BIOL 78 |
| Bruton's tyrosine kinase (BTK) is a cytoplasmic tyrosine kinase that contains one SH3 domain. The SH3 domain has been identified as a key player in the regulation of many proteins by binding to proline-rich peptides. The SH3 domain of BTK contains two tryptophan (W) residues, named W251 and W252, localized near the hydrophobic groove of the binding site of the SH3 domain. The mutations W251A, W251F, W252A and W252F were produced to determine the role of the W residues in the binding to the proline-rich peptides. Raman spectroscopy is a sensitive indicator of a molecule's chemical properties and environment. The BTK-SH3 domain proteins were purified to homogeneity and characterized by Raman spectroscopy utilizing the signature tryptophan vibrations: 1550 cm-1 and the ratio of the intensity of the Raman doublet 1360/1340 cm-1. The intensity of these bands is an indicator of structural changes in the W microenvironment. |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |