结构生物化学Chapter2 Structure of proteins.pptVIP

The Alpha Helix The α -helix dipole and the properties of proteins Schematic view of the cross-section of an α -helix. Side chains are shown as green circles. alpha-helices are often amphipathic ? An amphipathic alpha-helix can be shown in a helical wheel representation. In a helical wheel, a cross-sectional view of the alpha-helix is drawn as a spiral with amino acids occurring every 100 o along the spiral ? 360 o divided by 3.6 amino acids per turn gives 100 o per amino acid. The Beta-Pleated Sheet Composed of beta strands ? Also first postulated by Pauling and Corey, 1951 ? Strands may be parallel or antiparallel ? Rise per residue: – 3.47 Angstroms for antiparallel strands – 3.25 Angstroms for parallel strands – Each strand of a beta sheet may be pictured as a helix with two residues per turn The Beta-Pleated Sheet Parallel or anti-parallel beta-sheet AAs that tend to be found in beta-strands Val Ile Phe Tyr Trp Thr The Beta Turn (tight turn, or ? -bend ) ? Beta turns connect beta strands and reverse the direction of beta strands; ? Proline and glycine have high propensity for beta turns; ? The carbonyl oxygen of the i th residue forms H- bond with the amide proton of the (i+3) th residue; ? Tight turn promotes formation of antiparallel beta sheets. The Beta Turn The Beta Bulge ? Beta bulge occurs between normal beta-strands. Comprised of two residues on one strand and one on the other; ? Bulges cause bending of otherwise straight anti-parallel beta strands. Loops connect secondary structural elements together Loop Loop Loop Tertiary structure ? The three dimensional arrangement of all atoms in a given protein is referred to as the proteins tertiary structure . ? Contrast tertiary structure with secondary structure, which refers primarily with the arrangement of amino acids that are adjacent in the primary structure (sequence), or very close in the primary structure. Again, non-covalent forces are those that are most importan