Stress-induced Bimodal Ordering in POSS/PCL Biodegradable Shape Memory Nanocomposites

2012 ◽  
Vol 1450 ◽  
Author(s):  
Bonifacio Alvarado-Tenorio ◽  
Angel Romo-Uribe ◽  
Patrick T. Mather
Keyword(s):  
Shape Memory ◽  
Network Architecture ◽  
Crosslink Density ◽  
Room Temperature ◽  
Molar Ratio ◽  
Saxs Data ◽  
X Ray ◽  
X Ray Scattering ◽  
Shape Memory Properties ◽  
Induced Crystallization

ABSTRACTSimultaneous wide- and small- angle X-ray scattering (WAXS-SAXS) has revealed a stress-induced bimodal orientation of POSS crystals and PCL chains, both in a constrained POSS/PCL crosslinked network architecture with shape memory properties. POSS/PCL nanocomposites with molecular weight of 2,600 g/mol exhibiting shape memory behavior were synthesized and variation of crosslinker molar ratio was used to obtain POSS/PCL networks with different crosslink density (Alvarado-Tenorio et al., Macromolecules, 44, 5682, 2011). In that study it was shown that there are POSS crystals embedded in an amorphous PCL matrix, and the POSS crystals were ordered in a cubic nanostructure. In this work, it will be shown that elongation at room temperature of all the networks yielded a double-induced orientation (90º and 180º) of the POSS crystals, as indicated by the 101 reflection. Moreover, it was also detected stretched-induced crystallization of the otherwise amorphous PCL chains. Furthermore, SAXS data showed long periods in the meridional and equatorial orientations of 630 Å, 90 Å and 45 Å corresponding to a lamellar nanostructure of PCL chains. The induced bimodal orientation of the POSS-PCL molecular network will be correlated with its shape memory properties.

Stress-Induced Crystallization Properties of Natural and Synthetic CIS-Polyisoprene

2004 ◽  
Vol 77 (2) ◽  
pp. 303-316 ◽  
Author(s):  
S. Trabelsi ◽  
P.-A. Albouy ◽  
J. Rault
Keyword(s):  
Draw Ratio ◽  
Room Temperature ◽  
X Ray ◽  
X Ray Scattering ◽  
Synthetic Rubber ◽  
Chain Defects ◽  
Stress Induced Crystallization ◽  
Induced Crystallization ◽  
Melting And Crystallization Temperatures ◽  
Natural And Synthetic

Abstract Stress-induced crystallization and melting of natural and synthetic cis-isoprene are compared by simultaneous Wide Angles X-ray Scattering (WAXS) and mechanical measurements. Natural (NR) and synthetic polyisoprene (SR) rubbers have the same composition and sulfur crosslink density. At fixed elongation and during cyclic deformation, the properties X of the semi crystalline phase are determined as function of draw ratio λ; X being crystallites dimensions and orientation, half-time of crystallization, melting temperature, crystallinity and crystalline zone dimensions around a crack tip. It is shown that all the curves X(λ) of both types of rubber at room temperature can be superposed by a simple translation δλ along the draw ratio axis. This translation factor of the order of 0.5 to 1 does not depend on the property X. These effects are explained by the decrease of the melting and crystallization temperatures due to the presence of chain defects in synthetic rubber.

Structural refinement by restrained molecular-dynamics algorithm with small-angle X-ray scattering constraints for a biomolecule

2004 ◽  
Vol 37 (1) ◽  
pp. 103-109 ◽  
Author(s):  
Masaki Kojima ◽  
Alexander A. Timchenko ◽  
Junichi Higo ◽  
Kazuki Ito ◽  
Hiroshi Kihara ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Small Angle ◽  
Protein Structures ◽  
Saxs Data ◽  
X Ray ◽  
X Ray Scattering ◽  
Saxs Curve ◽  
Restrained Molecular Dynamics ◽  
Ray Scattering

