scholarly journals A reevaluation of computed proton affinities for the common α-amino acids

2009 ◽  
Vol 20 (11) ◽  
pp. 2116-2123 ◽  
Author(s):  
Scott Gronert ◽  
David C. Simpson ◽  
Keyanna M. Conner
Keyword(s):  
Amino Acids ◽  
Proton Affinities ◽  
The Common

Investigation of Optimum Conformations and Structure Analysis of RL and LR Nests using Ramachandran Plot

2015 ◽  
pp. 209-224
Author(s):  
Sumukh Deshpande ◽  
Saikat Kumar Basu ◽  
Pooja Purohit
Keyword(s):  
Amino Acids ◽  
Ring Structure ◽  
Ramachandran Plot ◽  
Binding Motifs ◽  
Automated Algorithm ◽  
Automation And Control ◽  
The Common ◽  
And Control ◽  
Common Anion ◽  
Unique Application

We have surveyed polypeptides with the optimal conformations of nests which are the common anion-binding motifs comprising 8% of the amino acids which are characterized by a structural depression or a hole. Using automated bioinformatics algorithm, novel ring structure of the nest has been found. Using automated algorithm, models of polypeptides were made in-silico (computationally) and oxygen atoms are inserted along the extension of the NH groups. These sophisticated algorithms allow insertion of atoms along the NH group at the correct distance which causes extension of the group thus forming hydrogen bond. Optimal conformations of these structures are found from these customized models. This study chapter provides a demonstration of an important discovery of optimum conformations of RL and LR nests by the use of sophisticated bioinformatics automation pipeline and a unique application of automation and control in bioinformatics.

scholarly journals A Practical Approach to the Investigation of Amino Acid Disorders

1988 ◽  
Vol 25 (2) ◽  
pp. 129-141 ◽  
Author(s):  
M A Edwards ◽  
S Grant ◽  
A Green
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Practical Approach ◽  
The Common ◽  
Common Problems

We have, in this paper, highlighted some of the common problems in amino acid analysis in our experience and listed the possible causes for increases in specific amino acids in urine—together with guidance on appropriate follow-up investigations.

scholarly journals Mycosporine-Like Amino Acids and Marine Toxins - The Common and the Different

Marine Drugs ◽  
2008 ◽  
Vol 6 (2) ◽  
pp. 147-163 ◽  
Author(s):  
Manfred Klisch ◽  
Donat Häder
Keyword(s):  
Amino Acids ◽  
Marine Toxins ◽  
The Common

Structure-function relationships of peptide fragments of gastrin and cholecystokinin.

1977 ◽  
Vol 233 (4) ◽  
pp. E286
Author(s):  
D L Kaminski ◽  
M J Ruwart ◽  
M Jellinek
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Bile Flow ◽  
Hydrogen Ion ◽  
Biliary System ◽  
Peptide Fragments ◽  
Hepatic Bile ◽  
Amino Acid Peptide ◽  
The Common ◽  
Active Fragments

This study evaluates the structure-function relationships of the C-terminal peptide fragments of gastrin and cholecystokinin (CCK) in the biliary system and the stomach. Dogs with chronic biliary and gastric fistulas were used. Administration of the common fragments of CCK and gastrin with four and five amino acids and the active fragments of CCK with six through eight amino acids without sulfation of tyrosine in position 7 failed to alter hepatic bile flow from control values while significantly stimulating gastric hydrogen ion output. Administration of the seven and eight amino acid peptide fragments of CCK with sulfation of tyrosine in position 7 significantly increased hepatic bile flow. Administration of the sulfated octapeptide with 4 microgram/kg per h of nonsulfated octapeptide did not result in the inhibition of the choleresis produced by the sulfated peptide. The gastric hydrogen ion response produced by the administration of the nonsulfated and sulfated peptide was equal to that of the nonsulfated peptide alone. These results suggest that in the biliary system the receptor is highly specific as sulfation of the peptide fragment of CCK is essential for combining with the receptor, whereas in the stomach the receptor has little specificity and combines with all of the peptide fragments evaluated.

Renal reabsorption of amino acids

1962 ◽  
Vol 203 (5) ◽  
pp. 891-896 ◽  
Author(s):  
Marian Ruszkowski ◽  
Cizesław Arasimowicz ◽  
Jan Knapowski ◽  
Jan Steffen ◽  
Krystyna Weiss
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Transport Mechanism ◽  
Flow Analysis ◽  
Proximal Segment ◽  
Renal Tubules ◽  
Basic Amino Acids ◽  
Tubular Transport ◽  
The Common ◽  
Stop Flow

Using the method of stop flow analysis an attempt was made to localize the process of amino acid reabsorption in the nephron of the dog. Special attention was given to the group of basic amino acids and cystine believed to share a common tubular transport mechanism. The evidence obtained in this study points clearly to the proximal segment as the site of intensive reabsorption of all amino acids investigated. During the infusion of arginine, lysine or ornithine, an increased excretion of two remaining basic amino acids plus cystine was observed, as a rule. Successful attempts were made to infuse cystine intravenously. The results of these experiments did provide the missing link for the hypothesis derived by Dent and Rose ( Quart. J. Med. 20: 205, 1951) concerning the common transport mechanism of arginine, ornithine, lysine, and cystine in the renal tubules. The functional cystinuria, which can be induced by saturating the common reabsorptive pathway with each of the above-mentioned amino acids, is fully reversible.

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