An unnatural tripeptide structure containing intramolecular double H-bonds mimics a turn hairpin conformation
Author:
Affiliation:
1. Key Laboratory of Radiopharmaceuticals
2. MOE; College of Chemistry
3. Beijing Normal University
4. Beijing 100875
5. China
6. Department of Chemistry
7. The State University of New York at Buffalo
8. Buffalo
9. USA
Abstract
A series of unnatural tripeptides, each consisting of two aromatic γ-amino acid residues and an ϖ-amino acid residue, are designed to probe their folding into hairpin conformations.
Funder
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2021/OB/D1OB00526J
Reference35 articles.
1. Roles of β-turns in protein folding: From peptide models to protein engineering
2. Role of Local Sequence in the Folding of Cellular Retinoic Acid Binding Protein I: Structural Propensities of Reverse Turns
3. Understanding the key factors that control the rate of -hairpin folding
4. Nanoassembly of Oligopeptides and DNA Mimics the Sequential Disassembly of a Spherical Virus
5. Efficient Gene Transfection through Inhibition of β-Sheet (Amyloid Fiber) Formation of a Short Amphiphilic Peptide by Gold Nanoparticles
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