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Journal article

Calorimetric dissection of colicin DNase--immunity protein complex specificity.

Abstract:

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 residues providing specificity. A key question for such complexes is the thermodynamic basis for specificity given the dominance of the hotspot. We address this question using, as our model, colicin ...

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Publication status:
Published

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Publisher copy:
10.1021/bi052373o

Authors


Keeble, AH More by this author
Kirkpatrick, N More by this author
Shimizu, S More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Biochemistry
Volume:
45
Issue:
10
Pages:
3243-3254
Publication date:
2006-03-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:c3d5bcaf-dbb7-4f41-991b-e4638dec026b
Source identifiers:
310195
Local pid:
pubs:310195

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