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Dissecting the thermodynamics of GAP-RhoA interactions
We describe a detailed study of the RhoA-binding epitope of the GAP domain of Graf, including the determination of the thermodynamic and kinetic parameters of the interaction of wild-type domain, and of its fifteen single-site mutants, with cognate GTPases. We show that residues important for the st...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2008
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2656442/ https://ncbi.nlm.nih.gov/pubmed/18929667 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jsb.2008.09.007 |
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