Role of charged amino acid side chains in the stability and lipid binding ofManduca sexta apolipophorin III

1995 ◽  
Vol 30 (2-3) ◽  
pp. 211-223 ◽  
Author(s):  
Minal Upadhyaya ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Douglas G. Scraba ◽  
Roger Bradley ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Side Chains ◽  
Apolipophorin Iii ◽  
Amino Acid Side Chains ◽  
The Stability

The role of amino acid side chains in stabilizing dipeptides: the laser ablation Fourier transform microwave spectrum of Ac-Val-NH2

2017 ◽  
Vol 19 (36) ◽  
pp. 24985-24990 ◽  
Author(s):  
I. León ◽  
E. R. Alonso ◽  
S. Mata ◽  
C. Cabezas ◽  
M. A. Rodríguez ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Amino Acid ◽  
Laser Ablation ◽  
Molecular Beam ◽  
Microwave Spectrum ◽  
Steric Effects ◽  
Side Chains ◽  
Isopropyl Group ◽  
Amino Acid Side Chains

The steric effects imposed by the isopropyl group of valine in the conformational stabilization of the capped dipeptide N-acetyl-l-valinamide (Ac-Val-NH2) have been studied by laser ablation molecular beam Fourier transform microwave (LA-MB-FTMW) spectroscopy.

scholarly journals Primary structure of peptides and ion channels. Role of amino acid side chains in voltage gating of melittin channels

1990 ◽  
Vol 58 (6) ◽  
pp. 1367-1375 ◽  
Author(s):  
M.T. Tosteson ◽  
O. Alvarez ◽  
W. Hubbell ◽  
R.M. Bieganski ◽  
C. Attenbach ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ion Channels ◽  
Primary Structure ◽  
Voltage Gating ◽  
Side Chains ◽  
Amino Acid Side Chains

The Functional Role of Positively Charged Amino Acid Side Chains in α-Bungarotoxin Revealed by Site-Directed Mutagenesis of a His-Tagged Recombinant α-Bungarotoxin†

Biochemistry ◽  
1999 ◽  
Vol 38 (24) ◽  
pp. 7847-7855 ◽  
Author(s):  
Julie A. Rosenthal ◽  
Mark M. Levandoski ◽  
Belle Chang ◽  
Jerald F. Potts ◽  
Qing-Luo Shi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Positively Charged

How non-bonding amino acid side-chains may enormously increase the stability of a Cu(II)—peptide complex

1998 ◽  
Vol 283 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Wojciech Bal ◽  
Marcin Dyba ◽  
Franciszek Kasprzykowski ◽  
Henryk Kozłowski ◽  
Rafał Latajka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Side Chains ◽  
Peptide Complex ◽  
Amino Acid Side Chains ◽  
The Stability

Role of Pyridine Hydrogen-Bonding Sites in Recognition of Basic Amino Acid Side Chains

2002 ◽  
Vol 124 (47) ◽  
pp. 14092-14103 ◽  
Author(s):  
Thomas W. Bell ◽  
Alisher B. Khasanov ◽  
Michael G. B. Drew
Keyword(s):  
Hydrogen Bonding ◽  
Amino Acid ◽  
Basic Amino Acid ◽  
Side Chains ◽  
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>

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