Centrin: Its secondary structure in the presence and absence of cations

Belinda Pastrana-Rios, Wanda Ocaña, Michelle Rios, German Lorenzo Vargas, Ginny Ysa, Gregory Poynter, Javier Tapia, Jeffrey L Salisbury

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Centrin is a low molecular mass (20 kDa) protein that belongs to the EF-hand superfamily of calcium-binding proteins. Local and overall changes were investigated for interactions between cations and Chlamydomonas centrin using Fourier transform infrared (FT-IR) and circular dichroic (CD) spectroscopies. FT-IR spectral features studied included the amide I' band and the side-chain absorbances for aspartate residues located almost exclusively at the calcium-binding sites in the spectral region of 1700-1500 cm-1. The amide I′ band is exquisitely sensitive to changes in protein secondary structure and is observed to shift from 1626.5 to 1642.7 cm-1 in the presence and absence of calcium. These spectral bands are complex and were further studied using two-dimensional Fourier transform infrared (2D-FT-IR) correlation along with curve-fitting routines. Using these methods the secondary structure contributions were determined for holocentrin and apocentrin. The α-helical content in centrin was determined to be 60%-53% in the presence and absence of cations, respectively. Furthermore, the β-strand content was determined to be 12%-36%, while the random coil component remained almost constant at 7%-13.5% in the presence and absence of cations, respectively. Changes in the side-chain band are mostly due to the monodentate coordination of aspartate to the cation. A shift of ∼4 cm-1 (for the COO-antisymmetric stretch in Asp) from 1565 to 1569 cm-1 is observed for apocentrin and holocentrin, respectively. Thermal dependence revealed reversible conformational transition temperatures for apocentrin at 37 °C and holocentrin at 45 °C, suggesting greater stability for holocentrin.

Original languageEnglish (US)
Pages (from-to)6911-6919
Number of pages9
JournalBiochemistry
Volume41
Issue number22
DOIs
StatePublished - Jun 4 2002

Fingerprint

Sulfamethoxazole Drug Combination Trimethoprim
Fourier Analysis
Cations
Fourier transforms
Infrared radiation
Aspartic Acid
Amides
Calcium
EF Hand Motifs
Chlamydomonas
Secondary Protein Structure
Calcium-Binding Proteins
Transition Temperature
Curve fitting
Molecular mass
Spectrum Analysis
Proteins
Hot Temperature
Binding Sites
Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pastrana-Rios, B., Ocaña, W., Rios, M., Vargas, G. L., Ysa, G., Poynter, G., ... Salisbury, J. L. (2002). Centrin: Its secondary structure in the presence and absence of cations. Biochemistry, 41(22), 6911-6919. https://doi.org/10.1021/bi0157971

Centrin : Its secondary structure in the presence and absence of cations. / Pastrana-Rios, Belinda; Ocaña, Wanda; Rios, Michelle; Vargas, German Lorenzo; Ysa, Ginny; Poynter, Gregory; Tapia, Javier; Salisbury, Jeffrey L.

In: Biochemistry, Vol. 41, No. 22, 04.06.2002, p. 6911-6919.

Research output: Contribution to journalArticle

Pastrana-Rios, B, Ocaña, W, Rios, M, Vargas, GL, Ysa, G, Poynter, G, Tapia, J & Salisbury, JL 2002, 'Centrin: Its secondary structure in the presence and absence of cations', Biochemistry, vol. 41, no. 22, pp. 6911-6919. https://doi.org/10.1021/bi0157971
Pastrana-Rios B, Ocaña W, Rios M, Vargas GL, Ysa G, Poynter G et al. Centrin: Its secondary structure in the presence and absence of cations. Biochemistry. 2002 Jun 4;41(22):6911-6919. https://doi.org/10.1021/bi0157971
Pastrana-Rios, Belinda ; Ocaña, Wanda ; Rios, Michelle ; Vargas, German Lorenzo ; Ysa, Ginny ; Poynter, Gregory ; Tapia, Javier ; Salisbury, Jeffrey L. / Centrin : Its secondary structure in the presence and absence of cations. In: Biochemistry. 2002 ; Vol. 41, No. 22. pp. 6911-6919.
@article{4935d3f9871b4d89b275d37b756e927c,
title = "Centrin: Its secondary structure in the presence and absence of cations",
abstract = "Centrin is a low molecular mass (20 kDa) protein that belongs to the EF-hand superfamily of calcium-binding proteins. Local and overall changes were investigated for interactions between cations and Chlamydomonas centrin using Fourier transform infrared (FT-IR) and circular dichroic (CD) spectroscopies. FT-IR spectral features studied included the amide I' band and the side-chain absorbances for aspartate residues located almost exclusively at the calcium-binding sites in the spectral region of 1700-1500 cm-1. The amide I′ band is exquisitely sensitive to changes in protein secondary structure and is observed to shift from 1626.5 to 1642.7 cm-1 in the presence and absence of calcium. These spectral bands are complex and were further studied using two-dimensional Fourier transform infrared (2D-FT-IR) correlation along with curve-fitting routines. Using these methods the secondary structure contributions were determined for holocentrin and apocentrin. The α-helical content in centrin was determined to be 60{\%}-53{\%} in the presence and absence of cations, respectively. Furthermore, the β-strand content was determined to be 12{\%}-36{\%}, while the random coil component remained almost constant at 7{\%}-13.5{\%} in the presence and absence of cations, respectively. Changes in the side-chain band are mostly due to the monodentate coordination of aspartate to the cation. A shift of ∼4 cm-1 (for the COO-antisymmetric stretch in Asp) from 1565 to 1569 cm-1 is observed for apocentrin and holocentrin, respectively. Thermal dependence revealed reversible conformational transition temperatures for apocentrin at 37 °C and holocentrin at 45 °C, suggesting greater stability for holocentrin.",
author = "Belinda Pastrana-Rios and Wanda Oca{\~n}a and Michelle Rios and Vargas, {German Lorenzo} and Ginny Ysa and Gregory Poynter and Javier Tapia and Salisbury, {Jeffrey L}",
year = "2002",
month = "6",
day = "4",
doi = "10.1021/bi0157971",
language = "English (US)",
volume = "41",
pages = "6911--6919",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "22",

