title: Reverse turns in peptides and proteins.
abstract: The evidence that reverse turns frequently occur as structural components of proteins, as well as of linear and cyclic peptides, is overwhelming. This review summarizes and examines critically the experimental evidence derived from physical methods such as 1H and 13C nuclear magnetic resonance spectroscopy, spin-lattice relaxation time, circular dichroism, IR spectroscopy, and X-ray crystallography. Secondly, theoretical evidence obtained from energy calculations, which rely on empirical energy functions, and correlative methods, which rely on algorithms based on the frequency of occurrence of amino acids, is evaluated. In particular, those theoretical studies for which complementary physical studies have been completed are emphasized. Finally, examples of structure-function relationships involving reverse turns and their biological recognition are demonstrated.
mesh_terms: D000588:Amines; D000900:Anti-Bacterial Agents; D000992:Antitoxins; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002942:Circular Dichroism; D003094:Collagen / Q000378:metabolism; D004549:Elastin / Q000378:metabolism; D004745:Enkephalins; D006023:Glycoproteins / Q000378:metabolism; D006728:Hormones; D006860:Hydrogen Bonding; D006900:Hydroxylation; D007476:Ionophores; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase / Q000276:immunology; D010455:Peptides; D010766:Phosphorylation; D011392:Proline / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000276:immunology; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D014118:Toxins, Biological; D014405:Tuftsin / Q000032:analysis; D014961:X-Ray Diffraction
chemical_list: D000588:Amines; D000900:Anti-Bacterial Agents; D000992:Antitoxins; D004745:Enkephalins; D006023:Glycoproteins; D006728:Hormones; D007476:Ionophores; D010455:Peptides; D011506:Proteins; D014118:Toxins, Biological; D003094:Collagen; D004549:Elastin; D011392:Proline; D009113:Muramidase; D014405:Tuftsin