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Thermodynamic Analysis of the Structural Stability of Phage 434 Cro Protein †

✍ Scribed by Padmanabhan, S.; Laurents, D. V.; Fernández, A. M.; Elias-Arnanz, M.; Ruiz-Sanz, J.; Mateo, P. L.; Rico, M.; Filimonov, V. V.

Book ID
127162865
Publisher
American Chemical Society
Year
1999
Tongue
English
Weight
144 KB
Volume
38
Category
Article
ISSN
0006-2960

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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