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Peptoid residues and beta-turn formation.
- Source :
-
Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2002 Jun; Vol. 8 (6), pp. 241-52. - Publication Year :
- 2002
-
Abstract
- A set of terminally protected tripeptoids containing a residue of either N-methylglycine or N-isobutylglycine in position i + 1/i + 2 were synthesized and tested for intramolecularly H-bonded beta-turn formation. By exploiting FT-IR absorption and 1H NMR techniques, their folding tendencies were compared with those of a variety of reference peptides. The amount of beta-turn induction and the relative extent of the various types of intramolecularly H-bonded beta-turn conformers were determined in chloroform solution.
- Subjects :
- Amino Acid Sequence
Chloroform chemistry
Glycine chemistry
Hydrogen Bonding
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular methods
Peptoids chemical synthesis
Peptoids chemistry
Protein Isoforms
Protein Structure, Secondary
Sarcosine chemistry
Spectroscopy, Fourier Transform Infrared
Glycine analogs & derivatives
Peptoids analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 1075-2617
- Volume :
- 8
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of peptide science : an official publication of the European Peptide Society
- Publication Type :
- Academic Journal
- Accession number :
- 12093001
- Full Text :
- https://doi.org/10.1002/psc.392