120 THE PHYSICS OF VIRUSES 



taken across the low potential barrier. On the other hand, wet 

 viruses are highly stable at low temperatures but in a small 

 temperature range may become inactivated very quickly. 



The high entropies of activation associated with the denatura- 

 tion of proteins are not necessarily found for virus inactivation 

 unless it is carried out at high temperatures. This fact will be 

 seen to be very significant in studies on the serological behavior 

 of viruses, and it turns out that serological affinity follows dena- 

 turation behavior in many cases. Thus if a virus is inactivated 

 rapidly at high temperatures, the virus protein is almost sure to 

 be denatured, with consequent damage to the antigens. If it is 

 slowly inactivated at medium temperatures over a period of 

 days, there is good reason to believe that great loss of infectivity 

 can occur with little or no loss in ability to combine serologically. 



Many more studies of thermal inactivation need to be made. 

 Thus all the complex of properties studied by Watson for T-2 

 bacteriophage and described in Chapter 3 can also be studied 

 for thermal inactivation. Actually, practically none of this 

 rewarding work has been done; this chapter is accordingly short. 

 Further mention of thermal studies in regard to the surface 

 properties of viruses are contained in the next chapter. 



References 



General references on thermal behavior are: Glasstone, S., Laidler, K. J., 

 and Eyring, H., The Theory of Rate Processes (McGraw-Hill Book Co., Inc., 

 New York, 1941), and Stearn, A. E., Advances in Enzymol. 9, 'io (1949). More 

 detailed references follow below. 



Adams, M. H., J. Gen. Physiol. 32, 579 (1949). 



Adams, M. H., and Lark, G., J. Immunol. 64, 335 (1950). 



Boyd. G. A., and Eberl, J. J., /. Phijs. & Colloid Chem. 52, 1146 (1948). 



Cherry, W. B., and Watson, D. W., J. Bacteriol. 58, 601, 611 (1949). 



Foster, R. A. C, Johnson, F. H., and Miller, V. K., J. Gen. Physiol. 33, 1 

 (1949). 



Friedman, M., In course of publication (1953). 



Johnson, F. H., Baylor, M. B., and Frazer, D., Arch. Biochem. 19, 240 

 (1948). 



Krueger, A. P., J. Gen. Physiol. 14, 493 (1931). 



Lauffer, M. A., Carnelly, H. L., and MacDonald, E., Arch. Biochem. 16, 

 321 (1948). 



Lauffer, M. A., and Price, W. C, J. Biol. Chem. 133, 1 (1941). 



Levy, M., and Benaglia, A. E., J. Biol. Chem. 186, 829 (1950). 



