By John. Gergely (auth.), Shoichi Imai, Iwao Ohtsuki, Makoto Endo (eds.)

The papers during this quantity have been contributed by means of shut acquaintances, co-workers and students of Professor Setsuro Ebashi. they're devoted to him to commemorate his nice and pioneering contribution to the development of muscle body structure and biochemistry, which, in time, exerted a superb impression more often than not box of existence technology. We think that this factor finds the current nation of study on muscle and/or calcium that was once spread out via Professor Ebashi.

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Results were analyzed mostly in terms of heat capacity changes, which is most closely related to the structural changes of the molecule on metal binding. Two high-affinity sites of rabbit skeletal troponin C are distinguishable in terms of their affinity to calcium and associated enthalpy changes. Heat capacity changes on calcium binding to one of the two high-affinity sites is negative and is in the range ascribed to the ligand binding. In contrast, that to the other of the high-affinity sites is large and positive, indicating that a substantial area of hydrophobic groups become exposed to the solvent.

AI-Hillawi E, Bhandari DG, Trayer HR, Trayer IP: The effect of phosphorylation of cardiac troponin I on its interaction with actin and cardiac troponin C. Eur J Biochem 228: 962-970, 1995 166. Dong M, Xing J, She M, Chandra M, Solaro RJ, Cheung HC: Phosphorylation increased distance in cardiac troponin I. Biophys J 70: A38, 1996 167. Chandra M, Pan B-S, Solaro JS: Effect of PKA dependent phosphorylation of cardiac troponin I with Nand C-terminal domains of cardiac troponin C. Biophys J 70: A53, 1996 168.

Structural consequences and functional implication. Eur J Biochem 248: 329-337, 1997 158a. Gasmi-Seabrook G, Howarth JW, Finley N, Abbott MB, Britto RM, Rosevear PR: Structure ofthe C-terminal domain ofcardiac troponin C complexed with the N-terminal of cardiac troponin I. Biophys J 74: A299, 1998 159. Kleerekoper 0, Howarth J, Guo X, Solaro Rj, Rosevear PR: Cardiac troponin I induced conformational changes in cardiac troponin C as monitored by NMR using site-directed spin and isotope labelling.

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