Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin

Mildred Ortiz, Zuleika Sanoguet, Haitao Hu, Walter J. Chazin, Cynthia McMurray, Jeffrey L. Salisbury, Belinda Pastrana-Rios

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)2409-2418
Number of pages10
Issue number7
StatePublished - Feb 22 2005

ASJC Scopus subject areas

  • Biochemistry


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