氨基酸与蛋白质5.pptVIP

(c) A heterologous interaction leading to a closed structure—a tetramer. (d) A tetramer formed by two sets of isologous interactions. The polypeptide backbone of the prealbumin dimer. The monomers associate in a manner that continues the β-sheets. A tetramer is formed by isologous interactions between the side chains extending outward from sheet D′A′G′H′HGAD in both dimers, which pack together nearly at right angles to one another. Several possible symmetric arrays of identical protein subunits, including (a) cyclic symmetry, (b) dihedral symmetry, and (c) cubic symmetry, including examples of tetrahedral (T), octahedral (O), and icosahedral (I) symmetry. Rotational symmetry in proteins. (a) In cyclic symmetry, subunits are related by rotation about a single n-fold axis, where n is the number of subunits so related. The axes are shown as black lines; the numbers are values of n. Only two of many possible Cn arrangements are shown. (b) In dihedral symmetry, all subunits can be related by rotation about one or both of two axes, one of which is twofold. D2 symmetry is most common. (c) Icosahedral symmetry. Relating all 20 triangular faces of an icosahedron requires rotation about one or more of three separate rotational axes: twofold, threefold, and fivefold. An end-on view of each of these axes is shown at the right. The oligomeric states of hemerythrin in various marine worms. (a) The hemerythrin in Thermiste zostericola crystallized as a monomer; (b) the octameric hemerythrin crystallized from Phascolopsis gouldii; (c) the trimeric hemerythrin crystallized from Siphonosoma collected in mangrove swamps in Fiji. Viral capsids. (a) Poliovirus. The coat proteins of poliovirus assemble into an icosahedron 300 ? in diameter. Icosahedral symmetry is a type of rotational symmetry. On the left is a surface contour image of the poliovirus capsid. In the image on the right, lines have been superimposed to show the axes of symmetry. (b) Tobacco mosaic virus. This rod-shaped vir