An analysis of amino acid composition of a few oxidoreductases by different methods

1983 ◽  
Vol 3 (3) ◽  
pp. 269-273
Author(s):  
Ali Naqui ◽  
Jean-Claude Vincent

1. All methods used to analyze amino acid composition of different enzymes agree well with each other. 2. They lead to a relationship between amino acid composition and function of proteins. 3. Cytochrome oxidase is in a class by itself; copper-containing oxidases are closely related as expected.

2021 ◽  
Author(s):  
Rik Dhar ◽  
Ryan Feehan ◽  
Joanna S.G. Slusky

AbstractUp-and-down β-barrel topology exists in both the membrane and soluble environment. However, β-barrels are virtually the only topology that exist in the outer membrane. By comparing features of these structurally similar proteins, we can determine what features are particular to the environment rather than the fold. Here we compare structures of membrane β-barrels to soluble β-barrels and evaluate their relative size, shape, amino acid composition, hydrophobicity, and periodicity. We find that membrane β-barrels are generally larger than soluble β-barrels in with more strands per barrel and more amino acids per strand, making them wider and taller. We also find that membrane β-barrels are inside-out soluble β-barrels. The inward region of membrane β-barrels have similar hydrophobicity to the outward region of soluble β-barrels, and the outward region of membrane β-barrels has similar hydrophobicity to the inward region of the soluble β-barrels. Moreover, even though both types of β-barrel have been assumed to have strands with amino acids that alternate in direction and hydrophobicity, we find that the membrane β-barrels have more regular alternation than soluble β-barrels. These features give insight into how membrane barrels maintain their fold and function in the membrane.


2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton

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