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By E. B. Astwood

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And Arquilla, Ε. R. (1967). Biochemistry 6, 2378. Carpenter, F. H . (1966). Amer. J. Med. 40, 750. , and Wake, R. G. (1962). Biochem. J. 8 2 , 401. , Ellis, R. , and Bromer, W, (1968). Science 161, 3837. Crowfoot, D . M . (1935). Nature {London) 136, 591. D e Zoeten, L. , and D e Bruin, O. A. (1961). Ree. Trav. Chim. Pays. Bas 8 0 , 907. Dodson, E . , Harding, M . , Hodgkin, D . C , and Rossmann, Μ . G. (1966). /. Mol. Biol. 16, 227. Fredericq, E . (1954). / . Polym. Sei. 12, 287. Fredericq, E.

P o t t s : D o you see a n y interesting possibiHties in the s t u d y of 3-dimensional tructure for bifunctional reagents that would stabiHze the monomer conformation or e v e n polymeric structures? If the conformation is so stabilized that rearrangements are impossible, then the full significance of conformation in receptor binding might be unequivocally assessed. T. L. B l u n d e l l : I have discussed this with Prof. H. Zahn. T h e main problem appears to result from the fact that m a n y chemical modifications of insuHn give rise to confor­ mational changes and they also inhibit the activity.

But that seems to be a little in the future at the moment. J. M . G e o r g e : Insulin, vasopressin, and oxytocin all have in their structures a ring with a c o m m o n number of atoms containing a disulfide bond. There was a period of time when it was thought that disulfide interchange might be the mode of a t t a c h m e n t of these three hormones to their receptors and for insulin it would be at the 6 and 11 residues. T h a t this is not the case at least for vasopressin has been shown with non-disulfide-containing biologically active analogs.

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