NMR spin-echo studies of hydration properties of the molecular chaperone alpha-crystallin in the bovine lens.

The water-binding properties of bovine lens alpha-crystallin, collagen from calf skin and bovine serum albumin (BSA), were investigated with various techniques. The water absorptive capacity was obtained in high vacuum desorption experiments volumetrically, and also gravimetrically in controlled atmosphere experiments. NMR spin-echo technique was used to study the hydration of protein samples and to determine the spin-spin relaxation times (T2) from the protons of water, absorbed on the proteins.