scholarly journals β ‐ sheet assembly in amyloidogenic glutamic acid nanostructures: Insights from X‐ray scattering and infrared nanospectroscopy

2019 ◽  
Vol 25 (6) ◽  
pp. e3170 ◽  
Author(s):  
Lucas R. Mello ◽  
Ian W. Hamley ◽  
Antonio Miranda ◽  
Wendel A. Alves ◽  
Emerson R. Silva
Keyword(s):  
Glutamic Acid ◽  
X Ray ◽  
X Ray Scattering ◽  
Β Sheet ◽  
Ray Scattering

scholarly journals Aggregation State of Residual α-Helices and Their Influence on Physical Properties of S. c. ricini Native Fiber

Molecules ◽  
2019 ◽  
Vol 24 (20) ◽  
pp. 3741 ◽  
Author(s):  
Kelvin O. Moseti ◽  
Taiyo Yoshioka ◽  
Tsunenori Kameda ◽  
Yasumoto Nakazawa
Keyword(s):  
Deformation Behavior ◽  
Structural Transition ◽  
Strain Curve ◽  
Silk Fiber ◽  
Plateau Region ◽  
Aggregation State ◽  
X Ray ◽  
X Ray Scattering ◽  
Β Sheet ◽  
Ray Scattering

Formation of the α-helical conformation in the poly-l-alanine (PA) sequence regions, subsequent structural transition to β-sheet during natural spinning, and presence of residual α-helices in Samia cynthia ricini (S. c. ricini) native silk fiber have been experimentally proven. However, the aggregation state of the residual α-helices, and their influence on the mechanical deformation behavior in native fiber remain unclear. Here we show that the α-helices form an ordered aggregation state with a hexagonal packing in the aqueous solution, some of which remain during natural spinning. X-ray scattering and differential scanning calorimetry (DSC) analyses revealed occurrence of a structural transition of the residual α-helices to the β-sheet structure, accompanied by disappearance of the plateau region in the force-strain curve, due to heat-treatment at ~220 °C. On the basis of X-ray scattering before and after tensile stretching of S. c. ricini native silk, a direct connection between the plateau region and the α-helix to β-sheet structural transition was confirmed. Our findings demonstrate the importance of the PA sequence regions in fiber structure formation and their influence on the tensile deformation behavior of S. c. ricini silk, features believed to be essentially similar in other saturniid silks. We strongly believe the residual ordered α-helices to be strategically and systematically designed by S. c. ricini silkworms to impart flexibility in native silk fiber. We anticipate that these knowledge forms a basis for fruitful strategies in the design and development of amino acid sequences for artificial silks with desired mechanical properties.

Conformational analysis of broken rodlike chains. 2. Conformational analysis of poly(D-glutamic acid) in aqueous solution by small-angle x-ray scattering

1988 ◽  
Vol 21 (9) ◽  
pp. 2756-2760 ◽  
Author(s):  
Yoshio Muroga ◽  
Hiroyuki Tagawa ◽  
Yuzuru Hiragi ◽  
Tatzuo Ueki ◽  
Mikio Kataoka ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Conformational Analysis ◽  
Glutamic Acid ◽  
Small Angle ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

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?

X-ray scattering by 1D molecular Guinier-Preston zones in ordered smectic phases

1992 ◽  
Vol 2 (6) ◽  
pp. 899-913 ◽  
Author(s):  
Patrick Davidson ◽  
Elisabeth Dubois-Violette ◽  
Anne-Marie Levelut ◽  
Brigitte Pansu
Keyword(s):  
X Ray ◽  
X Ray Scattering ◽  
Smectic Phases ◽  
Ray Scattering

An X-ray Scattering Study of Laterally Modulated Structures: Investigation of Coherence and Resolution Effects with a Grating

1996 ◽  
Vol 6 (8) ◽  
pp. 1085-1094 ◽  
Author(s):  
A. Gibaud ◽  
J. Wang ◽  
M. Tolan ◽  
G. Vignaud ◽  
S. K. Sinha
Keyword(s):  
X Ray ◽  
X Ray Scattering ◽  
Modulated Structures ◽  
Scattering Study ◽  
Ray Scattering

Pixel detectors: New detectors for X-ray scattering

2002 ◽  
Vol 12 (6) ◽  
pp. 385-390 ◽  
Author(s):  
J.-F. Bérar ◽  
L. Blanquart ◽  
N. Boudet ◽  
P. Breugnon ◽  
B. Caillot ◽  
...  
Keyword(s):  
X Ray ◽  
X Ray Scattering ◽  
Pixel Detectors ◽  
Ray Scattering
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