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Intramolecularly hydrogen-bonded peptide conformations.
CRC Critical Reviews in Biochemistry
|January 1, 1980
Summary
This review highlights intramolecularly hydrogen-bonded structures in peptides, focusing on solid-state studies. It details various conformations like beta-turns and gamma-turns in model and biological peptides.
Area of Science:
- Peptide Chemistry
- Structural Biology
- Solid-State Chemistry
Background:
- Intramolecularly hydrogen-bonded structures in peptides are gaining research interest.
- Solid-state studies are crucial for understanding peptide conformation.
- Peptide structure influences biological activity.
Purpose of the Study:
- To review solid-state studies on intramolecularly hydrogen-bonded peptide structures.
- To discuss various peptide conformations, including turns and analogs.
- To explore hydrogen bonding involving side chains, protecting groups, and beta-amino acids.
Main Methods:
- X-ray diffraction
- Infrared absorption spectroscopy
- Conformational energy calculations
Main Results:
- Detailed analysis of extended C5 and folded conformations (C7, C8, C10, C11, C13).
- Inclusion of cis peptide configurations in folded structures.
- Discussion of oxy-analogs and bifurcated hydrogen bonds.
- Exploration of intramolecular hydrogen bonds involving side chains, N-protecting groups, and beta-amino acids.
Conclusions:
- Solid-state studies provide key insights into peptide structures and hydrogen bonding.
- A variety of intramolecularly hydrogen-bonded conformations exist in peptides.
- These structural features are relevant to both model systems and biologically active polypeptides.