Reversible biomechano-responsive surface based on green fluorescent protein genetically modified with unnatural amino acids

2015 ◽  
Vol 51 (1) ◽  
pp. 232-235 ◽  
Author(s):  
Johan Longo ◽  
Chunyan Yao ◽  
César Rios ◽  
Nguyet Trang Thanh Chau ◽  
Fouzia Boulmedais ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Fluorescence Intensity ◽  
Unnatural Amino Acids ◽  
Fluorescent Protein ◽  
Genetically Modified ◽  
Uniaxial Stretching ◽  
Green Fluorescent

Uniaxial stretching of modified GFP “clicked” onto an elastomer leads to a repeatable and reversible decrease of its fluorescence intensity.

Structural and spectrophotometric investigation of two unnatural amino-acid altered chromophores in the superfolder green fluorescent protein

2021 ◽  
Vol 77 (8) ◽  
Author(s):  
Gregory M. Olenginski ◽  
Juliana Piacentini ◽  
Darcy R. Harris ◽  
Nicolette A. Runko ◽  
Brianna M. Papoutsis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Amino Acid ◽  
Unnatural Amino Acids ◽  
Fluorescent Protein ◽  
Photophysical Properties ◽  
Unnatural Amino Acid ◽  
Green Fluorescent ◽  
Absorbance Band ◽  
Protein Constructs

The spectrophotometric properties of the green fluorescent protein (GFP) result from the post-translationally cyclized chromophore composed of three amino acids including a tyrosine at the center of the β-barrel protein. Altering the amino acids in the chromophore or the nearby region has resulted in numerous GFP variants with differing photophysical properties. To further examine the effect of small atomic changes in the chromophore on the structure and photophysical properties of GFP, the hydroxyl group of the chromophore tyrosine was replaced with a nitro or a cyano group. The structures and spectrophotometric properties of these superfolder GFP (sfGFP) variants with the unnatural amino acids (UAAs) 4-nitro-L-phenylalanine or 4-cyano-L-phenylalanine were explored. Notably, the characteristic 487 nm absorbance band of wild-type (wt) sfGFP is absent in both unnatural amino-acid-containing protein constructs (Tyr66pNO2Phe-sfGFP and Tyr66pCNPhe-sfGFP). Consequently, neither Tyr66pNO2Phe-sfGFP nor Tyr66pCNPhe-sfGFP exhibited the characteristic emission of wt sfGFP centered at 511 nm when excited at 487 nm. Tyr66pNO2Phe-sfGFP appeared orange due to an absorbance band centered at 406 nm that was not present in wt sfGFP, while Tyr66pCNPhe-sfGFP appeared colorless with an absorbance band centered at 365 nm. Mass spectrometry and X-ray crystallography confirmed the presence of a fully formed chromophore and no significant structural changes in either of these UAA-containing protein constructs, signaling that the change in the observed photophysical properties of the proteins is the result of the presence of the UAA in the chromophore.

scholarly journals Fluorescence Modulation of Green Fluorescent Protein Using Fluorinated Unnatural Amino Acids

Molecules ◽  
2017 ◽  
Vol 22 (7) ◽  
pp. 1194 ◽  
Author(s):  
Jordan K. Villa ◽  
Hong-Anh Tran ◽  
Megha Vipani ◽  
Stephanie Gianturco ◽  
Konark Bhasin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Unnatural Amino Acids ◽  
Fluorescent Protein ◽  
Fluorescence Modulation ◽  
Green Fluorescent

scholarly journals Tuning the Photophysical Properties of the Green Fluorescent Protein with Unnatural Amino Acids

2015 ◽  
Vol 108 (2) ◽  
pp. 624a
Author(s):  
Gregory M. Olenginski ◽  
Christine M. Phillips-Piro ◽  
Scott H. Brewer
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Unnatural Amino Acids ◽  
Fluorescent Protein ◽  
Photophysical Properties ◽  
Green Fluorescent

scholarly journals Cellular Targets of Functional and Dysfunctional Mutants of Tobacco Mosaic Virus Movement Protein Fused to Green Fluorescent Protein

2000 ◽  
Vol 74 (23) ◽  
pp. 11339-11346 ◽  
Author(s):  
Vitaly Boyko ◽  
Jessica van der Laak ◽  
Jacqueline Ferralli ◽  
Elena Suslova ◽  
Myoung-Ok Kwon ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Tobacco Mosaic Virus ◽  
Inclusion Bodies ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Leading Edge ◽  
Intercellular Transport ◽  
C Terminus ◽  
Green Fluorescent

