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Three-Dimensional Solution Structure and Stability of Phage 434 Cro Protein †,‡

✍ Scribed by Padmanabhan, S.; Jiménez, M. A.; González, C.; Sanz, J. M.; Giménez-Gallego, G.; Rico, M.

Book ID
126027924
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
272 KB
Volume
36
Category
Article
ISSN
0006-2960

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📜 SIMILAR VOLUMES

A comparative study of dynamic structure
A comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysis
✍ Wako, Hiroshi; Tachikawa, Masanori; Ogawa, Atsushi 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 980 KB

T w o DNA binding proteins, Cro and the amino-terminal domain of the repressor of bacteriophage 434 (434 Cro and 434 repressor) that regulate gene expression and contain a helix-turn-helix (HTH) motif responsible for their site-specific DNA recognition adopt very similar three-dimensional structures