ChemInform Abstract: Synthesis of a New Unnatural Amino Acid with a Benzodiazepine- Containing Side Chain and Incorporation into a Tripeptide.

ChemInform ◽  
2010 ◽  
Vol 26 (6) ◽  
pp. no-no
Author(s):  
J. MULZER ◽  
F. SCHROEDER ◽  
A. LOBBIA ◽  
J. BUSCHMANN ◽  
P. LUGER
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Side Chain

scholarly journals Metallic Ion Sensing with a Benzothiazole-Based Fluorimetric Chemosensor

Proceedings ◽  
2018 ◽  
Vol 9 (1) ◽  
pp. 11
Author(s):  
Cátia D. F. Martins ◽  
M. Manuela M. Raposo ◽  
Susana P. G. Costa
Keyword(s):  
Amino Acid ◽  
Transition Metal ◽  
Acid Derivative ◽  
Metal Cations ◽  
Benzyl Ester ◽  
Unnatural Amino Acid ◽  
Amino Acid Derivative ◽  
Side Chain ◽  
Transition Metal Cations ◽  
Ion Sensing

An unnatural amino acid derivative, N-tert-butyloxycarbonyl asparagine benzyl ester bearing a benzothiazole unit at the side chain, was evaluated as a fluorimetric chemosensor for several transition metal cations with environmental, biological and analytic relevance. Spectrofluorimetric titrations of the heterocyclic asparagine derivative with the various ions were carried out in acetonitrile and acetonitrile/water (9:1). It was found that the unnatural amino acid had a remarkable fluorimetric response in the presence of Cu2+ in acetonitrile and in the presence of Fe3+ in acetonitrile/water (9:1).

Epimerization During Coupling to the Unnatural Amino Acid in Solid Phase Peptide Synthesis

2001 ◽  
Vol 66 (6) ◽  
pp. 923-932 ◽  
Author(s):  
Zhenyu Zhang ◽  
Arthur Van Aerschot ◽  
Patrick Chaltin ◽  
Roger Busson ◽  
Piet Herdewijn
Keyword(s):  
Amino Acid ◽  
Nucleic Acids ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Unnatural Amino Acid ◽  
Side Chain

Extensive epimerization was observed during the coupling of Fmoc-L-Trp(Boc) and Fmoc-L-Pro to D-Ual, a synthetic α-amino acid with a nucleobase in the side chain. This unnatural amino acid was used extensively in the construction of nucleic acids recognition libraries. Reaction protocols based on the use of DIC-HOAt-DIEA mixture without preactivation of the coupling mixture has been proven to suppress the epimerization reaction significantly.

scholarly journals Site-specific 19 F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid

2010 ◽  
Vol 20 (1) ◽  
pp. 224-228 ◽  
Author(s):  
Pan Shi ◽  
Hu Wang ◽  
Zhaoyong Xi ◽  
Chaowei Shi ◽  
Ying Xiong ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chemical Shift ◽  
Membrane Protein ◽  
Unnatural Amino Acid ◽  
Side Chain ◽  
Nmr Chemical Shift ◽  
Site Specific ◽  
Relaxation Analysis ◽  
19 F Nmr

Synthesis of a New Unnatural Amino Acid with a Benzodiazepine-Containing Side Chain and Incorporation into a Tripeptide

1994 ◽  
Vol 33 (17) ◽  
pp. 1737-1739 ◽  
Author(s):  
Johann Mulzer ◽  
Fridtjof Schröder ◽  
Alessandro Lobbia ◽  
Jürgen Buschmann ◽  
Peter Luger
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Side Chain

An Unnatural Amino Acid that Mimics a Tripeptide β-Strand and Forms β-Sheetlike Hydrogen-Bonded Dimers [J. Am. Chem. Soc.2000,122, 7654-7661]. 

2001 ◽  
Vol 123 (7) ◽  
pp. 1545-1546
Author(s):  
James S. Nowick ◽  
De Michael Chung ◽  
Kalyani Maitra ◽  
Santanu Maitra ◽  
Kimberly D. Stigers ◽  
...  
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Hydrogen Bonded

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

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