An enhanced monomeric blue fluorescent protein with the high chemical stability of the chromophore.
Commonly used monomeric blue fluorescent proteins suffer from moderate brightness. The brightest of them, mTagBFP, has a notably low chemical stability over time. Prolonged incubation of mTagBFP leads to its transition from a blue fluorescent state with absorbance at 401 nm to a non-fluorescent stat...
Main Authors: | Oksana M Subach, Paula J Cranfill, Michael W Davidson, Vladislav V Verkhusha |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2011-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3234270?pdf=render |
Similar Items
-
Near-infrared PAINT localization microscopy via chromophore replenishment of phytochrome-derived fluorescent tag
by: Kai Lu, et al.
Published: (2024-04-01) -
Chemical control of excited-state reactivity of the anionic green fluorescent protein chromophore
by: Nanna H. List, et al.
Published: (2024-02-01) -
Structural Flexibility of the Monomeric Red Fluorescent Protein DsRed
by: Ki Hyun Nam
Published: (2024-01-01) -
mKikGR, a monomeric photoswitchable fluorescent protein.
by: Satoshi Habuchi, et al.
Published: (2008-01-01) -
Generation of monomeric reversibly switchable red fluorescent proteins for far-field fluorescence nanoscopy.
by: Stiel, A, et al.
Published: (2008)