The effect of temperature on the fine structural characteristics of cotton fibre – a small-angle X-ray scattering investigation using correlation functions

1991 ◽  
Vol 24 (5) ◽  
pp. 712-714 ◽  
Author(s):  
T. Misra ◽  
D. K. Bisoyi ◽  
Md. N. Khan ◽  
T. Patel
1991 ◽  
Vol 24 (6) ◽  
pp. 1062-1062
Author(s):  
T. Misra ◽  
D. K. Bisoyi ◽  
Md. N. Khan ◽  
T. Patel

Owing to a typsetting error, the heading ER was wrongly mis-set as Eg in Table 1 of the paper by Misra, Bisoyi, Khan & Patel [J. Appl. Cryst. (1991), 24, 712–714]. The correct table is given.


1993 ◽  
Vol 32 (Part 1, No. 10) ◽  
pp. 4615-4621 ◽  
Author(s):  
Tripurari Misra ◽  
Pramoda Panda ◽  
Tnkadhar Patel ◽  
Dillip K. Bisoyi ◽  
Dillip K. Panda

2014 ◽  
Vol 213 ◽  
pp. 216-221
Author(s):  
Anna N. Galkina ◽  
Alexander A. Sergeev

The strucrture of CdS quantum dots 0,3% (mass), stabilized by the solution of the mercaptosuccinic acid in the gel matrix 50% THEOS is investigated by small-angle X-ray scattering (SAXS). Application of modern methods of SAXS data interpretation, including procedure of ab initio modeling of particle structure, allowed us for the to reveal structural organization of both individual nanoparticles and of their clusters incorporated in the polymer matrix. As a result, the shape, size, and size distribution of the obtained nanoparticles and their clusters depended on the structure of the gel matrix used as a formation medium.


1995 ◽  
Vol 28 (5) ◽  
pp. 546-552 ◽  
Author(s):  
R. B. Knott ◽  
M. Capel ◽  
S. Hansen ◽  
R. E. Handschumacher

The small-angle X-ray scattering (SAXS) technique was used to investigate structural characteristics of the protein cyclophilin in solution and to attempt to detect major changes induced by the binding of the immunosuppressant drug cyclosporin A. Maximum-entropy methods were used to analyse the experimental SAXS data. The measured radius of gyration, Rg , for cyclophilin is 16.3 (5) Å. This is equivalent to a compact sphere of radius 21.0 Å. There is qualitative agreement between the experimental SAXS profiles and the derived distance-distribution function, p(r), for cyclophilin, and similar profiles calculated from the crystallographic structure. The notable discrepancy is the difference of approximately 1.5 Å in the estimated radius of the equivalent sphere. On binding cyclosporin A, the main structure-related change in cyclophilin observed under these experimental conditions is an increased propensity to form oligomers. Meaningful estimates of Rg for the monomeric complex are not possible because of the presence of a significant population of aggregates. In a second series of experiments, both native cyclophilin and the cyclophilin/cyclosporin A complex readily formed aggregates under the prevailing experimental conditions.


Cellulose ◽  
2005 ◽  
Vol 12 (5) ◽  
pp. 469-477 ◽  
Author(s):  
Yoshiaki Yuguchi ◽  
Takahiro Hirotsu ◽  
Jun Hosokawa

2019 ◽  
Author(s):  
Christian Prehal ◽  
Aleksej Samojlov ◽  
Manfred Nachtnebel ◽  
Manfred Kriechbaum ◽  
Heinz Amenitsch ◽  
...  

<b>Here we use in situ small and wide angle X-ray scattering to elucidate unexpected mechanistic insights of the O2 reduction mechanism in Li-O2 batteries.<br></b>


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