## Abstract The effect of water on the low‐frequency (10^2^‐10^5^ H~z~) complex permittivitv of native, sold‐state collagen has been investigated experimentally. Measurements at ambient temperature show that dry collagen exhibits essentially no frequency or temperature dependence. As water is absor
Dielectric properties of hydrated collagen
✍ Scribed by J. Raul Grigera; Fernando Vericat; Klaas Hallenga; Herman J. C. Berendsen
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 587 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Dielectric measurements have been carried out on partially hydrated collagen in the frequency ranges 100 kHz–5 MHz, 100 MHz–1 GHz, and 8–23 GHz. In the low‐frequency range, a dispersion was observed around 100 kHz which results from inhomogeneous conductivity of the samples. A dielectric relaxation was observed aroud 0.3 GHz using time‐domain‐spectroscopy techniques. This relaxation can be considered to originate from mobile side chains. Microwave measurements indicate that the water relaxation may extend into the 10‐GHz region. An apparent discrepancy between the main water relaxation time and the average rotational correlation time of water as measured by nmr line widths was resolved by the assumption that a fraction of the water molecules is bound to the collagen with residence times on the order of 10^−6^ sec, whereas the remainder of the water is only weakly bound and exhibits rotational rates on the order of 10^−10^ sec.
📜 SIMILAR VOLUMES
The frequency dependences of the dielectric constant, E ' , and the loss factor, E", in collagen were measured a t several water contents from 0.1 to 0.3 g/g collagen over a frequency range of 30 Hz to 100 kHz and at a temperature of 20°C. Remarkable dispersion was observed at the lower frequencies
## Abstract The dc conductivity of hydrated bovine Achilles' tendon collagen has been determined as a function of hydration over a limited temperature range. At ambient temperature the conductivity changes from 10^−15^ (Ω cm)^−1^ in the dry state to about 10^−8^ (Ω cm)^−1^ at ∼24% water content by
## Abstract Two dielectric relaxation peaks were found in moist collagen by the time domain reflectometry. The low‐frequency peak around 100 MHz moves little as the water content is varied. Its relaxation strength depends on the content and vanishes for completely dried collagen. This process is co
Nuclear magnetic resonance and dielectric data on hydrated collagen are interpreted in terms of Ramachandran's hydration model. It is found that all data are compatible with this model, indicating two specific binding sites per three amino acids in the threefold collagen helix. Sorption data have be