Three-dimensional structure of herring sperm protamine Y-I with the aid of dark field electron microscopy.

AUTOR(ES)

Ottensmeyer, F P

RESUMO

High resolution electron micrographs of herring sperm protamine (clupeine) Y-I provide sufficient detail to constrain the folding of the known amino-acid sequence of the protein into a unique three-dimensional configuration. The structure consists of a loose helix of turns of various sizes held together at one edge, spread apart along the other. This form appears to represent the shape of several fish protamines.

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