Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin |
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Authors: | Ortiz Mildred Sanoguet Zuleika Hu Haitao Chazin Walter J McMurray Cynthia T McMurray Cynthia Salisbury Jeffrey L Pastrana-Rios Belinda |
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Institution: | Department of Chemistry and Center for Protein Structure Function and Dynamics, University of Puerto Rico, Mayagüez Campus, P.O. Box 9019, Mayagüez, Puerto Rico 00681-9019. |
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Abstract: | Chlamydomonas reinhardtii centrin is a 169-amino acid residue calcium binding protein belonging to the EF-hand protein superfamily. Centrin is associated with the microtubule organizing center (MTOC) in all eukaryotes, and in Chlamydomonas, centrin is a component of the flagellar basal body apparatus. Recombinant full-length centrin, calmodulin, and terminal domain fragments Ccen-N (residues 1-94) and Ccen-C (residues 99-169)] were used to examine hydrogen-deuterium (H --> D) exchange dynamics using combined attenuated total reflectance (ATR) Fourier transform-infrared (FT-IR) spectroscopy, curve fit, and two-dimensional correlation analysis. Analysis of the Ccen-N and Ccen-C fragments allowed separation of domain specific solvent exchange events and together with analysis of the full-length proteins provides novel insight into domain accessibility to the aqueous environment and the internal dynamics of the protein. |
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