Biophysical Journal 70: 971-976 (1996)
© 1996 the Biophysical Society

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Strambini, G B Articles by Gabellieri, E Search for Related Content PubMed PubMed Citation Articles by Strambini, G B Articles by Gabellieri, E

Proteins in frozen solutions: evidence of ice-induced partial unfolding.

Istituto di Biofisica, Consiglio Nazionale delle Richerche, Pisa, Italy.

ABSTRACT

From a drastic decrease in the phosphorescence lifetime of tryptophan residues buried in compact rigid cores of globular proteins, it was possible to demonstrate that freezing of aqueous solutions is invariably accompanied by a marked loosening of the native fold, an alteration that entails considerable loss of secondary and tertiary structure. The phenomenon is largely reversible on ice melting although, in some cases, a small fraction of macromolecules recovers neither the initial phosphorescence properties nor the catalytic activity. The variation in the lifetime parameter was found to be a smooth function of the residual volume of liquid water in equilibrium with ice and to depend on the morphology of ice. The addition of cryoprotectants such as glycerol and sucrose profoundly attenuates or even eliminates the perturbation. These results are interpreted in terms of adsorption of protein molecules onto the surface of ice.

This article has been cited by other articles:

				G. B. Strambini and M. Gonnelli Protein Stability in Ice Biophys. J., March 15, 2007; 92(6): 2131 - 2138. [Abstract] [Full Text] [PDF]

				P. Cioni Role of Protein Cavities on Unfolding Volume Change and on Internal Dynamics under Pressure Biophys. J., November 1, 2006; 91(9): 3390 - 3396. [Abstract] [Full Text] [PDF]

				E. Gabellieri and G. B. Strambini ANS Fluorescence Detects Widespread Perturbations of Protein Tertiary Structure in Ice Biophys. J., May 1, 2006; 90(9): 3239 - 3245. [Abstract] [Full Text] [PDF]

				J. Broos, E. Gabellieri, G. I. van Boxel, J. B. Jackson, and G. B. Strambini Tryptophan Phosphorescence Spectroscopy Reveals That a Domain in the NAD(H)-binding Component (dI) of Transhydrogenase from Rhodospirillum rubrum Has an Extremely Rigid and Conformationally Homogeneous Protein Core J. Biol. Chem., November 28, 2003; 278(48): 47578 - 47584. [Abstract] [Full Text] [PDF]

				E. Gabellieri and G. B. Strambini Perturbation of Protein Tertiary Structure in Frozen Solutions Revealed by 1-Anilino-8-Naphthalene Sulfonate Fluorescence Biophys. J., November 1, 2003; 85(5): 3214 - 3220. [Abstract] [Full Text] [PDF]