scholarly journals Conformational stabilization of a β-hairpin through a triazole–tryptophan interaction

2018 ◽  
Vol 16 (5) ◽  
pp. 787-795 ◽  
Author(s):  
Donatella Diana ◽  
Claudia Di Salvo ◽  
Veronica Celentano ◽  
Lucia De Rosa ◽  
Alessandra Romanelli ◽  
...  
Keyword(s):  
Hairpin Conformation ◽  
Conformational Stabilization ◽  
Aromatic Interaction

Triazole and indole rings stabilize a β-hairpin conformation through an aromatic–aromatic interaction.

An usnic acid derivative as new tweezer for non-covalent aromatic interaction complex

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
B Legouin ◽  
M Chollet-Krugler ◽  
S Tomasi ◽  
P Uriac ◽  
P van de Weghe
Keyword(s):  
Acid Derivative ◽  
Usnic Acid ◽  
Aromatic Interaction

Mechanism and Stereoselectivity of the Phosphinylation of 3-Acyl Coumarins-Stereocontrol Via Concurrent Aromatic Interaction/Oxaphosphole Formation

2009 ◽  
Vol 6 (2) ◽  
pp. 180-185
Author(s):  
Petar Petrov ◽  
Nikolay Vassilev ◽  
Silvia Angelova ◽  
Boris Shivachev ◽  
Galin Petrov
Keyword(s):  
Aromatic Interaction

Fibrinogen Bern I: A Hereditary Fibrinogen Variant With Defective Conformational Stabilization By Calcium Ions

1981 ◽  
Author(s):  
C Rupp ◽  
C Kuyas ◽  
A Häberli ◽  
M Furlan ◽  
E A Beck
Keyword(s):  
Calcium Ions ◽  
Gel Electrophoresis ◽  
Calcium Binding ◽  
Negative Charge ◽  
Fibrinopeptide A ◽  
Isoelectric Focussing ◽  
High Calcium ◽  
Two Generations ◽  
Polypeptide Chains ◽  
Conformational Stabilization

Inherited hypodysfibrinogenemia (fibrinogen Bern I) was found in four members (two generations) of a family with no haemorrhagic or thrombotic history. Fibrin aggregation curves (350 nm, 37°C) with patient plasma or purified fibrinogen Bern I, after addition of thrombin, were normal at high calcium concentrations (5mM) but delayed at lower calcium concentrations (≤0.lmM). The release of fibrinopeptide A was normal. Whereas the polypeptide chains of fibrinogen Bern I were indistinguishable from normal fibrinogen by SDS-gel-electrophoresis, an abnormal γ-chain with a decreased negative charge was found by isoelectric focussing.Plasmic degradation o| normal fibrinogen, in the presence of calcium (≥ImM), results in only one terminal D fragment which is stabilized by calcium against further degradation of γ-chains. In contrast, degradation of fibrinogen Bern I, under the same conditions, yielded at least two additional smaller D fragments. In conclusion, fibrinogen Bern I is characterized by defective calcium binding in the D domain of the γ-chain.

Analysis of the Orbital and Electrostatic Contributions to the Lone Pair–Aromatic Interaction Using Molecular Rotors

2021 ◽  
Author(s):  
Erik C. Vik ◽  
Ping Li ◽  
Daniel O. Madukwe ◽  
Ishwor Karki ◽  
Gabriel S. Tibbetts ◽  
...  
Keyword(s):  
Lone Pair ◽  
Molecular Rotors ◽  
Aromatic Interaction

scholarly journals Designability of Aromatic Interaction Networks at E. coli Bacterioferritin B-Type Channels

Molecules ◽  
2017 ◽  
Vol 22 (12) ◽  
pp. 2184 ◽  
Author(s):  
Yu Zhang ◽  
Jinhua Zhou ◽  
Maziar Ardejani ◽  
Xun Li ◽  
Fei Wang ◽  
...  
Keyword(s):  
Interaction Networks ◽  
E Coli ◽  
Aromatic Interaction

scholarly journals Design of a heme-binding peptide motif adopting a β-hairpin conformation

2018 ◽  
Vol 293 (24) ◽  
pp. 9412-9422 ◽  
Author(s):  
Deepesh Nagarajan ◽  
Sujeesh Sukumaran ◽  
Geeta Deka ◽  
Kiran Krishnamurthy ◽  
Hanudatta S. Atreya ◽  
...  
Keyword(s):  
Peptide Motif ◽  
Heme Binding ◽  
Binding Peptide ◽  
Hairpin Conformation

Influence of Substituents on the Edge-to-Face Aromatic Interaction: Halogens

1999 ◽  
pp. 331-334 ◽  
Author(s):  
G. Chessari ◽  
C. A. Hunter ◽  
J. L. Jimenez Blanco ◽  
C. R. Low ◽  
J. G. Vinter
Keyword(s):  
Influence Of Substituents ◽  
Aromatic Interaction
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