Time-Resolved Detection of Intermolecular Interaction of Photosensor Proteins

2009 ◽  
pp. 149-172
Author(s):  
M. Terazima
Keyword(s):  
Intermolecular Interaction ◽  
Time Resolved

Comparison between pyrrolidinium-based and imidazolium-based dicationic ionic liquids: intermolecular interaction, structural organization, and solute dynamics

2021 ◽  
Vol 23 (37) ◽  
pp. 21029-21041
Author(s):  
Amita Mahapatra ◽  
Manjari Chakraborty ◽  
Sahadev Barik ◽  
Moloy Sarkar
Keyword(s):  
Ionic Liquids ◽  
Steady State ◽  
Nmr Spectroscopy ◽  
Intermolecular Interaction ◽  
Structural Organization ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Dicationic Ionic Liquids ◽  
The Difference ◽  
Solute Dynamics

This work investigates the difference in the microscopic behaviour of imidazolium and pyrrolidinium based ILs employing combined steady state and time-resolved fluorescence, EPR and NMR spectroscopy.

scholarly journals 3P240 Time-resolved study on the intermolecular interaction change in the signal transduction of LOV protein YtvA(18A. Photobiology: Vision & Photoreception,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S251
Author(s):  
Seokwoo Choi ◽  
Yusuke Nakasone ◽  
Klaas Hellingwerf ◽  
Masahide Terazima
Keyword(s):  
Signal Transduction ◽  
Intermolecular Interaction ◽  
Time Resolved ◽  
Interaction Change

scholarly journals A Time-Resolved Diffusion Technique for Detection of the Conformational Changes and Molecular Assembly/Disassembly Processes of Biomolecules

2021 ◽  
Vol 12 ◽  
Author(s):  
Yusuke Nakasone ◽  
Masahide Terazima
Keyword(s):  
Intermolecular Interaction ◽  
Conformational Changes ◽  
Molecular Mechanisms ◽  
Dna Interaction ◽  
Molecular Assembly ◽  
Kinetic Measurements ◽  
Time Resolved ◽  
Molecular Events ◽  
Diffusion Technique ◽  
Sensor Proteins

Biological liquid–liquid phase separation (LLPS) is driven by dynamic and multivalent interactions, which involves conformational changes and intermolecular assembly/disassembly processes of various biomolecules. To understand the molecular mechanisms of LLPS, kinetic measurements of the intra- and intermolecular reactions are essential. In this review, a time-resolved diffusion technique which has a potential to detect molecular events associated with LLPS is presented. This technique can detect changes in protein conformation and intermolecular interaction (oligomer formation, protein-DNA interaction, and protein-lipid interaction) in time domain, which are difficult to obtain by other methods. After the principle and methods for signal analyses are described in detail, studies on photoreactive molecules (intermolecular interaction between light sensor proteins and its target DNA) and a non-photoreactive molecule (binding and folding reaction of α-synuclein upon mixing with SDS micelle) are presented as typical examples of applications of this unique technique.

Microtubule nucleation sequence studied by time-resolved x-ray scattering and electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 766-767
Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas
Keyword(s):  
Electron Microscopy ◽  
Dynamic Equilibrium ◽  
Time Resolved ◽  
X Ray ◽  
Additional Information ◽  
X Ray Scattering ◽  
Low Concentrations ◽  
Microtubule Growth ◽  
Ray Patterns ◽  
Ray Scattering

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.

Electron Channeling Patterns

1977 ◽  
Vol 35 ◽  
pp. 12-13
Author(s):  
David C. Joy
Keyword(s):  
Electron Diffraction ◽  
Incidence Angle ◽  
Photographic Plate ◽  
Diffraction Effect ◽  
Angle Of Incidence ◽  
Bulk Single Crystal ◽  
Time Resolved ◽  
Electron Channeling ◽  
Spatially Resolved ◽  
Large Bulk

Electron channeling patterns (ECP) were first found by Coates (1967) while observing a large bulk, single crystal of silicon in a scanning electron microscope. The geometric pattern visible was shown to be produced as a result of the changes in the angle of incidence, between the beam and the specimen surface normal, which occur when the sample is examined at low magnification (Booker, Shaw, Whelan and Hirsch 1967).A conventional electron diffraction pattern consists of an angularly resolved intensity distribution in space which may be directly viewed on a fluorescent screen or recorded on a photographic plate. An ECP, on the other hand, is produced as the result of changes in the signal collected by a suitable electron detector as the incidence angle is varied. If an integrating detector is used, or if the beam traverses the surface at a fixed angle, then no channeling contrast will be observed. The ECP is thus a time resolved electron diffraction effect. It can therefore be related to spatially resolved diffraction phenomena by an application of the concepts of reciprocity (Cowley 1969).

Time-resolved high-resolution electron microscopy of structural stability in mgo clusters

1996 ◽  
Vol 54 ◽  
pp. 672-673
Author(s):  
T. Kizuka ◽  
N. Tanaka
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Magnesium Oxide ◽  
Structural Stability ◽  
High Resolution Electron Microscopy ◽  
Video Tape ◽  
Solid State Physics ◽  
Time Resolved ◽  
Resolution Electron ◽  
Structural And Functional Properties

Structure and stability of atomic clusters have been studied by time-resolved high-resolution electron microscopy (TRHREM). Typical examples are observations of structural fluctuation in gold (Au) clusters supported on silicon oxide films, graphtized carbon films and magnesium oxide (MgO) films. All the observations have been performed on the clusters consisted of single metal element. Structural stability of ceramics clusters, such as metal-oxide, metal-nitride and metal-carbide clusters, has not been observed by TRHREM although the clusters show anomalous structural and functional properties concerning to solid state physics and materials science.In the present study, the behavior of ceramic, magnesium oxide (MgO) clusters is for the first time observed by TRHREM at 1/60 s time resolution and at atomic resolution down to 0.2 nm.MgO and gold were subsequently deposited on sodium chloride (001) substrates. The specimens, single crystalline MgO films on which Au particles were dispersed were separated in distilled water and observed by using a 200-kV high-resolution electron microscope (JEOL, JEM2010) equipped with a high sensitive TV camera and a video tape recorder system.

Cryo-TEM of amphiphilic polymer and amphiphile/polymer solutions

1993 ◽  
Vol 51 ◽  
pp. 876-877
Author(s):  
Yeshayahu Talmon
Keyword(s):  
Microstructural Characterization ◽  
Building Blocks ◽  
Quantitative Information ◽  
Physical Models ◽  
Specimen Preparation ◽  
Time Resolved ◽  
Temperature Changes ◽  
Temperature And Humidity ◽  
Microstructured Fluids ◽  
Air Streams

To achieve complete microstructural characterization of self-aggregating systems, one needs direct images in addition to quantitative information from non-imaging, e.g., scattering or Theological measurements, techniques. Cryo-TEM enables us to image fluid microstructures at better than one nanometer resolution, with minimal specimen preparation artifacts. Direct images are used to determine the “building blocks” of the fluid microstructure; these are used to build reliable physical models with which quantitative information from techniques such as small-angle x-ray or neutron scattering can be analyzed.To prepare vitrified specimens of microstructured fluids, we have developed the Controlled Environment Vitrification System (CEVS), that enables us to prepare samples under controlled temperature and humidity conditions, thus minimizing microstructural rearrangement due to volatile evaporation or temperature changes. The CEVS may be used to trigger on-the-grid processes to induce formation of new phases, or to study intermediate, transient structures during change of phase (“time-resolved cryo-TEM”). Recently we have developed a new CEVS, where temperature and humidity are controlled by continuous flow of a mixture of humidified and dry air streams.

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