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Titolo:
Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions
Autore:
Vrzheshch, PV; Akovbian, NA; Varfolomeyev, SD; Verkhusha, VV;
Indirizzi:
Moscow State Univ, Ctr Mol Med, Moscow 119899, Russia Moscow State Univ Moscow Russia 119899 tr Mol Med, Moscow 119899, Russia Moscow State Univ, Fac Chem, Dept Chem Enzymol, Moscow 119899, Russia Moscow State Univ Moscow Russia 119899 em Enzymol, Moscow 119899, Russia
Titolo Testata:
FEBS LETTERS
fascicolo: 2, volume: 487, anno: 2000,
pagine: 203 - 208
SICI:
0014-5793(200012)487:2<203:DAPROA>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM; FLUORESCENT PROTEINS;
Keywords:
red fluorescent protein; pH dependence; denaturation; renaturation; tetramer; kinetics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Vrzheshch, PV Moscow State Univ, Ctr Mol Med, Vorobevy Gory, Moscow 119899, Russia Moscow State Univ Vorobevy Gory Moscow Russia 119899 Russia
Citazione:
P.V. Vrzheshch et al., "Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions", FEBS LETTER, 487(2), 2000, pp. 203-208

Abstract

The red fluorescent protein, DsRed, recently cloned from coral Discosoma sp. has one of the longest fluorescence waves and one of the most complex absorbance spectra among the family of fluorescent proteins. In this work we found that with time DsRed fluorescence decreases under mildly acidic conditions (pH 4.0-4.8) in a pH-dependent manner, and this fluorescence inactivation could be partially recovered by subsequent re-alkalization. The DsRed absorbance and circular dichroism spectra under these conditions revealed that the fluorescence changes were caused by denaturation followed by partial renaturation of the protein. Further, analytical ultracentrifugation determined that native DsRed formed a tight tetramer under various native conditions, Quantitative analysis of the data showed that several distinct states of protein exist during the fluorescence inactivation and recovery, and the inactivation of fluorescence can be caused by protonation of a single ionogenic group in each monomer of DsRed tetramer. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. Alt rights reserved.

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Documento generato il 05/12/20 alle ore 13:54:45