ABSTRACT Intercellular transport of tobacco mosaic virus (TMV) RNA involves the accumulation of virus-encoded movement protein (MP) in plasmodesmata (Pd), in endoplasmic reticulum (ER)-derived inclusion bodies, and on microtubules. The functional significance of these interactions in viral RNA (vRNA) movement was tested in planta and in protoplasts with TMV derivatives expressing N- and C-terminal deletion mutants of MP fused to the green fluorescent protein. Deletion of 55 amino acids from the C terminus of MP did not interfere with the vRNA transport function of MP:GFP but abolished its accumulation in inclusion bodies, indicating that accumulation of MP at these ER-derived sites is not a requirement for function in vRNA intercellular movement. Deletion of 66 amino acids from the C terminus of MP inactivated the protein, and viral infection occurred only upon complementation in plants transgenic for MP. The functional deficiency of the mutant protein correlated with its inability to associate with microtubules and, independently, with its absence from Pd at the leading edge of infection. Inactivation of MP by N-terminal deletions was correlated with the inability of the protein to target Pd throughout the infection site, whereas its associations with microtubules and inclusion bodies were unaffected. The observations support a role of MP-interacting microtubules in TMV RNA movement and indicate that MP targets microtubules and Pd by independent mechanisms. Moreover, accumulation of MP in Pd late in infection is insufficient to support viral movement, confirming that intercellular transport of vRNA relies on the presence of MP in Pd at the leading edge of infection.

scholarly journals Episodic Bursting Activity and Response to Excitatory Amino Acids in Acutely Dissociated Gonadotropin-Releasing Hormone Neurons Genetically Targeted with Green Fluorescent Protein

2002 ◽  
Vol 22 (6) ◽  
pp. 2313-2322 ◽  
Author(s):  
M. Cathleen Kuehl-Kovarik ◽  
Wendy A. Pouliot ◽  
Gloriana L. Halterman ◽  
Robert J. Handa ◽  
F. Edward Dudek ◽  
...  
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Excitatory Amino Acids ◽  
Fluorescent Protein ◽  
Gonadotropin Releasing Hormone ◽  
Releasing Hormone ◽  
Green Fluorescent ◽  
Bursting Activity

1258 POSTER Phase I Clinical Trial of a Genetically Modified Oncolytic Vaccinia Virus GL-ONC1 With Green Fluorescent Protein Imaging

2011 ◽  
Vol 47 ◽  
pp. S162 ◽  
Author(s):  
A. Biondo ◽  
J.V. Pedersen ◽  
E.M. Karapanagiotou ◽  
N. Tunariu ◽  
D. Mansfield ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Green Fluorescent Protein ◽  
Phase I ◽  
Vaccinia Virus ◽  
Fluorescent Protein ◽  
Genetically Modified ◽  
Phase I Clinical Trial ◽  
Protein Imaging ◽  
Green Fluorescent ◽  
Green Fluorescent Protein Imaging

A phase I clinical trial of a genetically modified and imageable oncolytic vaccinia virus GL-ONC1 with clinical green fluorescent protein (GFP) imaging.

2011 ◽  
Vol 29 (15_suppl) ◽  
pp. 2577-2577 ◽  
Author(s):  
J. V. Pedersen ◽  
E. M. Karapanagiotou ◽  
A. Biondo ◽  
N. Tunariu ◽  
M. Puglisi ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Green Fluorescent Protein ◽  
Phase I ◽  
Vaccinia Virus ◽  
Fluorescent Protein ◽  
Genetically Modified ◽  
Phase I Clinical Trial ◽  
Green Fluorescent

Experimental Evolution of a Green Fluorescent Protein Composed of 19 Unique Amino Acids without Tryptophan

2014 ◽  
Vol 44 (2) ◽  
pp. 75-86 ◽  
Author(s):  
Akio Kawahara-Kobayashi ◽  
Mitsuhiro Hitotsuyanagi ◽  
Kazuaki Amikura ◽  
Daisuke Kiga
Keyword(s):  
Amino Acids ◽  
Green Fluorescent Protein ◽  
Experimental Evolution ◽  
Fluorescent Protein ◽  
Green Fluorescent
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