Nitrogenase of Klebsiella pneumoniae Water proton NMR relaxation studies on the binding of divalent metal ions and nucleotides to the iron protein

1977 ◽  
Vol 482 (2) ◽  
pp. 286-300 ◽  
Author(s):  
Edward O. Bishop ◽  
Melvin D. Lambert ◽  
David Orchard ◽  
Barry E. Smith
Keyword(s):  
Klebsiella Pneumoniae ◽  
Metal Ions ◽  
Proton Nmr ◽  
Nmr Relaxation ◽  
Divalent Metal ◽  
Water Proton ◽  
Divalent Metal Ions ◽  
Iron Protein ◽  
Relaxation Studies

Interaction of divalent metal ions with DNA investigated by 23Na NMR relaxation

2000 ◽  
Vol 2 (10) ◽  
pp. 2425-2428 ◽  
Author(s):  
Flaminia Cesare Marincola ◽  
Mariano Casu ◽  
Giuseppe Saba ◽  
Cesare Manetti ◽  
Adolfo Lai
Keyword(s):  
Metal Ions ◽  
Nmr Relaxation ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
23Na Nmr

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves

scholarly journals Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers

RSC Advances ◽  
2021 ◽  
Vol 11 (21) ◽  
pp. 12815-12825
Author(s):  
Yajie Wang ◽  
Feihong Meng ◽  
Tong Lu ◽  
Chunyun Wang ◽  
Fei Li
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Membrane Damage ◽  
Islet Amyloid Polypeptide ◽  
Divalent Metal ◽  
Human Islet ◽  
Divalent Metal Ions ◽  
Islet Amyloid ◽  
Induced Membrane ◽  
Human Islet Amyloid Polypeptide

Their is a counteraction between a decrease in the disruptive ability of metal-associated oligomer species and an increase in the quantity of oligomers promoted by the metal binding in the activity of hIAPP induced membrane damage.

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