Helix Geometry in Proteins

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Presentation transcript:

Helix Geometry in Proteins D. J. Barlow and J. M. Thornton Department of Crystallography Birkbeck College London J.Molec.Biol. (1988) 201, 601-619

general analysis of 291 helices the 310-helix “ideal” pauling model. : -74, : -4 figure 2. ,  angles of 310-helices averaged model. : -71, : -18

analysis of the regularity and curvature of 48 -helices using HBEND Rl : r.m.s deviation of axis points from a line Rc : r.m.s.d. of axis from a circle radius of curvature figure 5. helix curvature and regularity (a) (b) (c )

the helices (figures 6, 8 and 9) linear kinked irregular  /  : # res./turn r.m.s.e.

figure 13 avian pancreatic peptide (aPP) rad:68A, Rc:0.08A, Rl:0.37A solvent face hydrophobic packing

proline and the -helix o i+4 o i+3 n i n i+1 citrate synthase. residues 166-195, =28˚ (figures 11 and 13)-helix