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...
المؤلفون الرئيسيون: | Keeble, A, Kirkpatrick, N, Shimizu, S, Kleanthous, K |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2006
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مواد مشابهة
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The kinetic basis for dual recognition in colicin endonuclease-immunity protein complexes.
حسب: Keeble, A, وآخرون
منشور في: (2005) -
Structure of the ultra-high-affinity colicin E2 DNase--Im2 complex.
حسب: Wojdyla, J, وآخرون
منشور في: (2012) -
Thermodynamic dissection of colicin interactions.
حسب: Housden, N, وآخرون
منشور في: (2011) -
Structure of the ultra-high-affinity colicin E2 DNase-Im2 complex
حسب: Wojdyla, J, وآخرون
منشور في: (2012) -
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
حسب: Keeble, A, وآخرون
منشور في: (2008)