Humidity-dependent structural changes in native collagen studied by X-ray diffractometry.
1. X-ray diffractometry was used in this work to study structural modifications of powdered native collagen submitted to repeated cycles of gradual drying and hydration. 2. Hysteresis effects known to exist in water sorption isotherms of this fibrous protein were detected in the plots of relative humidity vs integrated intensity of the wide angle X-ray reflections which constitute the main features of the diffraction pattern. 3. A gradual loss of structured material was observed after each drying and rehydration process. An increase in the amorphous regions of the fibrils could also be inferred from the diffraction data. 4. Drying the samples up to a critical degree of hydration (0.12 g H2O per g protein) did not produce a hysteresis loop in the plots of the parameters studied. 5. One-step drying-rehydration cycles did not seem to affect the order of the samples since they repeatedly recovered their original structure. The difference between these results and those of the gradual hydration processes may be attributed to the kinetic properties of biopolymer hydration. The rate of water removal seems to be an important factor in the structural modifications produced by the hydration (dehydration) process.
Labaki
L C
LC
Faculdade de Engenharia Civil, Universidade Estadual de Campinas, SP, Brasil.
Torriani
I L
IL
Grigera
J R
JR
D003094:Collagen / Q000737:chemistry*; D006813:Humidity; D011487:Protein Conformation; D014961:X-Ray Diffraction
D003094:Collagen