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Báo cáo khoa học: Structural study of the catalytic domain of PKCf using infrared spectroscopy and two-dimensional infrared correlation spectroscopy

The secondary structure of the catalytic domain from protein kinase Cf was studied using IR spectroscopy. In the presence of the substrate MgATP, there was a significant change in the secondary structure. After heating to 80 C, a 14% decrease in thea-helix component was observed, accompanied by a 6% decrease in the b-pleated sheet; no change was observed in the large loops or in 310 -helix plus associated loops. | ềFEBS Journal Structural study of the catalytic domain of PKCf using infrared spectroscopy and two-dimensional infrared correlation spectroscopy Sonia Sanchez-Bautista Andris Kazaks Melanie Beaulande Alejandro Torrecillas Senena Corbalán-García and Juan C. Gomez-Fernandez Departamento de Bioquimica y Biologia Molecular Universidad de Murcia Spain Keywords 2D-correlation catalytic domain FTIR protein kinase C protein structure Correspondence J. C. Gomez-Fernandez Departamento de Bioquimica y Biologia Molecular A Facultad de Veterinaria Universidad de Murcia Apartado de Correos 4021 E-30080 Murcia Spain Fax 34 968 36 4766 Tel 34 968 36 4766 E-mail jcgomez@um.es Present address BiomedicalResearch and Study Centre University of Latvia Riga Latvia Received 27 January 2006 revised 22 May 2006 accepted 23 May 2006 doi 10.1111 j.1742-4658.2006.05338.x The secondary structure of the catalytic domain from protein kinase C f was studied using IR spectroscopy. In the presence of the substrate MgATP there was a significant change in the secondary structure. After heating to 80 C a 14 decrease in the a-helix component was observed accompanied by a 6 decrease in the b-pleated sheet no change was observed in the large loops or in 310-helix plus associated loops. The maximum increase with heating was observed in the aggregated b-sheet component with an increase of 14 . In the presence of MgATP and compared with the sample heated in its absence there was a substantial decrease in the 310-helix plus associated loops and an increase in a-helix. Synchronous 2D-IR correlation showed that the main changes occurred at 1617 cm-1 which was assigned to changes in the intermolecular aggregated b-sheet of the denaturated protein. This increase was mainly correlated with the change in a-helix. In the presence of MgATP the main correlation was between aggregated b-sheet and the large loops component. The asynchronous 2D-correlation spectrum indicated that a number of components are transformed .