Conformation of amylose in water. I. Light-scattering and sedimentation-equilibrium measurements
✍ Scribed by M. Kodama; H. Noda; T. Kamata
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 756 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The conformation of amylose in aqueous solution has been found to be dependent on its molecular weight. When the molecular weight of amylose is outside of the so‐called “dissolving gap” described by Burchard (6500<M~r~<160,000) it behaves as a random coil, whereas when its molecular weight is within the “dissolving gap,” it easily aggregates forming a rigid coil which is the B‐type (retrograded) amylose. The conformation of this rigid coil is suggested to be a double helix.
📜 SIMILAR VOLUMES
## Abstract The molecular weights and radii of gyration of __Streptococcus salivarius__ levan fractions were obtained from light‐scattering measurements in water. Sedimentation coefficients and partial specific volumes of the fractions were also obtained. Double logarithmic plots of [η] versus __M̄
## Abstract Light scattered from a macromolecular solution in a capillary tube is used to determine both the sedimentation and translational diffusion coefficients. The capillary tube is spun in a preparative centrifuge, removed, and placed in a light‐scattering photometer equipped with a scanning
Biological self-assembly process of tropoelastin in an extracellular space, viewed as a key step of the elastogenesis, can be mimicked by the temperature-dependent coacervation of the elastin-related polypeptide-water system. Early and late stages of the phase separation behavior of the bovine neck