Nuclease-T: An Active Derivative of Staphylococcal Nuclease Composed of Two Noncovalently Bonded Peptide Fragments
- Contributor(s):
- Sodja, Ann Taniuchi, Horoshi Anfinsen, Christian B. (Christian Boehmer), 1916-1995 Proceedings of the National Academy of Sciences of the United States of America
- Publication:
- National Academy Press (U.S.), September 1967
- Language(s):
- English
- Format:
- Text
- Subject(s):
- Peptide Mapping Enzymes Research Design Staphylococcus aureus
- Genre(s):
- Archival Materials Articles
- Abstract:
- This is one of many articles produced by Anfinsen's research team and others on the factors contributing to the translation of the genetic message for a particular protein backbone. Taniuchi, Sodja, and Anfinsen determined that such a translation was no longer possible if the linear information had been manipulated through the deletion of amino acid residues. However, they did find that some proteins that they termed "recombining systems" could be cleaved into two, or even three, fragments that recombined through non-covalent forces to yield biologically active structures with physical properties very similar to those of the parent protein molecules.
- Copyright:
- This item may be under copyright protection; contact the copyright owner for permission before re-use.
- Extent:
- 8 pages
- NLM Unique ID:
- 101584571X170 (See in Profiles in Science)
- Profiles in Science ID:
- KKBBLD
- Permanent Link:
- http://resource.nlm.nih.gov/101584571X170
- Archival Collection:
- The Christian B. Anfinsen Papers (Profiles in Science)