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3-Aminothiophenecarboxylic acid (3-Atc)-induced folding in peptides.
- Source :
-
New Journal of Chemistry . Nov2016, Vol. 40 Issue 11, p9205-9210. 6p. - Publication Year :
- 2016
-
Abstract
- This paper describes the consequences of incorporating a constrained heterocyclic aromatic β-amino acid 3-aminothiophenecarboxylic acid (3-Atc) into peptides containing β-turn forming elements such as Pro-Gly motif and the effect on the secondary structural architecture of the entire peptide backbone. Conformational investigations of oligomers comprising an α,β,α peptide sequence were carried out by single-crystal X-ray diffraction, solution-state NMR, nOe-restrained MD simulation and circular dichroism studies. The results suggested that these peptide sequences assume helical architecture. The helical folding in the oligomers was found to be devoid of inter-residual H-bonding, instead found to be stabilized by a co-operative effect of 6-membered H-bonding within the 3-Atc unit and conformational restrictions of individual amino acids in the peptide backbone. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 11440546
- Volume :
- 40
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- New Journal of Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 119169979
- Full Text :
- https://doi.org/10.1039/c6nj01667g