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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vrzheshch PV,Akovbian NA,Varfolomeyev SD,Verkhusha VVdoi
10.1016/s0014-5793(00)02344-9keywords:
subject
Has Abstractpub_date
2000-12-29 00:00:00pages
203-8issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02344-9journal_volume
487pub_type
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