Turn induction by N‐aminoproline Comparison of the Gly‐Pro‐Gly and Glyψ[CO‐NH‐N]Pro‐Gly sequences
- 1 October 1994
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 44 (4) , 378-387
- https://doi.org/10.1111/j.1399-3011.1994.tb01023.x
Abstract
The folded structure induced by the N-aminoproline residue (the hydrazino analogue of proline, denoted hPro) in the Boc-Gly1-hPro2-Gly3-NHiPr hydrazino tripeptide has been characterized in the solid state by X-ray diffraction, and compared to the usual beta II-turn structure in the Boc-Gly1-Pro2-Gly36-NHiPr cognate tripeptide. It is stabilized by a bifurcated hydrogen bond in which (Gly3)NH interacts with both (Gly1)CO and (hPro2)N alpha. This conformation is retained in CH2Cl2 and CHCl3 solutions, and allows an overall folded conformation of the hydrazino tripeptide in which (iPr)NH is hydrogen-bonded to (Boc)CO. The hPro alpha-hydrazino acid residue appears to promote a local folded structure, and might behave as a beta-turn mimic.Keywords
This publication has 39 references indexed in Scilit:
- Peptide mimics for structural features in proteinsInternational Journal of Peptide and Protein Research, 1993
- Electrophilic amination: preparation and use of N-Boc-3-(4-cyanophenyl)oxaziridine, a new reagent that transfers a N-Boc group to N- and C-nucleophilesThe Journal of Organic Chemistry, 1993
- Designing peptide and protein ligands for biological receptorsCurrent Opinion in Biotechnology, 1991
- N-amination using N-methoxycarbonyl-3-phenyloxaziridine. Direct access to chiral Nβ-protected α-hydrazinoacids and carbazatesJournal of the Chemical Society, Chemical Communications, 1991
- Infrared spectral study of hydration of N,N-dimethylbenzamide in dioxane-water mixtures: molecular level structure of hydrated amides and hydration constantsThe Journal of Physical Chemistry, 1990
- Crystal Structure of a β-Turn Model Dipeptide, (3S, 6S, 9R)-2-Oxo-3-t-butyloxycarboxylamino-7-thia-1-aza-bicyclo[4.3.0]nonane-9-carboxylic AcidAnalytical Sciences, 1989
- .beta.-Turns in model dipeptides. An infrared quantitative analysis with NMR correlationJournal of the American Chemical Society, 1985
- Comparison of X-ray and neutron diffraction results for the N-H ...O=C hydrogen bondActa crystallographica Section B, Structural science, crystal engineering and materials, 1983
- Conformational restrictions of biologically active peptides via amino acid side chain groupsLife Sciences, 1982
- Experimental investigations on the backbone folding of proline‐containing model tripeptidesBiopolymers, 1979