## Abstract Integral enthalpies of solution of several dipeptides and tripeptides in water at low concentrations have been determined at 25 and 35Β°C. These data have been used to derive the changes in heat capacity on dissolution at infinite dilution Ξ__C__ at 30Β°C. Limiting partial molal heat capa
The heat capacity of water in hydrated collagen
β Scribed by B. M. Fung; J. A. Cox
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 202 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Over the past 10 years calorimetric studies of collagen have been performed by several It is known that about 0.45-0.55 g H20 per collagen cannot be frozen,'^^-^ even at very low temperature.6 The freezable part of water has a melting point somewhat below 0Β°C.5,6 It was estimated that the enthalpy of the melting of collagen fiber (AH:, ca. 5OoC) is 18.0 f 0.8 cal/g or 5.4 kcal/mol per tripeptide unit.6 The AH: for acid-soluble collagen ranges from 0.8 to 1.6 kcal/mol per single peptide unit, increasing with the increasing content of imino acids and the associated heat stability.2
The heat capacity6 of collagen, dry or hydrated, has a fairly large temperature dependence below 0Β°C and very little temperature dependence above room t e m p e r a t ~r e . ~. ~ However, the interpretation of the heat capacity data of hydrated collagen above 2OoC is controversial. Haly and Snaith5 found the heat capacity of water in hydrated collagen a t 2OoC to be 1.00 cal deg-' g-' (18.0 cal deg-' mol-I), the same as that of bulk water. However, Hoeve and Kakivaya7 suggested that the C, of water in hydrated collagen at 3OoC was 1.24 cal deg-' g-' (23 cal deg-' mol-I), an amazingly high value. These authors interpret their results as indicating that "collagen acts, at least partly, as a nonpolar surface toward water chains." Since the interpretation of heat capacity data yields important implications for the understanding of the structure of hydrated collagen, we have undertaken a more detailed calorimetric study of the heat capacity of collagen hydrated with H2O and D20 in order to gain a better understanding of the nature of this system.
π SIMILAR VOLUMES
## Abstract The spinβlattice relaxation time (__T__~1~) of water adsorbed on collagen fibers was determined at six frequencies and temperatures varying from 25Β° to β80Β°C. Care was taken to eliminate the contributions to the signal of protons other than those in the adsorbed water. Quantitative calc
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 20Β°C. Remarkable dispersion was observed at the lower frequencies
Background and Objective: A common assumption made in the thermal response of biological materials due to laser irradiation is the constancy of the specific heat capacity at constant pressure, Cp. In this investigation, Cp of pure hydrated Type I collagen films is measured in time during laser irrad
Water proton transverse relaxation times (T 2 ) and self-diffusion coefficients (D) were measured in randomly oriented hydrated collagen fibers. Three T 2 relaxation times were discerned indicating the presence of at least three water fractions in the collagen sample. The D values associated with ea