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. 1975 Dec;72(12):4953-5.
doi: 10.1073/pnas.72.12.4953.

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

F P Ottensmeyer, R F Whiting, A P Korn

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

F P Ottensmeyer et al. Proc Natl Acad Sci U S A. 1975 Dec.

Abstract

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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References

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