scholarly journals Fluorinated aromatic amino acids distinguish side chain cation‐π interactions from membrane insertion (1002.5)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Mary Roberts ◽  
Tao He ◽  
Jianmin Gao
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Side Chain ◽  
Membrane Insertion ◽  
Π Interactions

scholarly journals Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion

2015 ◽  
Vol 290 (31) ◽  
pp. 19334-19342 ◽  
Author(s):  
Tao He ◽  
Anne Gershenson ◽  
Stephen J. Eyles ◽  
Yan-Jiun Lee ◽  
Wenshe R. Liu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Membrane Insertion ◽  
Π Interactions

On the interaction between the imidazolium cation and aromatic amino acids. A computational study

2015 ◽  
Vol 13 (29) ◽  
pp. 7961-7972 ◽  
Author(s):  
Ana A. Rodríguez-Sanz ◽  
Enrique M. Cabaleiro-Lago ◽  
Jesús Rodríguez-Otero
Keyword(s):  
Amino Acids ◽  
Computational Study ◽  
Aromatic Amino Acids ◽  
Imidazolium Cation ◽  
Π Interactions

Phe, Tyr and Trp form parallel complexes with cation⋯π interactions. His complexes are the strongest, but without making contact with the aromatic cloud.

BIOSYNTHESIS OF THE PHENYLPROPANOID MOIETY OF CHLORAMPHENICOL

1964 ◽  
Vol 10 (5) ◽  
pp. 705-716 ◽  
Author(s):  
L. C. Vining ◽  
D. W. S. Westlake
Keyword(s):  
Amino Acids ◽  
Shikimic Acid ◽  
Aromatic Amino Acids ◽  
Side Chain ◽  
Streptomyces Sp ◽  
Pass Through

Cultures of Streptomyces sp. 3022a were grown in the presence of C14-labelled substrates and incorporation of radioactivity into chloramphenicol measured. D-Glucose, labelled in carbons 1 or 2 or uniformly, was an efficient precursor of the p-nitrophenylserinol moiety and of the phenylpropanoid amino acids of the mycelium. The distribution of label in the ring and side-chain carbon atoms of p-nitrophenylserinol and cellular phenylalanine from experiments in which glucose-1-C14, glucose-2-C14, and glycine-2-C14 were fed provided evidence that the two phenylpropanoid systems had a common biosynthetic origin. The results were also consistent with their formation via the shikimic acid – prephenic acid route. Uniformly C14-labelled shikimic acid, though poorly utilized by this organism, was incorporated selectively into both the aromatic portion of chloramphenicol and the aromatic amino acids in the mycelium. L-Phenylalanine-U-C14, L-phenylalanine-carboxyl-C14, L-tyrosine-carboxyl-C14, DL-p-hydroxyphenylserine-2-C14, and acetate-2-C14 were poor precursors of the p-nitrophenylserinol moiety. Since phenylalanine and tyrosine were incorporated into the mycelium the biosynthetic route to the phenylpropanoid portion of chloramphenicol evidently does not pass through either of these amino acids but branches at an earlier step.

Side Chain Cyclized Aromatic Amino Acids: Great Tools as Local Constraints in Peptide and Peptidomimetic Design

2016 ◽  
Vol 59 (24) ◽  
pp. 10865-10890 ◽  
Author(s):  
Olivier Van der Poorten ◽  
Astrid Knuhtsen ◽  
Daniel Sejer Pedersen ◽  
Steven Ballet ◽  
Dirk Tourwé
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Side Chain ◽  
Local Constraints

Serine and Cysteine π-Interactions in Nature: A Comparison of the Frequency, Structure, and Stability of Contacts Involving Oxygen and Sulfur

2015 ◽  
Vol 68 (3) ◽  
pp. 385 ◽  
Author(s):  
Hanzala B. Hussain ◽  
Katie A. Wilson ◽  
Stacey D. Wetmore
Keyword(s):  
Amino Acids ◽  
High Resolution ◽  
Protein Stability ◽  
Crystal Structures ◽  
Protein Complexes ◽  
Aromatic Amino Acids ◽  
Biological Macromolecules ◽  
Great Stability ◽  
Π Interactions ◽  
And Function

Despite many DNA–protein π-interactions in high-resolution crystal structures, only four X–H···π or X···π interactions were found between serine (Ser) or cysteine (Cys) and DNA nucleobase π-systems in over 100 DNA–protein complexes (where X = O for Ser and X = S for Cys). Nevertheless, 126 non-covalent contacts occur between Ser or Cys and the aromatic amino acids in many binding arrangements within proteins. Furthermore, Ser and Cys protein–protein π-interactions occur with similar frequencies and strengths. Most importantly, due to the great stability that can be provided to biological macromolecules (up to –20 kJ mol–1 for neutral π-systems or –40 kJ mol–1 for cationic π-systems), Ser and Cys π-interactions should be considered when analyzing protein stability and function.

scholarly journals Cation-π Interactions Involving Aromatic Amino Acids

2007 ◽  
Vol 137 (6) ◽  
pp. 1504S-1508S ◽  
Author(s):  
Dennis A. Dougherty
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Π Interactions

Side chain dynamics of two aromatic amino acids in pancreatic phospholipase A2 as studied by deuterium nuclear magnetic resonance

Biochemistry ◽  
1985 ◽  
Vol 24 (13) ◽  
pp. 3268-3273 ◽  
Author(s):  
P. R. Allegrini ◽  
G. J. M. Van Scharrenburg ◽  
A. J. Slotboom ◽  
G. H. De Haas ◽  
J. Seelig
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Phospholipase A2 ◽  
Aromatic Amino Acids ◽  
Side Chain ◽  
Chain Dynamics ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Side Chain Dynamics
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