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...
Main Authors: | Keeble, A, Kirkpatrick, N, Shimizu, S, Kleanthous, K |
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פורמט: | Journal article |
שפה: | English |
יצא לאור: |
2006
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פריטים דומים
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The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes.
מאת: Keeble, A, et al.
יצא לאור: (2005) -
Structure of the ultra-high-affinity colicin E2 DNase--Im2 complex.
מאת: Wojdyla, J, et al.
יצא לאור: (2012) -
Thermodynamic dissection of colicin interactions.
מאת: Housden, N, et al.
יצא לאור: (2011) -
Structure of the ultra-high-affinity colicin E2 DNase-Im2 complex
מאת: Wojdyla, J, et al.
יצא לאור: (2012) -
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
מאת: Keeble, A, et al.
יצא לאור: (2008)