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

doi:10.1021/bi0484419

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

Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

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.

Original language	English (US)
Pages (from-to)	2409-2418
Number of pages	10
Journal	Biochemistry
Volume	44
Issue number	7
DOIs	https://doi.org/10.1021/bi0484419
State	Published - Feb 22 2005

ASJC Scopus subject areas

Biochemistry

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10.1021/bi0484419

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title = "Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin",

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.",

author = "Mildred Ortiz and Zuleika Sanoguet and Haitao Hu and Chazin, {Walter J.} and Cynthia McMurray and Salisbury, {Jeffrey L.} and Belinda Pastrana-Rios",

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AU - Ortiz, Mildred

AU - Sanoguet, Zuleika

AU - Hu, Haitao

AU - Chazin, Walter J.

AU - McMurray, Cynthia

AU - Salisbury, Jeffrey L.

AU - Pastrana-Rios, Belinda

PY - 2005/2/22

Y1 - 2005/2/22

N2 - 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.

AB - 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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ER -

Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin

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