[NMR paper] Rational Engineering of Photoconvertible Fluorescent Proteins for Dual-Color Fluorescence Nanoscopy Enabled by a Triplet-State Mechanism of Primed Conversion
Rational Engineering of Photoconvertible Fluorescent Proteins for Dual-Color Fluorescence Nanoscopy Enabled by a Triplet-State Mechanism of Primed Conversion
Green-to-red photoconvertible fluorescent proteins (pcFPs) are powerful tools for super-resolution localization microscopy and protein tagging. Recently, they have been found to undergo efficient photoconversion not only by the traditional 400-nm illumination but also by an alternative method termed primed conversion, employing dual wavelength illumination with blue and far-red/near-infrared light. Primed conversion has been...
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07-12-2017 12:48 AM
[NMR paper] A triplet state mechanism of primed conversion enables rational engineering of photoconvertible fluorescent proteins for dual color fluorescence nanoscopy
A triplet state mechanism of primed conversion enables rational engineering of photoconvertible fluorescent proteins for dual color fluorescence nanoscopy
Photoconvertible fluorescent proteins (pcFPs) are powerful tools for super-resolution localization microscopy and protein tagging. Recently, they have been found to undergo efficient photoconversion by an alternative method termed primed conversion, employing dual wavelength illumination with blue and far-red/near-infrared light. Primed conversion has been reported only for Dendra2 and its mechanism has remained elusive. Here, we...
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06-30-2017 05:34 AM
Molecular Dissection of the Forces Responsible forViral Capsid Assembly and Stabilization by Decoration Proteins
Molecular Dissection of the Forces Responsible forViral Capsid Assembly and Stabilization by Decoration Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00705/20170125/images/medium/bi-2016-00705u_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00705
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/j9Ibvk-KE98
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The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013
The second round of Critical Assessment of Automated Structure Determination of Proteins by NMR: CASD-NMR-2013
Abstract
The second round of the community-wide initiative Critical Assessment of automated Structure Determination of Proteins by NMR (CASD-NMR-2013) comprised ten blind target datasets, consisting of unprocessed spectral data, assigned chemical shift lists and unassigned NOESY peak and RDC lists, that were made available in both curated (i.e. manually refined) or un-curated (i.e. automatically generated) form. Ten structure calculation...
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06-13-2015 11:09 PM
[NMR paper] Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Related Articles Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Chemistry. 2013 Dec 9;19(50):17141-9
Authors: Huang F, Pei YY, Zuo HH, Chen JL, Yang Y, Su XC
Abstract
Site-specific labeling of proteins with lanthanide ions offers great opportunities for investigating the structure, function, and dynamics of proteins by virtue of the unique properties of lanthanides. Lanthanide-tagged proteins can be studied by NMR, X-ray, fluorescence, and EPR...
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12-07-2013 01:00 PM
[NMR paper] Evaluation of parameters critical to observing proteins inside living Escherichia col
Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
Related Articles Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
J Am Chem Soc. 2001 Sep 19;123(37):8895-901
Authors: Serber Z, Ledwidge R, Miller SM, Dötsch V
Our recently developed in-cell NMR procedure now enables one to observe protein conformations inside living cells. Optimization of the technique demonstrates that distinguishing the signals produced by a...
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11-19-2010 08:44 PM
[NMR paper] Conformation and orientation of the retinyl chromophore in rhodopsin: a critical eval
Conformation and orientation of the retinyl chromophore in rhodopsin: a critical evaluation of recent NMR data on the basis of theoretical calculations results in a minimum energy structure consistent with all experimental data.
Related Articles Conformation and orientation of the retinyl chromophore in rhodopsin: a critical evaluation of recent NMR data on the basis of theoretical calculations results in a minimum energy structure consistent with all experimental data.
Biochemistry. 2001 Apr 10;40(14):4201-4
Authors: Singh D, Hudson BS, Middleton C,...
Chromophore Isomer Stabilization Is Critical to theEfficient Fluorescence of Cyan Fluorescent Proteins
Linear Mode