A new algorithm to refine protein structures in solution from small-angle X-ray scattering (SAXS) data was developed based on restrained molecular dynamics (MD). In the method, the sum of squared differences between calculated and observed SAXS intensities was used as a constraint energy function, and the calculation was started from given atomic coordinates, such as those of the crystal. In order to reduce the contribution of the hydration effect to the deviation from the experimental (objective) curve during the dynamics, and purely as an estimate of the efficiency of the algorithm, the calculation was first performed assuming the SAXS curve corresponding to the crystal structure as the objective curve. Next, the calculation was carried out with `real' experimental data, which yielded a structure that satisfied the experimental SAXS curve well. The SAXS data for ribonuclease T1, a single-chain globular protein, were used for the calculation, along with its crystal structure. The results showed that the present algorithm was very effective in the refinement and adjustment of the initial structure so that it could satisfy the objective SAXS data.

scholarly journals Structural Analysis of the Partially Disordered Protein EspK from Mycobacterium tuberculosis

Crystals ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 18
Author(s):  
Abril Gijsbers ◽  
Nuria Sánchez-Puig ◽  
Ye Gao ◽  
Peter J. Peters ◽  
Raimond B. G. Ravelli ◽  
...  
Keyword(s):  
Host Response ◽  
Limited Proteolysis ◽  
Maximal Dimension ◽  
Globular Domain ◽  
Saxs Data ◽  
X Ray ◽  
Disordered Protein ◽  
X Ray Scattering ◽  
C Terminus ◽  
New Treatments

For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker.

Single-Crystal X-Ray Scattering Study of Superstructures and Phase Transitions in Graphite-Hno3 and Graphite-Br2 Intercalation Compounds

1982 ◽  
Vol 20 ◽  
Author(s):  
R. Moret ◽  
R. Comes ◽  
G. Furdin ◽  
H. Fuzellier ◽  
F. Rousseaux
Keyword(s):  
Phase Transitions ◽  
Low Temperature ◽  
Room Temperature ◽  
Temperature Phase ◽  
Temperature Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Temperature Liquid ◽  
Low Temperature Phase

ABSTRACTIn α-C5n-HNO3 the condensation of the room-temperature liquid-like diffuse ring associated with the disorder-order transition around 250 K is studied and the low-temperature. superstructure is examined.It is found that β-C8n-HNO3 exhibits an in-plane incommensurate order at room temperature.Two types of graphite-Br2 are found. Low-temperature phase transitions in C8Br are observed at T1 ≍ 277 K and T2 ≍ 297 K. The room-temperature structure of C14Br is reexamined. Special attention is given to diffuse scattering and incommensurability.

Fabrication of an Apatite/Collagen Composite Coating on the NiTi Shape Memory Alloy through Electrochemical Deposition and Coating Characterisation

2009 ◽  
Vol 618-619 ◽  
pp. 319-323 ◽  
Author(s):  
Parama Chakraborty Banerjee ◽  
Tao Sun ◽  
Jonathan H.W. Wong ◽  
Min Wang
Keyword(s):  
Shape Memory Alloy ◽  
Shape Memory ◽  
Composite Coating ◽  
Electrochemical Deposition ◽  
Room Temperature ◽  
Composite Coatings ◽  
Deposition Process ◽  
Niti Shape Memory Alloy ◽  
X Ray ◽  
Niti Sma

To improve the biocompatibility and bioactivity of NiTi shape memory alloy (SMA), apatite/collagen composite coatings were fabricated on the surface of NiTi SMA at room temperature using the electrochemical deposition technique. Spherical apatite particles and fibrous collagen that formed the composite coating were visible under scanning electron microscope (SEM). The Ca/P ratio of the apatite component in the coating, as determined by energy dispersive X-ray spectroscopy (EDX), was about 1.38 which is slightly higher than that of octocalcium phosphate (OCP). X-ray diffraction result showed that the apatite was amorphous, which was due to the low temperature (i.e., room temperature) deposition process. The structure of the composite coatings was further characterized using Fourier transform infrared reflection spectroscopy (FTIR). It was also found that, compared to bare NiTi SMA samples, the wettability of as-deposited samples was increased because of the formation of the composite coating.

