Voltammetric sensor system based on Cu(II) and Zn(II) amino acid complexes for recognition and determination of atenolol enantiomers

Author(s):  
Yulia A. Yarkaeva ◽  
Valery N. Maistrenko ◽  
Liana R. Zagitova ◽  
Marat I. Nazyrov ◽  
Tatyana V. Berestova
1991 ◽  
Vol 30 (16) ◽  
pp. 3147-3155 ◽  
Author(s):  
Luther E. Erickson ◽  
Garth S. Jones ◽  
Jason L. Blanchard ◽  
Kazi J. Ahmed

2020 ◽  
Author(s):  
Michele Larocca

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>


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