}

TY - JOUR

T1 - Centrin

T2 - Its secondary structure in the presence and absence of cations

AU - Pastrana-Rios, Belinda

AU - Ocaña, Wanda

AU - Rios, Michelle

AU - Vargas, German Lorenzo

AU - Ysa, Ginny

AU - Poynter, Gregory

AU - Tapia, Javier

AU - Salisbury, Jeffrey L

PY - 2002/6/4

Y1 - 2002/6/4

N2 - Centrin is a low molecular mass (20 kDa) protein that belongs to the EF-hand superfamily of calcium-binding proteins. Local and overall changes were investigated for interactions between cations and Chlamydomonas centrin using Fourier transform infrared (FT-IR) and circular dichroic (CD) spectroscopies. FT-IR spectral features studied included the amide I' band and the side-chain absorbances for aspartate residues located almost exclusively at the calcium-binding sites in the spectral region of 1700-1500 cm-1. The amide I′ band is exquisitely sensitive to changes in protein secondary structure and is observed to shift from 1626.5 to 1642.7 cm-1 in the presence and absence of calcium. These spectral bands are complex and were further studied using two-dimensional Fourier transform infrared (2D-FT-IR) correlation along with curve-fitting routines. Using these methods the secondary structure contributions were determined for holocentrin and apocentrin. The α-helical content in centrin was determined to be 60%-53% in the presence and absence of cations, respectively. Furthermore, the β-strand content was determined to be 12%-36%, while the random coil component remained almost constant at 7%-13.5% in the presence and absence of cations, respectively. Changes in the side-chain band are mostly due to the monodentate coordination of aspartate to the cation. A shift of ∼4 cm-1 (for the COO-antisymmetric stretch in Asp) from 1565 to 1569 cm-1 is observed for apocentrin and holocentrin, respectively. Thermal dependence revealed reversible conformational transition temperatures for apocentrin at 37 °C and holocentrin at 45 °C, suggesting greater stability for holocentrin.

AB - Centrin is a low molecular mass (20 kDa) protein that belongs to the EF-hand superfamily of calcium-binding proteins. Local and overall changes were investigated for interactions between cations and Chlamydomonas centrin using Fourier transform infrared (FT-IR) and circular dichroic (CD) spectroscopies. FT-IR spectral features studied included the amide I' band and the side-chain absorbances for aspartate residues located almost exclusively at the calcium-binding sites in the spectral region of 1700-1500 cm-1. The amide I′ band is exquisitely sensitive to changes in protein secondary structure and is observed to shift from 1626.5 to 1642.7 cm-1 in the presence and absence of calcium. These spectral bands are complex and were further studied using two-dimensional Fourier transform infrared (2D-FT-IR) correlation along with curve-fitting routines. Using these methods the secondary structure contributions were determined for holocentrin and apocentrin. The α-helical content in centrin was determined to be 60%-53% in the presence and absence of cations, respectively. Furthermore, the β-strand content was determined to be 12%-36%, while the random coil component remained almost constant at 7%-13.5% in the presence and absence of cations, respectively. Changes in the side-chain band are mostly due to the monodentate coordination of aspartate to the cation. A shift of ∼4 cm-1 (for the COO-antisymmetric stretch in Asp) from 1565 to 1569 cm-1 is observed for apocentrin and holocentrin, respectively. Thermal dependence revealed reversible conformational transition temperatures for apocentrin at 37 °C and holocentrin at 45 °C, suggesting greater stability for holocentrin.

UR - http://www.scopus.com/inward/record.url?scp=0037018917&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037018917&partnerID=8YFLogxK

U2 - 10.1021/bi0157971

DO - 10.1021/bi0157971

M3 - Article

C2 - 12033923

AN - SCOPUS:0037018917

VL - 41

SP - 6911

EP - 6919

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 22

ER -