Determination of endogenous amino acid flow at the terminal ileum of the rat

1988 ◽  
Vol 44 (3) ◽  
pp. 227-235 ◽  
Author(s):  
Grant A Skilton ◽  
Paul J Moughan ◽  
William C Smith
Keyword(s):  
Amino Acid ◽  
Terminal Ileum ◽  
Endogenous Amino Acid

Endogenous amino acid flows at the terminal ileum of broilers, layers and adult roosters

2004 ◽  
Vol 79 (2) ◽  
pp. 265-271 ◽  
Author(s):  
V. Ravindran ◽  
W. H. Hendriks
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Terminal Ileum ◽  
Crude Protein ◽  
Amino Acid Profile ◽  
The Other ◽  
Endogenous Protein ◽  
Abundant Amino Acid ◽  
Endogenous Amino Acid

AbstractEndogenous flows of nitrogen and amino acids at the terminal ileum of broilers (6 weeks old), layers (70 weeks old) and adult roosters (70 weeks old) were determined using the peptide alimentation method. The ileal endogenous output of nitrogen and total amino acids in broilers, layers and roosters, expressed as mg/kg dry matter intake, were similar (F > 0-05). Endogenous flows were similar (F > 0-05) for nine of the 17 amino acids analysed, but the flows of serine, glutamic acid, proline, alanine, isoleucine, tyrosine, arginine and methionine differed (P < 0-05) among the classes of chickens. The amino acid profile of endogenous protein, expressed asg/100 g crude protein, did not differ (F > 0-05) between the three classes of chickens, except for serine, glutamic acid, proline and isoleucine. The concentrations of proline were higher (F < 0-05) in broilers, compared with the other two groups. The concentrations of glutamic acid in layers were lower (F < 0-05) than the other two groups. The concentrations of serine and isoleucine were higher (F < 0-05) in roosters than the other two groups. In all three groups, the most abundant amino acid in the ileal endogenous protein was glutamic acid, followed by aspartic acid, proline, serine, glycine and threonine. The present study provides estimates for endogenous amino acid flow at the terminal ileum in broilers, layers and adult roosters under normal physiological conditions.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<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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