MOLECULAR MODELLING AND SPECTROSCOPIC STUDIES OF THE INTERACTIONS BETWEEN CHELATING AND ELECTRON-DONOR METAL EXTRACTANTS: THE SYSTEM TRI-N-OCTYLPHOSPHINE OXIDE - 3-PHENYL-4-BENZOYL-ISOXAZOL-5-ONE ( ‘HPBI‘ ) IN WET TOLUENE AND CHLOROFORM.

1996 ◽  
Vol 14 (4) ◽  
pp. 653-687 ◽  
Author(s):  
G.J. Goetz-Grandmont ◽  
M. Chaoui Roqai ◽  
J.P. Brunette ◽  
G. Kaufmann
Keyword(s):  
Electron Donor ◽  
Molecular Modelling ◽  
Spectroscopic Studies

Spectroscopic studies and molecular modelling of the aflatoxin M1-bovine α-lactalbumin complex formation

2020 ◽  
Vol 209 ◽  
pp. 111957
Author(s):  
Carlos Jiménez-Pérez ◽  
Salvador R. Tello-Solís ◽  
Carlos Z. Gómez-Castro ◽  
Sergio Alatorre-Santamaría ◽  
Lorena Gómez-Ruiz ◽  
...  
Keyword(s):  
Complex Formation ◽  
Molecular Modelling ◽  
Spectroscopic Studies ◽  
Aflatoxin M1

scholarly journals Molecular modelling indicates that the pathological conformations of prion proteins might be β-helical

1999 ◽  
Vol 343 (2) ◽  
pp. 453-460 ◽  
Author(s):  
Donald T. DOWNING ◽  
N. D. LAZO
Keyword(s):  
Molecular Modelling ◽  
Amyloid Fibrils ◽  
Prion Proteins ◽  
Prion Diseases ◽  
Spectroscopic Studies ◽  
Cellular Protein ◽  
Precursor Protein ◽  
Random Coil ◽  
Helical Conformation ◽  
Spongiform Encephalopathy

Creutzfeldt-Jakob disease, kuru, scrapie and bovine spongiform encephalopathy are diseases of the mammalian central nervous system that involve the conversion of a cellular protein into an insoluble extracellular isoform. Spectroscopic studies have shown that the precursor protein contains mainly α-helical and random-coil conformations, whereas the prion isoform is largely in the β conformation. The pathogenic prion is resistant to denaturation and protease digestion and can promote the conversion of the precursor protein to the pathogenic form. These properties have yet to be explained in terms of the structural conformations of the proteins. In the present study, molecular modelling showed that prion proteins could adopt the β-helical conformation, which has been established for a number of fibrous proteins and has been suggested previously as the basis of amyloid fibrils. The β-helical conformation provides explanations for the biophysical and biochemical stability of prions, their ability to form templates for the transmission of pathological conformation, and the existence of phenotypical strains of the prion diseases.

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