Three-dimensional structure of herring sperm protamine Y-I with the aid of dark field electron microscopy.
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 toge...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1975
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC388852/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1061083/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.72.12.4953 |
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