The role of quarternary structure in fluorescent protein stability

Olesia V. Stepanenko, Vladislav Verkhusha, M. M. Shavlovskiǐ, T. D. Aleǐnikova, V. N. Uverskiǐ, I. M. Kuznetsova, K. K. Turoverov

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The stability of fluorescent proteins (FPs) is of great importance for their use as reporters in studies of gene expression, protein dynamics and localization in cell. A comparative analysis of conformational stability of fluorescent proteins, having different association state was done. The list of studied proteins includes EGFP (monomer of green fluorescent protein, GFP), zFP506 (tetramer GFP), mRFP1 and "dimer2" (monomer and dimmer of red fluorescent protein), DsRed1 (red tetramer). The character of fluorescence intensity changes induced by guanidine hydrochloride (GdnHCl) of these proteins differs significantly. Green tetramer zFP506 has been shown to be more stable than green monomer EGFP, red dimmer "dimer2" has been shown to be less stable than red tetramer DsRed1, while red monomer mRFP1 has been shown to be practically as stable as tetramer DsRedl. It is concluded that the quaternary structure, being an important stabilizing factor, does not represent the only circumstance dictating the dramatic variations between fluorescent proteins in their conformational stability.

Original languageEnglish (US)
Pages (from-to)1017-1027
Number of pages11
JournalTsitologiia.
Volume47
Issue number11
StatePublished - 2005
Externally publishedYes

Fingerprint

Protein Stability
Green Fluorescent Proteins
Proteins
Guanidine
Fluorescence
Gene Expression

ASJC Scopus subject areas

  • Histology

Cite this

Stepanenko, O. V., Verkhusha, V., Shavlovskiǐ, M. M., Aleǐnikova, T. D., Uverskiǐ, V. N., Kuznetsova, I. M., & Turoverov, K. K. (2005). The role of quarternary structure in fluorescent protein stability. Tsitologiia., 47(11), 1017-1027.

The role of quarternary structure in fluorescent protein stability. / Stepanenko, Olesia V.; Verkhusha, Vladislav; Shavlovskiǐ, M. M.; Aleǐnikova, T. D.; Uverskiǐ, V. N.; Kuznetsova, I. M.; Turoverov, K. K.

In: Tsitologiia., Vol. 47, No. 11, 2005, p. 1017-1027.

Research output: Contribution to journalArticle

Stepanenko, OV, Verkhusha, V, Shavlovskiǐ, MM, Aleǐnikova, TD, Uverskiǐ, VN, Kuznetsova, IM & Turoverov, KK 2005, 'The role of quarternary structure in fluorescent protein stability', Tsitologiia., vol. 47, no. 11, pp. 1017-1027.
Stepanenko OV, Verkhusha V, Shavlovskiǐ MM, Aleǐnikova TD, Uverskiǐ VN, Kuznetsova IM et al. The role of quarternary structure in fluorescent protein stability. Tsitologiia. 2005;47(11):1017-1027.
Stepanenko, Olesia V. ; Verkhusha, Vladislav ; Shavlovskiǐ, M. M. ; Aleǐnikova, T. D. ; Uverskiǐ, V. N. ; Kuznetsova, I. M. ; Turoverov, K. K. / The role of quarternary structure in fluorescent protein stability. In: Tsitologiia. 2005 ; Vol. 47, No. 11. pp. 1017-1027.
@article{a94ba0fe18404fd7a258ba07cd560306,
title = "The role of quarternary structure in fluorescent protein stability",
abstract = "The stability of fluorescent proteins (FPs) is of great importance for their use as reporters in studies of gene expression, protein dynamics and localization in cell. A comparative analysis of conformational stability of fluorescent proteins, having different association state was done. The list of studied proteins includes EGFP (monomer of green fluorescent protein, GFP), zFP506 (tetramer GFP), mRFP1 and {"}dimer2{"} (monomer and dimmer of red fluorescent protein), DsRed1 (red tetramer). The character of fluorescence intensity changes induced by guanidine hydrochloride (GdnHCl) of these proteins differs significantly. Green tetramer zFP506 has been shown to be more stable than green monomer EGFP, red dimmer {"}dimer2{"} has been shown to be less stable than red tetramer DsRed1, while red monomer mRFP1 has been shown to be practically as stable as tetramer DsRedl. It is concluded that the quaternary structure, being an important stabilizing factor, does not represent the only circumstance dictating the dramatic variations between fluorescent proteins in their conformational stability.",
author = "Stepanenko, {Olesia V.} and Vladislav Verkhusha and Shavlovskiǐ, {M. M.} and Aleǐnikova, {T. D.} and Uverskiǐ, {V. N.} and Kuznetsova, {I. M.} and Turoverov, {K. K.}",
year = "2005",
language = "English (US)",
volume = "47",
pages = "1017--1027",
journal = "Tsitologiya",
issn = "0041-3771",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "11",

}

TY - JOUR

T1 - The role of quarternary structure in fluorescent protein stability

AU - Stepanenko, Olesia V.

AU - Verkhusha, Vladislav

AU - Shavlovskiǐ, M. M.

AU - Aleǐnikova, T. D.

AU - Uverskiǐ, V. N.

AU - Kuznetsova, I. M.

AU - Turoverov, K. K.

PY - 2005

Y1 - 2005

N2 - The stability of fluorescent proteins (FPs) is of great importance for their use as reporters in studies of gene expression, protein dynamics and localization in cell. A comparative analysis of conformational stability of fluorescent proteins, having different association state was done. The list of studied proteins includes EGFP (monomer of green fluorescent protein, GFP), zFP506 (tetramer GFP), mRFP1 and "dimer2" (monomer and dimmer of red fluorescent protein), DsRed1 (red tetramer). The character of fluorescence intensity changes induced by guanidine hydrochloride (GdnHCl) of these proteins differs significantly. Green tetramer zFP506 has been shown to be more stable than green monomer EGFP, red dimmer "dimer2" has been shown to be less stable than red tetramer DsRed1, while red monomer mRFP1 has been shown to be practically as stable as tetramer DsRedl. It is concluded that the quaternary structure, being an important stabilizing factor, does not represent the only circumstance dictating the dramatic variations between fluorescent proteins in their conformational stability.

AB - The stability of fluorescent proteins (FPs) is of great importance for their use as reporters in studies of gene expression, protein dynamics and localization in cell. A comparative analysis of conformational stability of fluorescent proteins, having different association state was done. The list of studied proteins includes EGFP (monomer of green fluorescent protein, GFP), zFP506 (tetramer GFP), mRFP1 and "dimer2" (monomer and dimmer of red fluorescent protein), DsRed1 (red tetramer). The character of fluorescence intensity changes induced by guanidine hydrochloride (GdnHCl) of these proteins differs significantly. Green tetramer zFP506 has been shown to be more stable than green monomer EGFP, red dimmer "dimer2" has been shown to be less stable than red tetramer DsRed1, while red monomer mRFP1 has been shown to be practically as stable as tetramer DsRedl. It is concluded that the quaternary structure, being an important stabilizing factor, does not represent the only circumstance dictating the dramatic variations between fluorescent proteins in their conformational stability.

UR - http://www.scopus.com/inward/record.url?scp=33745484289&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745484289&partnerID=8YFLogxK

M3 - Article

C2 - 16706203

AN - SCOPUS:33745484289

VL - 47

SP - 1017

EP - 1027

JO - Tsitologiya

JF - Tsitologiya

SN - 0041-3771

IS - 11

ER -