Advances in enzymology : and related areas of molecular by Eric J. Toone

By Eric J. Toone

This publication covers€important advances in enzymology, explaining the habit of enzymes and the way they are often applied to increase novel medications, synthesize identified and novel compounds, and comprehend evolutionary processes.

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Ferner kann die Sedimelitation eines Eiweisskorpers oder Virusproteins gesttirt werden, wenn die Partikelchen eine elektrische Ladung tragen, was bei Eiweisskorpern meist der Fail ist, oder in dissoziierter Form vorliegen. In diesem Fall kann durch das Zentrifugieren eine Trennung der positiv und negativ geladenen Teilchen erfolgen, sodass ein dem Zentrifugenpotential entgegengerichtetes Potential entsteht. Auf diese Erscheinung wurde unter anderem von J. W. Beams (4) hingewiesen. Man verhindert praktisch diesen Umstand durch Hinzufugen von niedermolekularen Elektrolyten und Puffersubstanzen, was jedoch auch nicht vijllig einwandfrei ist, da eine selektive Bindung von Pufferionen stattfindet, die wiederum das physikalische Verhalten der Eiweisslosungen beeinflussen konnen, sodass es keineswegs gleichgiiltig ist, ob die Einstellung des jeweils gewunschten pH-Wertes mit Nn' oder NH,' bezw.

M. Wrinch. See list of reference$ in Zbid;, 6, 122 (1938). 56. D. M. Wrinch and I. Lnngmuir, J . Am. Chem. ,60, 2247 (1938). 57. D. l\rrinch, Phil. 3 (1938). ,X. I. Imigniuir, Proc. Phys. , 51, 592 (1939). 39. J,. Pniiling and C. Kiemann, J . Am. Chein. , 61,1860 (1939). 60. D. Crowfoot, I’roc. Roy. Soc. (London), A164,580 (1938); ,J. Ikrnal, Nafurc, 143,74 (1939); D. 1’. Riley tincl I. , 143,648 (1939). 61. M. I,. Anson :ind A. 15. Mirsky, J . , 35, 185 (1931). 62. bl. I,. , J . Chem. , 8, 598 (19-20).

Recently, Huggins (62, 63) has suggested two hypothetical types of structures derived by folding from basic patterns containing extended zig-zag chains. These chains are joined together by 0-H--N hydrogen bridges. The two basic patterns of the Fig. -Two hypothetical types of folding of zig-zag peptide chains. The chains extended zig-zag peptide chains are heid together hy hydrogen bridges are shown in Fig. 8. hetween the nitrogen and oxygen atoms. The first type of pattern ( A ) Structure A (left) corresponds to the foldcan be folded, without breaking ing of pattern A shown in Fig.

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