecular_biophysics

    It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from a random coil. [17] Each protein exists as an unfolded polypeptide or random coil when translated from a sequence of mRNA to a linear chain of amino acids. This polypeptide lacks any stable (long-lasting) three ...

  8. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Proteins are often synthesized in an inactive precursor form; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function. The protein is activated by cleaving off the inhibitory peptide. Some proteins even have the power to cleave themselves.

  9. Glossary of cellular and molecular biology (M–Z) - Wikipedia

    en.wikipedia.org/wiki/Glossary_of_cellular_and...

    M phase See mitosis. macromolecule Any very large molecule composed of dozens, hundreds, or thousands of covalently bonded atoms, especially one with biological significance. . Many important biomolecules, such as nucleic acids and proteins, are polymers consisting of a repeated series of smaller monomers; others such as lipids and carbohydrates may not be polymeric but are nevertheless large ...