Synthesis, Biological Activity, and NMR-Based Structural Studies of Deltorphin I Analogs Modified in Message Domain with a Newα,α-Disubstituted Glycines

2016 ◽  
Vol 87 (6) ◽  
pp. 824-832 ◽  
Author(s):  
Anika Lasota ◽  
Oliwia Frączak ◽  
Adriana Muchowska ◽  
Michał Nowakowski ◽  
Maciej Maciejczyk ◽  
...  
2017 ◽  
Vol 176 ◽  
pp. 8-16 ◽  
Author(s):  
Aleksandra Drzewiecka-Antonik ◽  
Paweł Rejmak ◽  
Marcin T. Klepka ◽  
Anna Wolska ◽  
Piotr Pietrzyk ◽  
...  

2005 ◽  
Vol 41 (2) ◽  
pp. 117-140 ◽  
Author(s):  
V. I. Lutskii ◽  
A. S. Gromova ◽  
E. A. Khamidullina ◽  
N. L. Owen

2015 ◽  
Vol 145 ◽  
pp. 94-100 ◽  
Author(s):  
Marcin T. Klepka ◽  
Aleksandra Drzewiecka-Antonik ◽  
Anna Wolska ◽  
Paweł Rejmak ◽  
Kinga Ostrowska ◽  
...  

1980 ◽  
Vol 191 (1) ◽  
pp. 183-191 ◽  
Author(s):  
D Beale ◽  
J K Fazakerley

Treatment of porcine immunoglobulin M (IgM) with pepsin at pH 4.6 and 37 degrees C was found to gradually remove Fab arms and Cmicro2 domains over a period of 18h. Structural studies failed to find any other change. The main products can therefore be regarded as IgM-like molecules with limited numbers of Fab arms and Cmicro2 domains. Results indicated that this removal of Fab arms is probably a random process. As the average number of Fab arms per molecule was decreased the ability to agglutinate Salmonella oranienburg (mt-H) gradually diminished. Complement fixation by the complexes however, decreased rapidly, and became negligible when the average number of Fab arms was four. This was confirmed by using a preparation containing mainly molecules with three or four Fab arms. The overall results showed that molecules with three or four Fab arms can agglutinate Salmonella but that these complexes do not fix complement. Molecules with five arms probably behave like those with four. Complexes formed by molecules with six arms fix complement quite efficiently. Possible explanations for these results are discussed.


2009 ◽  
Vol 37 (2) ◽  
pp. 400-407 ◽  
Author(s):  
Michael R. Jones

Photoreaction centres are Nature's solar batteries. These nanometre-scale power producers are responsible for transducing the energy of sunlight into a form that can be used by biological systems, thereby powering most of the biological activity on the planet. Although to the layman the word ‘photosynthesis’ is usually associated with green plants, much of our understanding of the molecular basis of biological transduction of light energy has come from studies of purple photosynthetic bacteria. Their RCs (reaction centres) and attendant light-harvesting complexes have been subjected to an intensive spectroscopic scrutiny, coupled with genetic manipulation and structural studies, that has revealed many of the molecular and mechanistic details of biological energy transfer, electron transfer and coupled proton translocation. This review provides a short overview of the structure and mechanism of the purple bacterial RC, focusing in the main on the most heavily studied complex from Rhodobacter sphaeroides.


2020 ◽  
Vol 44 (17) ◽  
pp. 6889-6901
Author(s):  
Dinkar Choudhari ◽  
Sunita Salunke-Gawali ◽  
Debamitra Chakravarty ◽  
Samir R. Shaikh ◽  
Dipali N. Lande ◽  
...  

Design and development of drugs in multi-drug resistant (MDR) infections have been of growing interest. The syntheses, structural studies, antibacterial and antifungal activities of imidazole-based 1,4-naphthoquinones are studied in this investigation.


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