## Abstract The 218‐nm peak, characteristic of the circular dichroism of randomly coiled poly‐α‐amino acids can be demonstrated in solutions of penta‐L‐lysine, α‐glycyl‐L‐lysine, as well as poly‐L‐lysine. The thermal stability of the particular state that gives rise to this 218‐nm band in the CD is
Conformation of malformin A: A proton magnetic resonance and a circular dichroism study
✍ Scribed by Marius Ptak
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 785 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Malformin A is a cyclic pentapeptide with an intramolecular disulfide bridge. The conformation in solution of this molecule has been studied by NMR and CD. The 270 MHz Proton spectrum in dimethyl sulfoxide is well resolved and the peaks corresponding to the five residues have been assigned.
From the temperature dependence of chemical shifts of the peptide protons and from the exchange rate of these protons, it is concluded that the NH proton of one Cys is shielded from the solvent. This observation and HN~α~CH angles, estimated from the corresponding coupling constants, a proposed conformation of the peptide backbone. From the H~β~C~α~CH coupling constants, a P chirality for the disulfide bridge is proposed. Such a conformation is confirmed by the circular dichroism spectrum which shows a negative band at λ > 250 nm.
It is concluded that the conformation of malformin A is rigid and that the disulfide bridge is exposed to interact with biological receptors.
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## Abstract The conformation of the cyclic pentapeptide malformin A has been deduced by systematically generating possible models for the molecule, and minimizing the conformation energy of each. Only one of the low‐energy solutions is fully consistent with the reported CD and NMR spectra, and this
## Abstract The conformational properties of a series of gastrin‐related peptides in aqueous solution and in 2,2,2‐trifluoroethanol (TFE) have been investigated by CD measurements. In aqueous solution the peptides Leu^32^‐HG‐34 (human big gastrin), Nle^15^‐HG‐17 (human little gastrin), and Nle^11^‐
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## Abstract CD spectra of calf thymus, __C. perfringens, E. coli__, and __M. luteus__ DNA have been measured in the vacuum‐uv region to about 168 nm for the A‐, B‐, and C‐forms. The positive band at about 187 nm and the negative band at about 170 nm found for each type and form of DNA are sensitive
Working within the restrictions of a model, we have calculated the circular dichroism of the dinucleoside phosphates ApA, CpC, ApC, and CpA for various conformations. Comparing the calculated curves with those measured in aqueous solution we find agreement for ( 1 ) ApA as a right-handed helix with