By Hans J. Vogel
Calcium-binding proteins play a massive function in numerous important organic procedures, starting from blood clotting and sign transduction in cells, to attaching proteins to membranes and serving as an critical resource of calcium. In Calcium-Binding Protocols-Volume 1: reports and Case stories and quantity 2: tools and Techniques-Hans Vogel and a panel of top researchers evaluation the protein chemistry and behaviour of this important protein category, and supply a finished number of confirmed experimental recommendations for his or her examine either in vitro and in vivo. this primary quantity discusses the position of calcium in intracellular secondary messenger activation mechanisms, together with designated points of calcium chemistry and its usage in dairy proteins and blood clotting. exact case experiences supply a wealth of important information regarding protein purification and characterization concepts, X-ray crystallography, and particular calcium-binding proteins and their modes of motion. the second one better half quantity, tools and strategies, makes a speciality of state of the art experimental tools for learning answer constitution, balance, dynamics, calcium-binding houses, and organic job of calcium-binding proteins in general.
accomplished and hugely functional, the 2 volumes of Calcium-Binding Protocols offer experimental and scientific biologists with a bunch of complex experimental equipment that may be utilized effectively to the learn of either latest and newly stumbled on contributors of this severely very important category of proteins.
Read or Download Calcium-Binding Protein Protocols: Volume 1: Reviews and Case Studies PDF
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Extra info for Calcium-Binding Protein Protocols: Volume 1: Reviews and Case Studies
57. , Klee, C. , and Bax, A. (1995) Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2, 768–776. 58. , and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758–762. 59. Rhoads, A. R. and Friedberg, F. (1997) Sequence motifs for calmodulin recognition. FASEB J. 11, 331–340. 60. Zhang, M. and Vogel, H. J. (1997) Interaction of a partial calmodulin-binding domain of caldesmon with calmodulin. Prot.
The common form of Ba2+ and Sr2+ in geological or biological hard structures is as BaSO4 and SrSO 4, respectively (see Fig. 1). , organic carboxylates and phosphates. For example, calcium has an insoluble oxalate, often found in plant tissue, but magnesium does not. Moreover, calcium tends to precipitate many polyanions, such as DNA, RNA, and some acidic proteins. There is difficulty then in keeping calcium and accompanying anions in solution inside cells and as a protection calcium is rejected.
And Robinson, R. C. (1997) The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation. Cell 90, 661–670. Robinson, R. , Le, V. , Burtnick, L. , Yin, H. , and Choe, S. (1999) Domain movement in gelsolin: a calcium-activated switch. Science 286, 1939–1942. Vogel, H. J. (1994) Calmodulin: a versatile calcium mediator protein. Biochem. Cell Biol. 72, 357–376. Means, A. , VanBerkum, M. F. , Lu, K. , and Rasmussen, C. D. (1991) Regulatory functions of calmodulin.