Hydration mobility in peptide structures
β Scribed by Yu. N. Chirgadze; A. M. Ovsepyan
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1972
- Tongue
- English
- Weight
- 481 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Synopsis
The structural behavior of hydrochlorides of poly-Llysine and tetraglycine depends on water vapor pressure. At low relative humidities, structural rearrangements are slow. Water molecules catalyze these structural rearrangements; thus, in tetraglycine hydrochloride, structural transitions are observed at a very low water content of about 1 H,O molecule per 10 peptide residues. Some general aspects of the mechanism of the hydration mobility in peptide structures are discussed.
π SIMILAR VOLUMES
An analysis of the water molecules in the first solvation shell obtained from the molecular dynamics simulation of the amyloid beta(10-35)NH2 peptide and the amyloid beta(10-35)NH2E22Q "Dutch" mutant peptide is presented. The structure, energetics, and dynamics of water in the hydration shell have b