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It is apparent that effectors for related Ca2+ binding proteins could be explored with a photo+ affinity approach. , 1 9 8 0 ) . , Keller, C H . R. (1981). Troc. Natl. Acad. Sci. USA in press. Y. (1979). Sci. 201, 19. , and Fox, C F . (1979). Ann. Rev. Biophys. Bioeng. 8, 165. J. (1963). Biochim. Biophys. Acta 100, 119. F. (1977). Biochim. Biophys. Acta 471, 49. U. (1980). Biochem. J. 189, 81. , and Blostein, R. (1975). Biochim. Biophys. Acta 389, 314. F. (1974). J. Gen. Physiol. 63, 324. K. (1970).

3. Chem. 254, 6232 (1979). 4. , in press. 5. Pharmacol. 13, 690 (1977). 6. Chem. 254, 9955 (1979). S-100: A CALCIUM-TRIGGER PROTEIN Rachel Ε. Klevit, Pierre Girard, M. P. Williams Inorganic Chemistry Laboratory University of Oxford Oxford, England This paper illustrates the properties of many calcium trigger proteins such as calmodulins and troponins by r e ­ ference to our recent studies of the S-100 protein from beef brain. The protein was made following conventional procedures. It was investigated by high resolution proton nuclear magnetic resonance (NMR) spectroscopy by methods which we have descri­ bed in detail elsewhere ( 1 ) .

Klevit, Pierre Girard, M. P. Williams Inorganic Chemistry Laboratory University of Oxford Oxford, England This paper illustrates the properties of many calcium trigger proteins such as calmodulins and troponins by r e ­ ference to our recent studies of the S-100 protein from beef brain. The protein was made following conventional procedures. It was investigated by high resolution proton nuclear magnetic resonance (NMR) spectroscopy by methods which we have descri­ bed in detail elsewhere ( 1 ) .

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