分子生物物理学MolecularBiophysics.pptVIP

Sheet 20-28% (Kabsch Sander, 1983; Creighton, 1993) Turn that serve to reverse the direction of the polypeptide chain Surface of the protein Antibody recognition, phosphorylation, glycosylation, hydroxylation Identification of secondary structure Distortions of a-helices The majority of a-helices in globular proteins are curved or distorted somewhat compared with the standard Pauling-Corey model. Why? The packing of buried helices against other secondary structure elements in the core of the protein Proline residues induce distortions of around 20 degrees in the direction of the helix axis 3. Solvent. Exposed helices are often bent away from the solvent region. This is because the exposed C=O groups tend to point towards solvent to maximise their H-bonding capacity, i.e. tend to form H-bonds to solvent as well as N-H groups. 310 helix introduction Only 3.4% of the residues are involved in 310 helices, and nearly all those in helical segments containing i-i+3 hydrogen bonds. Ideal (-74.0, -4.0) / found (-71.0 and -18.0) CO---HN hydrogen bond: i-i+3 Standard 310 helix Proline helix Left handed helix 3.0 residues per turn pitch = 9.4 ? No hydrogen bonding in the backbone but helix still forms. Poly-glycine also forms this type of helix Collagen: high in Gly-Pro residues has this type of helical structure p-helices introduction The pi helix is an extremely rare secondary structural element in proteins. the backbone C=O of residue i hydrogen bonds to the backbone HN of residue i+5. i- - i + 5 H-bonds 2.8angstrom the phi and psi angles of the pure pi helix ( -57.1, -69.7) lie at the very edge of an allowed, minimum energy region of the Ramachandran (phi, psi) map. the pi helix requires that the angle tau (N-Ca-C) be larger (114.9) than the standard tetrahedral angle of 109.5 degrees. the large radius of the pi helix means the polypeptide backbone is no longer in van der Waals contact across the helical axis forming an axial hole too small for solvent