| Literature DB >> 1061083 |
F P Ottensmeyer, R F Whiting, A P Korn.
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.Mesh:
Substances:
Year: 1975 PMID: 1061083 PMCID: PMC388852 DOI: 10.1073/pnas.72.12.4953
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205