Calorimetric dissection of colicin DNase--immunity protein complex specificity.
We explore the thermodynamic strategies used to achieve specific, high-affinity binding within a family of conserved protein-protein complexes. Protein-protein interactions are often stabilized by a conserved interfacial hotspot that serves as the anchor for the complex, with neighboring variable re...
Κύριοι συγγραφείς: | Keeble, A, Kirkpatrick, N, Shimizu, S, Kleanthous, K |
---|---|
Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
2006
|
Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
-
The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes.
ανά: Keeble, A, κ.ά.
Έκδοση: (2005) -
Structure of the ultra-high-affinity colicin E2 DNase--Im2 complex.
ανά: Wojdyla, J, κ.ά.
Έκδοση: (2012) -
Thermodynamic dissection of colicin interactions.
ανά: Housden, N, κ.ά.
Έκδοση: (2011) -
Structure of the ultra-high-affinity colicin E2 DNase-Im2 complex
ανά: Wojdyla, J, κ.ά.
Έκδοση: (2012) -
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
ανά: Keeble, A, κ.ά.
Έκδοση: (2008)