Synthesis of Linear Oligomers of (R)-3-Hydroxybutyrate and Solid-State Structural Investigations by electron microscopy and X-ray scattering

1994 ◽  
Vol 77 (4) ◽  
pp. 1099-1123 ◽  
Author(s):  
Dieter Seebach ◽  
H. Michael Bürger ◽  
Hans-Martin Müller ◽  
Urs D. Lengweiler ◽  
Albert K. Beck ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Solid State ◽  
Structural Investigations ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Multiscale Structural Elucidation of Peptide Nanotubes by X-Ray Scattering Methods

2021 ◽  
Vol 9 ◽  
Author(s):  
Theyencheri Narayanan ◽  
Axel Rüter ◽  
Ulf Olsson
Keyword(s):  
Electron Microscopy ◽  
Formation Mechanism ◽  
Structural Organization ◽  
The Self ◽  
Structural Investigations ◽  
Peptide Nanotubes ◽  
X Ray ◽  
X Ray Scattering ◽  
Molecular Scale ◽  
Ray Scattering

This mini-review presents the structural investigations of the self-assembled peptide nanotubes using X-ray scattering techniques. As compared to electron microscopy, scattering methods enable studies of nanotubes in solution under the appropriate physicochemical conditions and probe their formation mechanism. In addition, a combination of X-ray scattering methods allow the elucidation of structural organization from the molecular scale to the dimension of nanotubes.

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.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

scholarly journals Alpha helical surfactant-like peptides self-assemble into pH-dependent nanostructures

Soft Matter ◽  
2021 ◽  
Vol 17 (11) ◽  
pp. 3096-3104
Author(s):  
Valeria Castelletto ◽  
Jani Seitsonen ◽  
Janne Ruokolainen ◽  
Ian W. Hamley
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Small Angle ◽  
Self Assembly ◽  
X Ray ◽  
Cryogenic Transmission Electron Microscopy ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ph Dependent ◽  
Ray Scattering

A designed surfactant-like peptide is shown, using a combination of cryogenic-transmission electron microscopy and small-angle X-ray scattering, to have remarkable pH-dependent self-assembly properties.

scholarly journals Small angle x-ray scattering and electron microscopy of nanoparticles formed in an electrical arc

AIP Advances ◽  
2013 ◽  
Vol 3 (3) ◽  
pp. 032139 ◽  
Author(s):  
E. Carvou ◽  
J. L. Le Garrec ◽  
J. Pérez ◽  
J. Praquin ◽  
M. Djeddi ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Angle ◽  
X Ray ◽  
Electrical Arc ◽  
X Ray Scattering ◽  
Ray Scattering

Analysis of InGaN/GaN single quantum wells by X-ray scattering and transmission electron microscopy

2003 ◽  
Vol 240 (2) ◽  
pp. 297-300 ◽  
Author(s):  
T. M. Smeeton ◽  
M. J. Kappers ◽  
J. S. Barnard ◽  
M. E. Vickers ◽  
C. J. Humphreys
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Quantum Wells ◽  
Single Quantum ◽  
X Ray ◽  
X Ray Scattering ◽  
Transmission Electron ◽  
Ray Scattering

scholarly journals Structure of the Lassa Virus Nucleoprotein Revealed by X-ray Crystallography, Small-angle X-ray Scattering, and Electron Microscopy

2011 ◽  
Vol 286 (44) ◽  
pp. 38748-38756 ◽  
Author(s):  
Linda Brunotte ◽  
Romy Kerber ◽  
Weifeng Shang ◽  
Florian Hauer ◽  
Meike Hass ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Small Angle ◽  
Lassa Virus ◽  
X Ray ◽  
X Ray Crystallography ◽  
X Ray Scattering ◽  
Ray Scattering
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