Effects of metal ions on the structure and spectra of the peptide group
โ Scribed by D. Balasubramanian; B. C. Misra
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 468 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
โฆ Synopsis
Abstract
The interaction between salts of Groups IA and IIA and model aliphatic amides has been studied. The interaction has been monitored by calorimetry and spectroscopy. Among the alkali cations, lithium ion interacts strongest, while in Group II calcium appears to interact somewhat stronger than magnesium. The metal cation binds to the amide oxygen atom and causes alteration in the amide group geometry. As a consequence, significant alterations are seen in the infrared, nuclear magnetic resonance, ultraviolet, and circular dichroism spectra of the ligand peptide. These findings are suggested to be of importance to the conformational studies of polypeptides and proteins.
๐ SIMILAR VOLUMES
The effects of alcohols on local protein structure have been simulated using computational approaches and model peptides. Molecular simulations were carried out on a 7-residue peptide created in both an extended conformation and an โฃ-helix to explore alcohol-induced changes in peptide structure. It
The acrylic fibers containing 10.8 wt % of acrylic acid as a comonomer were treated with 5% aqueous solution of sulphates of alkali metals (sodium and potassium) and transition metals (cobalt and nickel) at 90ะC for 5 min. The effect of this treatment on the chemical structure, thermal behavior and