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 journalArticle

17 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2409-2418
Number of pages10
JournalBiochemistry
Volume44
Issue number7
DOIs
StatePublished - Feb 22 2005

Fingerprint

Chlamydomonas
Deuterium
Sulfamethoxazole Drug Combination Trimethoprim
Hydrogen
Microtubule-Organizing Center
Basal Bodies
EF Hand Motifs
Chlamydomonas reinhardtii
Proteins
Calcium-Binding Proteins
Fourier Transform Infrared Spectroscopy
Calmodulin
Eukaryota
Ion exchange
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ortiz, M., Sanoguet, Z., Hu, H., Chazin, W. J., McMurray, C., Salisbury, J. L., & Pastrana-Rios, B. (2005). Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin. Biochemistry, 44(7), 2409-2418. https://doi.org/10.1021/bi0484419

Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin. / Ortiz, Mildred; Sanoguet, Zuleika; Hu, Haitao; Chazin, Walter J.; McMurray, Cynthia; Salisbury, Jeffrey L; Pastrana-Rios, Belinda.

In: Biochemistry, Vol. 44, No. 7, 22.02.2005, p. 2409-2418.

Research output: Contribution to journalArticle

Ortiz, M, Sanoguet, Z, Hu, H, Chazin, WJ, McMurray, C, Salisbury, JL & Pastrana-Rios, B 2005, 'Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin', Biochemistry, vol. 44, no. 7, pp. 2409-2418. https://doi.org/10.1021/bi0484419
Ortiz M, Sanoguet Z, Hu H, Chazin WJ, McMurray C, Salisbury JL et al. Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin. Biochemistry. 2005 Feb 22;44(7):2409-2418. https://doi.org/10.1021/bi0484419
Ortiz, Mildred ; Sanoguet, Zuleika ; Hu, Haitao ; Chazin, Walter J. ; McMurray, Cynthia ; Salisbury, Jeffrey L ; Pastrana-Rios, Belinda. / Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin. In: Biochemistry. 2005 ; Vol. 44, No. 7. pp. 2409-2418.
@article{7d1f2dad36de48c698ccae7718533920,
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",
year = "2005",
month = "2",
day = "22",
doi = "10.1021/bi0484419",
language = "English (US)",
volume = "44",
pages = "2409--2418",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "7",

}

TY - JOUR

T1 - Dynamics of hydrogen-deuterium exchange in Chlamydomonas centrin

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.

UR - http://www.scopus.com/inward/record.url?scp=14044277598&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=14044277598&partnerID=8YFLogxK

U2 - 10.1021/bi0484419

DO - 10.1021/bi0484419

M3 - Article

VL - 44

SP - 2409

EP - 2418

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 7

ER -