Arginine side chain stacking with peptide plane stabilizes the protein helix conformation in a cooperative way

2018 ◽  
Vol 86 (6) ◽  
pp. 684-692 ◽  
Author(s):  
Jia Wang ◽  
Jingfei Chen ◽  
Jingwen Li ◽  
Liaoyuan An ◽  
Yefei Wang ◽  
...  
Keyword(s):  
Side Chain ◽  
Arginine Side Chain ◽  
Helix Conformation ◽  
Peptide Plane

Arginine side-chain dynamics in the HIV-1 Rev-RRE complex 1 1Edited by M. F. Summers

2000 ◽  
Vol 303 (4) ◽  
pp. 515-529 ◽  
Author(s):  
Thomas A. Wilkinson ◽  
Maria Victoria Botuyan ◽  
Bruce E. Kaplan ◽  
John J. Rossi ◽  
Yuan Chen
Keyword(s):  
Side Chain ◽  
Chain Dynamics ◽  
Arginine Side Chain ◽  
Side Chain Dynamics ◽  
Hiv 1

A general synthetic approach to novel conformationally restricted arginine side chain mimetics

Tetrahedron ◽  
2002 ◽  
Vol 58 (8) ◽  
pp. 1557-1563 ◽  
Author(s):  
Lucija Peterlin-Mašič ◽  
Andreja Jurca ◽  
Petra Marinko ◽  
Anita Jančar ◽  
Danijel Kikelj
Keyword(s):  
Side Chain ◽  
Synthetic Approach ◽  
Conformationally Restricted ◽  
Arginine Side Chain

scholarly journals Methylguanidinium at the Air/Water Interface: A Simulation Study with the Drude Polarizable Force Field

2020 ◽  
Author(s):  
Jian Zhu ◽  
Jing Huang
Keyword(s):  
Force Field ◽  
Model Compound ◽  
Side Chain ◽  
Water Interface ◽  
Polarizable Force Field ◽  
Polarization Effects ◽  
Structure And Dynamics ◽  
Arginine Side Chain ◽  
Air Water Interface ◽  
Dynamics Simulations

<div>Methylguanidinium is an important molecular ion which also serves as the model compound for arginine side chain. We studied the structure and dynamics of methylguanidium ion at the air/water interface by molecular dynamics simulations employing the Drude polarizable force field. We found out that methylguanidinium accumulate on the interface with a majority adopting tilted conformations. We also demonstrated that methylguanidinium and guanidinium ions have different preference towards the air/water interface. Our results illustrate the importance to explicitly include the electronic polarization effects in modeling interfacial properties.</div><div><br> </div>

scholarly journals Substituted polyfluoroaryl interactions with an arginine side chain in galectin-3 are governed by steric-, desolvation and electronic conjugation effects

2019 ◽  
Vol 17 (5) ◽  
pp. 1081-1089 ◽  
Author(s):  
Rohit Kumar ◽  
Kristoffer Peterson ◽  
Majda Misini Ignjatović ◽  
Hakon Leffler ◽  
Ulf Ryde ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Affinity ◽  
Binding Sites ◽  
Binding Pocket ◽  
Side Chain ◽  
Complex Interplay ◽  
Protein Binding Sites ◽  
Arginine Side Chain ◽  
Galectin 3 ◽  
Insight Into

Analysis of a ligand induced-aglycone-binding pocket in galectin-3 provides detailed insight into interactions of fluorinated phenyl moieties with arginine-containing protein binding sites and the complex interplay of different energetic components in defining the binding affinity.

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