Publisher’s Note: “Solvation thermodynamics of amino acid side chains on a short peptide backbone” [J. Chem. Phys. 142, 144502 (2015)]

2015 ◽  
Vol 142 (16) ◽  
pp. 169901 ◽  
Author(s):  
Timir Hajari ◽  
Nico F. A. van der Vegt
Keyword(s):  
Amino Acid ◽  
Chem Phys ◽  
Side Chains ◽  
Peptide Backbone ◽  
Short Peptide ◽  
Solvation Thermodynamics ◽  
Amino Acid Side Chains

Amino acid side chains affect the bioactivity of designed short peptide amphiphiles

2016 ◽  
Vol 4 (13) ◽  
pp. 2359-2368 ◽  
Author(s):  
Cuixia Chen ◽  
Jing Hu ◽  
Cheng Yang ◽  
Yu Zhang ◽  
Fang Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Peptide Amphiphiles ◽  
Side Chains ◽  
Short Peptide ◽  
Amino Acid Side Chains

Amino acid side chains of a short amphiphilic G(AABB)3A-NH2peptide affect its bioactivity.

Peptide Backbone Effect on Hydration Free Energies of Amino Acid Side Chains

2014 ◽  
Vol 118 (46) ◽  
pp. 13162-13168 ◽  
Author(s):  
Timir Hajari ◽  
Nico F. A. van der Vegt
Keyword(s):  
Amino Acid ◽  
Side Chains ◽  
Free Energies ◽  
Peptide Backbone ◽  
Amino Acid Side Chains

Predicting the Strength of Stacking Interactions Between Heterocycles and Aromatic Amino Acid Side Chains

2019 ◽  
Author(s):  
Andrea N. Bootsma ◽  
Analise C. Doney ◽  
Steven Wheeler
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acids ◽  
Biologically Active ◽  
Side Chains ◽  
Stacking Interactions ◽  
Inhibitor Binding ◽  
Protein Binding Sites ◽  
Amino Acid Side Chains

<p>Despite the ubiquity of stacking interactions between heterocycles and aromatic amino acids in biological systems, our ability to predict their strength, even qualitatively, is limited. Based on rigorous <i>ab initio</i> data, we have devised a simple predictive model of the strength of stacking interactions between heterocycles commonly found in biologically active molecules and the amino acid side chains Phe, Tyr, and Trp. This model provides rapid predictions of the stacking ability of a given heterocycle based on readily-computed heterocycle descriptors. We show that the values of these descriptors, and therefore the strength of stacking interactions with aromatic amino acid side chains, follow simple predictable trends and can be modulated by changing the number and distribution of heteroatoms within the heterocycle. This provides a simple conceptual model for understanding stacking interactions in protein binding sites and optimizing inhibitor binding in drug design.</p>

A Strategy for Thioamide Incorporation During Fmoc Solid-Phase Peptide Synthesis with Robust Stereochemical Integrity

2019 ◽  
Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller
Keyword(s):  
Amino Acid ◽  
Functional Groups ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Peptide Elongation

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>

scholarly journals Mobile unnatural amino acid side chains in the core of staphylococcal nuclease

1996 ◽  
Vol 5 (6) ◽  
pp. 1026-1031 ◽  
Author(s):  
Richard Wynn ◽  
Paul C. Harkins ◽  
Frederic M. Richards ◽  
Robert O. Fox
Keyword(s):  
Amino Acid ◽  
Staphylococcal Nuclease ◽  
Unnatural Amino Acid ◽  
Side Chains ◽  
The Core ◽  
Amino Acid Side Chains

scholarly journals Intrinsic Energy Landscapes of Amino Acid Side-Chains

2012 ◽  
Vol 52 (6) ◽  
pp. 1559-1572 ◽  
Author(s):  
Xiao Zhu ◽  
Pedro E.M. Lopes ◽  
Jihyun Shim ◽  
Alexander D. MacKerell
Keyword(s):  
Amino Acid ◽  
Side Chains ◽  
Energy Landscapes ◽  
Amino Acid Side Chains ◽  
Intrinsic Energy
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