The Structure and Function of Ribonuclease T1: XIV. Isolation and Amino Acid Composition of Chymotryptic Peptides from Performic Acid-oxidized and Heat-denatured Ribonuclease T1*

1971 ◽  
Vol 70 (4) ◽  
pp. 603-615 ◽  
Author(s):  
Kenji TAKAHASHI
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.


1998 ◽  
Vol 67 (1) ◽  
pp. 165-170 ◽  
Author(s):  
W. H. Hendriks ◽  
M. F. Tarttelin ◽  
P. J. Moughan

AbstractThe amino acid composition of cat hair was determined by conventional 24-h acid hydrolysis and non-linear least-squares extrapolation to time zero of the amino acid composition data from a series of hydrolysis intervals. Twenty-five individual samples of cat hair, consisting of four colours, were also analysed (24-h hydrolysis) to determine if there was an effect of hair colour on amino acid composition. Amino acids were determined following HCl hydrolysis (6 mol/l) with cysteine and methionine determined by performic acid oxidation of the sample prior to hydrolysis.There was no significant (P > 0·05) effect of hair colour on the amino acid composition of cat hair. The non-linear compartmental model used to determine the amino acid composition of cat hair took into account the simultaneously occurring processes of hydrolysis and degradation of amino acids over time. The amino acids cysteic acid, methionine-sulphone, threonine and serine exhibited high loss rates during 6 molll HCl hydrolysis while the peptide bonds involving valine and leucine were slowly hydrolysed. Amino acid nitrogen accounted for 0·94 of the total nitrogen in cat hair when determined by conventional 24-h hydrolysis and 0·99 of the total nitrogen when the compartmental model was applied. The average nitrogen proportion in cat hair protein was found to be 0·175. The amino acid composition of cat hair protein is comparable with that of dog, horse, sheep and human hair although the proline content of cat hair protein appears to be lower than that in the other species.


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.


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