Thermodynamic evaluation of ligands binding to the Grb2 SH2 domain: effects of α,α-disubstitution at the pY+1 position
A series of phosphotripeptide ligands for the Grb2 SH2 domain was designed and synthesized, each of which derived from the minimal consensus sequence required for binding: Ac-pYXN. The binding affinity and related thermodynamic parameters were determined by isothermal titration calorimetry. Both t...
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| Format: | Others |
| Language: | English |
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2010
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| Online Access: | http://hdl.handle.net/2152/ETD-UT-2009-12-453 |