Probing Eudesmane Cation−π Interactions in Catalysis by Aristolochene Synthase with Non-canonical Amino Acids

2011 ◽  
Vol 133 (35) ◽  
pp. 13906-13909 ◽  
Author(s):  
Juan A. Faraldos ◽  
Alicja K. Antonczak ◽  
Verónica González ◽  
Rebecca Fullerton ◽  
Eric M. Tippmann ◽  
...  
Keyword(s):  
Amino Acids ◽  
Π Interactions ◽  
Aristolochene Synthase

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.

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

Tetraphenylethene-based tetracationic cyclophanes and their selective recognition for amino acids and adenosine derivatives in water

2019 ◽  
Vol 55 (16) ◽  
pp. 2372-2375 ◽  
Author(s):  
Lin Cheng ◽  
Haiyang Zhang ◽  
Yunhong Dong ◽  
Yanxia Zhao ◽  
Yang Yu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Selective Recognition ◽  
Π Interactions ◽  
Adenosine Derivatives

Tetracationic cyclophane 1 with a trapezoid-like cavity exhibited highly-selective recognition for tryptophan and ATP through electrostatic and π–π interactions in water.

Anion–π interactions in complexes of proteins and halogen-containing amino acids

2016 ◽  
Vol 21 (3) ◽  
pp. 357-368 ◽  
Author(s):  
Sunčica Z. Borozan ◽  
Mario V. Zlatović ◽  
Srđan Đ. Stojanović
Keyword(s):  
Amino Acids ◽  
Π Interactions

scholarly journals Aromatic Amino Acids-Guanidinium Complexes through Cation-π Interactions

Molecules ◽  
2015 ◽  
Vol 20 (5) ◽  
pp. 9214-9228 ◽  
Author(s):  
Cristina Trujillo ◽  
Ana Rodriguez-Sanz ◽  
Isabel Rozas
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids ◽  
Π Interactions
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