scholarly journals Universal nature of collapsibility in the context of protein folding and evolution

2018 ◽  
Author(s):  
D. Thirumalai ◽  
Himadri S. Samanta ◽  
Hiranmay Maity ◽  
Govardhan Reddy
Keyword(s):  
Single Molecule ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Saxs Data ◽  
X Ray ◽  
Model Free ◽  
X Ray Scattering ◽  
Theoretical Predictions ◽  
Helical Proteins ◽  
Universal Nature

AbstractTheory and simulations predicted sometime ago that the sizes of unfolded states of globular proteins should decrease continuously as the denaturant concentration is shifted from a high to a low value. However, small angle X-ray scattering (SAXS) data were used to assert the opposite, while interpretation of single molecule Forster resonance energy transfer experiments (FRET) supported the theoretical predictions. The disagreement between the two experiments is the SAXS-FRET controversy. By harnessing recent advances in SAXS and FRET experiments and setting these findings in the context of a general theory and simulations, we establish that compaction of unfolded states is universal. The theory also predicts that proteins rich in β-sheets are more collapsible than α-helical proteins. Because the extent of compaction is small, experiments have to be accurate and their interpretations should be as model free as possible. Theory also suggests that collapsibility itself could be a physical restriction on the evolution of foldable sequences, and provides a physical basis for the origin of multi-domain proteins.

scholarly journals Plasmodium falciparum Kelch13 and its artemisinin-resistant mutants assemble as hexamers in solution: a SAXS data driven shape restoration study

2021 ◽  
Author(s):  
Nainy Goel ◽  
Kanika Dhiman ◽  
Nidhi Kalidas ◽  
Anwesha Mukhopadhyay ◽  
Ashish ◽  
...  
Keyword(s):  
Artemisinin Resistance ◽  
Resistant Mutant ◽  
Data Driven ◽  
Wild Type ◽  
Saxs Data ◽  
Mutant Proteins ◽  
X Ray ◽  
X Ray Scattering ◽  
Shape Restoration ◽  
Spatial Positioning

AbstractArtemisinin-resistant mutations in PfKelch13 identified worldwide are mostly confined to its BTB/POZ and KRP domains. To date, only two crystal structures of the BTB/POZ-KRP domains as tight dimers are available, which limits structure-based interpretations of its functionality. Our solution Small-Angle X-ray Scattering (SAXS) data driven shape restoration of larger length of protein brought forth that: i) PfKelch13 forms a stable hexamer in P6 symmetry, ii) interactions of the N-termini drive the hexameric assembly, and iii) the six KRP domains project independently in space, forming a cauldron-like architecture. While artemisinin-sensitive mutant A578S packed like the wild-type, hexameric assemblies of dominant artemisinin-resistant mutant proteins R539T and C580Y displayed detectable differences in spatial positioning of their BTB/POZ-KRP domains. Lastly, mapping of mutations known to enable artemisinin resistance explained that most mutations exist mainly in these domains because they are non-detrimental to assembly of mutant PfKelch13 and yet can alter the flux of downstream events essential for susceptibility to artemisinin.

A portable extruder forin situwide angle x-ray scattering study on multi-dimensional flow field induced crystallization of polymer

2018 ◽  
Vol 89 (2) ◽  
pp. 025101 ◽  
Author(s):  
Jiarui Chang ◽  
Zhen Wang ◽  
Xiaoliang Tang ◽  
Fucheng Tian ◽  
Ke Ye ◽  
...  
Keyword(s):  
Flow Field ◽  
X Ray ◽  
Dimensional Flow ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Induced Crystallization ◽  
Ray Scattering
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