Thermal transitions in gelatin: Optical rotation and enthalpy changes
- 1 December 1972
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 11 (12) , 2521-2532
- https://doi.org/10.1002/bip.1972.360111211
Abstract
Enthalpy changes [as determined by differential scanning calorimetry (DSC)] and optical rotation changes over the helix → coil transition were measured for various gelatin solutions and films. From these studies it has been concluded that: (1) a linear correlation between ΔH and Δ[α] exists for gelatin solutions, independent of the temperature at which gelation occurred; (2) the amount of triple helical structure regained when a melted gelatin solution is quenched can be calculated from DSC data, but the values obtained will be dependent on assumptions about the number and strength of hydrogen bonds; (3) the anomalously high levorotation values found for cold‐dried films of gelatin do not reflect the presence of an extraordinarily large amount of triple helical structure; rather, the large rotations appear to be the result of orientation of helices in the plane of the film.Keywords
This publication has 37 references indexed in Scilit:
- NMR study of the slowly exchanging hydrogens of 640 Å steerskin collagenBiopolymers, 1970
- NMR Investigation of Deuterated CollagenNature, 1970
- On the Molecular Structure of CollagenNature, 1969
- Interchain hydrogen bonds via bound water molecules in the collagen triple helixBiopolymers, 1968
- The molecular structure of collagenJournal of Molecular Biology, 1961
- Structure of CollagenNature, 1961
- The Structure of CollagenNature, 1955
- Studies on collagenProceedings of the Indian Academy of Sciences - Section A, 1955
- Structure of CollagenNature, 1955
- Structure of CollagenNature, 1954