Studies on bovine pancreatic ribonuclease A and model compounds in aqueous 2-methyl-2,4-pentanediol. I. Amino acid solubility, thermal reversibility of ribonuclease A, and preferential hydration of ribonuclease A crystals.
@article{Pittz1971StudiesOB, title={Studies on bovine pancreatic ribonuclease A and model compounds in aqueous 2-methyl-2,4-pentanediol. I. Amino acid solubility, thermal reversibility of ribonuclease A, and preferential hydration of ribonuclease A crystals.}, author={E. P. Pittz and J. Bello}, journal={Archives of biochemistry and biophysics}, year={1971}, volume={146 2}, pages={ 513-24 } }
Abstract For X-ray investigations, RNase-A is crystallized from a mixture of 55% 2-methyl-2,4-pentanediol (MPD) and 45% water. Interactions of RNase-A and amino acids with this solvent have been studied. From the solubilities of amino acids in water and 55% MPD it is calculated that the unfolding of RNase-A in 55% MPD would have a positive free-energy change. RNase-A in 50% MPD and in water has nearly identical CD spectra. After being heated in 50% MPD and cooled, there is nearly complete… CONTINUE READING
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