scholarly journals Studying structure and dynamics of self-assembled peptide nanostructures using fluorescence and super resolution microscopy

2017 ◽  
Vol 53 (53) ◽  
pp. 7294-7297 ◽  
Author(s):  
Sílvia Pujals ◽  
Kai Tao ◽  
Adrià Terradellas ◽  
Ehud Gazit ◽  
Lorenzo Albertazzi

Understanding the formation and properties of self-assembled peptide nanostructures is the basis for the design of new architectures for various applications.

ACS Nano ◽  
2016 ◽  
Vol 10 (5) ◽  
pp. 4973-4980 ◽  
Author(s):  
Lennart H. Beun ◽  
Lorenzo Albertazzi ◽  
Daan van der Zwaag ◽  
Renko de Vries ◽  
Martien A. Cohen Stuart

Author(s):  
Kalina L. Tosheva ◽  
Yue Yuan ◽  
Pedro M. Pereira ◽  
Siân Culley ◽  
Ricardo Henriques

Super-Resolution Microscopy enables non-invasive, molecule-specific imaging of the internal structure and dynamics of cells with sub-diffraction limit spatial resolution. One of its major limitations is the requirement for high-intensity illumination, generating considerable cellular phototoxicity. This factor considerably limits the capacity for live-cell observations, particularly for extended periods of time. Here, we overview new developments in hardware, software and probe chemistry aiming to reduce phototoxicity. Additionally, we discuss how the choice of biological model and sample environment impacts the capacity for live-cell observations.


Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 42-51
Author(s):  
S. S. Ryabichko ◽  
◽  
A. N. Ibragimov ◽  
L. A. Lebedeva ◽  
E. N. Kozlov ◽  
...  

2019 ◽  
Author(s):  
Jeffrey Chang ◽  
Matthew Romei ◽  
Steven Boxer

<p>Double-bond photoisomerization in molecules such as the green fluorescent protein (GFP) chromophore can occur either via a volume-demanding one-bond-flip pathway or via a volume-conserving hula-twist pathway. Understanding the factors that determine the pathway of photoisomerization would inform the rational design of photoswitchable GFPs as improved tools for super-resolution microscopy. In this communication, we reveal the photoisomerization pathway of a photoswitchable GFP, rsEGFP2, by solving crystal structures of <i>cis</i> and <i>trans</i> rsEGFP2 containing a monochlorinated chromophore. The position of the chlorine substituent in the <i>trans</i> state breaks the symmetry of the phenolate ring of the chromophore and allows us to distinguish the two pathways. Surprisingly, we find that the pathway depends on the arrangement of protein monomers within the crystal lattice: in a looser packing, the one-bond-flip occurs, whereas in a tighter packing (7% smaller unit cell size), the hula-twist occurs.</p><p> </p><p> </p><p> </p><p> </p><p> </p><p> </p> <p> </p>


2015 ◽  
Vol 9 (1-2) ◽  
pp. 161-170 ◽  
Author(s):  
Martin Lehmann ◽  
Gregor Lichtner ◽  
Haider Klenz ◽  
Jan Schmoranzer

Author(s):  
Philipp Werther ◽  
Klaus Yserentant ◽  
Felix Braun ◽  
Kristin Grußmayer ◽  
Vytautas Navikas ◽  
...  

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