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Amer. chem. Soc. 84, 4160-4162 (1962). 71. , u. E. L. Smith: Nature 192, 1121-1123 (1961). , u. H. T u p p y : Nature 192, 1123-1125 (1961). , E. L. Smith, G. Kreil u. H. Tuppy: Nature 192, 1125-1127 (1961). The amino acid sequence of horse heart eytochrome e. a) Peptides released by digestion with chymotrypsin. 17) Pet~tides, terminal and internal, released b y digestion with trypsin. c) Complete amino acid sequence. 72. , A . L. Grossberg, and D. Pressman: The disulfide bonds of rabbit 5,-globulin and its fragments.

References . . . . . . . . . . . . . 41 43 44 48 51 60 61 62 63 Introduction (38) Proteins are large complex molecules consisting of polymers of amino acids. I n order to u n d e r s t a n d the w a y in which t h e y function it is essential to have a knowledge of the g e o m e t r y of their structure, t h a t is of their three-dinlensional conformation, as well as of their chemical composition. The a c t i v i t y of a protein m a y be lost b y tile process of denaturation (which m a y be reversible) in which no chemical bonds are broken but the three-dimensional conformation is altered; conversely the molecule m a y become active when sections, which are quite distinct chemically, are b r o u g h t close to each other.

Merigan, T. , W. J. Dreyer, and A. Berger: Technique for the specific cleavage of arginyl-bonds by trypsin. Biochim. Biophys. Acta 62, 122-13I (1952). 75. ~]5orris, C. [, O. R. : Thin-layer chromatography of proteins on Scphadex G-100 and G-200. J. Chromatogr. 16, 167-175 (1964). 76. , K. Titani, Y. Yaoi, and II. 3'Iuvahami: The complete amino acid sequence in baker's yeast cytochrom c. Bioctlim. Biophys. -690 (1963). 77. Niu, C. , and H. Fraenkel-Conrat: C-termina! amino acid sequence of tobacco mosaic virus protein.

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