Anisotropic thermal motion and polypeptide secondary structure studied by X-ray analysis at 0.98A resolution.
aPP is a 36-amino acid polypeptide which forms a stable globular structure stabilised by hydrophobic interactions between a polyproline-like helix and an alpha-helix. Crystals contain dimers and are crosslinked by coordination through zinc ions leading to a well-ordered lattice which diffracts X-rays to a resolution of 0.98A. This gives a 5:1 ratio of observations-to-parameters even when anisotropic thermal ellipsoids defined by six parameters for each non-hydrogen atom were refined using least-squares techniques. Rigid body refinement of groups within the polypeptide was also undertaken. The relationship of the principal axes of individual thermal ellipsoids and the librations of rigid side groups to features of secondary, tertiary, and quaternary structures of aPP and its interactions with water molecules are described.
D000818:Animals; D001717:Birds; D003460:Crystallization; D008958:Models, Molecular; D010191:Pancreatic Polypeptide; D011487:Protein Conformation; D013816:Thermodynamics; D014961:X-Ray Diffraction
D010191:Pancreatic Polypeptide