Osmolyte Effects on the Conformational Dynamics of a DNA Hairpin at Ambient and Extreme Environmental Conditions

2017 ◽  
Vol 129 (18) ◽  
pp. 5127-5131 ◽  
Author(s):  
Satyajit Patra ◽  
Christian Anders ◽  
Nelli Erwin ◽  
Roland Winter
Keyword(s):  
Environmental Conditions ◽  
Conformational Dynamics ◽  
Dna Hairpin

Osmolyte Effects on the Conformational Dynamics of a DNA Hairpin at Ambient and Extreme Environmental Conditions

2017 ◽  
Vol 56 (18) ◽  
pp. 5045-5049 ◽  
Author(s):  
Satyajit Patra ◽  
Christian Anders ◽  
Nelli Erwin ◽  
Roland Winter
Keyword(s):  
Environmental Conditions ◽  
Conformational Dynamics ◽  
Dna Hairpin

FRET Fluctuation Spectroscopy:  Exploring the Conformational Dynamics of a DNA Hairpin Loop

2000 ◽  
Vol 104 (48) ◽  
pp. 11551-11555 ◽  
Author(s):  
Mark Ian Wallace ◽  
Liming Ying ◽  
Shankar Balasubramanian ◽  
David Klenerman
Keyword(s):  
Conformational Dynamics ◽  
Hairpin Loop ◽  
Dna Hairpin

Antagonistic effects of natural osmolyte mixtures and hydrostatic pressure on the conformational dynamics of a DNA hairpin probed at the single-molecule level

2018 ◽  
Vol 20 (19) ◽  
pp. 13159-13170 ◽  
Author(s):  
Satyajit Patra ◽  
Christian Anders ◽  
Paul Hendrik Schummel ◽  
Roland Winter
Keyword(s):  
Hydrostatic Pressure ◽  
Nucleic Acids ◽  
Single Molecule ◽  
Deep Sea ◽  
Conformational Dynamics ◽  
Dna Hairpin ◽  
Antagonistic Effects ◽  
Single Molecule Level

Osmolyte mixtures from deep sea organisms are able to rescue nucleic acids from pressure-induced unfolding.

scholarly journals NMR reveals light-induced changes in the dynamics of a photoswitchable fluorescent protein

2019 ◽  
Author(s):  
N. E. Christou ◽  
I. Ayala ◽  
K. Giandoreggio-Barranco ◽  
M. Byrdin ◽  
V. Adam ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Environmental Conditions ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Conformational Dynamics ◽  
X Ray ◽  
X Ray Crystallography ◽  
Dynamic View ◽  
Fluorescent State ◽  
Induced Changes

AbstractThe availability of fluorescent proteins with distinct phototransformation properties is crucial for a wide range of applications in advanced fluorescence microscopy and biotechnology. To rationally design new variants optimized for specific applications, a detailed understanding of the mechanistic features underlying phototransformation is essential. At present, little is known about the conformational dynamics of fluorescent proteins at physiological temperature, and how these dynamics contribute to the observed phototransformation properties. Here, we apply high-resolution NMR spectroscopy in solution combined with in-situ sample illumination at different wavelengths to investigate the conformational dynamics of rsFolder, a GFP-derived protein that can be reversibly switched between a green fluorescent state and a non-fluorescent state. Our results add a dynamic view to the static structures obtained by X-ray crystallography. Including NMR into the analytical toolbox used for fluorescent protein research provides new opportunities for investigating the effect of mutations or changes in the environmental conditions on the conformational dynamics of phototransformable fluorescent proteins, and their correlation with the observed photochemical and photophysical properties.SignificancePhoto-transformable Fluorescent Proteins (PTFPs) are essential tools for super-resolution (SR) microscopy. In practical applications, however, researchers often encounter problems when using PTFPs in a particular cellular context, because the environmental conditions (pH, temperature, redox potential, oxygen level, viscosity, …) affect their brightness, photostability, phototransformation kinetics, etc. Rational fluorescent protein engineering exploits the mechanistic information available from structural studies, mainly X-ray crystallography, in order to design new PTFP variants with improved properties for particular applications. Here we apply NMR spectroscopy in solution to investigate the light-induced changes in conformational dynamics of rsFolder, a reversibly switchable fluorescent protein. The dynamic view offered by NMR highlights protein regions that comprise potentially interesting mutation points for future mutagenesis campaigns.

scholarly journals Alteration of the Conformational Dynamics of a DNA Hairpin by α‐Synuclein in the Presence of Aqueous Two‐Phase Systems

2020 ◽  
Vol 26 (48) ◽  
pp. 10987-10991
Author(s):  
Sanjib K. Mukherjee ◽  
Jim‐Marcel Knop ◽  
Simone Möbitz ◽  
Roland H. A. Winter
Keyword(s):  
Conformational Dynamics ◽  
Dna Hairpin ◽  
Two Phase ◽  
Aqueous Two Phase Systems ◽  
Phase Systems

scholarly journals Correlative Single-Molecule Force-FRET Measurements of DNA Hairpin Conformational Dynamics

2021 ◽  
Vol 120 (3) ◽  
pp. 220a
Author(s):  
Nastaran Hadizadeh Yazdi ◽  
Jordi Cabanas-Danés ◽  
Sheema Rahmanseresht ◽  
Ann Mukhortava ◽  
Rosalie P.C. Driessen ◽  
...  
Keyword(s):  
Single Molecule ◽  
Conformational Dynamics ◽  
Dna Hairpin

Vibration Isolator System for Electron Microscope

1990 ◽  
Vol 48 (1) ◽  
pp. 182-183
Author(s):  
K. Ohi ◽  
M. Mizuno ◽  
T. Kasai ◽  
Y. Ohkura ◽  
K. Mizuno ◽  
...  
Keyword(s):  
Electron Microscope ◽  
Magnetic Fields ◽  
Environmental Conditions ◽  
Vibration Isolator ◽  
Air Conditioners ◽  
Vibration Isolators ◽  
Large Size ◽  
Electron Microscopes

In recent years, with electron microscopes coming into wider use, their installation environments do not necessarily give their performance full play. Their environmental conditions include air-conditioners, magnetic fields, and vibrations. We report a jointly developed entirely new vibration isolator which is effective against the vibrations transmitted from the floor.Conventionally, large-sized vibration isolators which need the digging of a pit have been used. These vibration isolators, however, are large present problems of installation and maintenance because of their large-size.Thus, we intended to make a vibration isolator which1) eliminates the need for changing the installation room2) eliminates the need of maintenance and3) are compact in size and easily installable.

Sign in / Sign up

Export Citation Format

Share Document