Application Notes

Microscale Thermophoresis measurements on in vitro synthesized proteins

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4 40 % MST power. For the interactions between Calmodulin and the M13 peptides 20 % MST power were used and for that of AntiEC5218 and Cyclophilin 80 % MST power were used. The Laser-On time was always set to 30 sec, the Laser-Off time 5 sec. References Ikura M, Kay LE, Krinks M, Bax A: Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix. Biochemistry 1991, 4;30(22):5498-5504. Blumenthal DK, Takio K, Edelman AM, Charbonneau H, Titani K, Walsh KA, Krebs EG: Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proc Natl Acad Sci U S A. 1985 May 82(10): 3187–3191. Gerrits M, Strey J, Claußnitzer I, von Groll U, Schäfer F, Rimmele M, Stiege W: Cell-free Synthesis of Defined Protein Conjugates by Site-directed Cotranslational Labeling. In: T. Kudlicki, F. Katzen, R. Bennett (Ed.) Cell-free Expression. Landes Bioscience, Austin. 2007 Serwa R, Wilkening I, Del Signore G, Muehlberg M, Claußnitzer I, Weise C, Gerrits M, Hackenberger C: Chemoselective Staudinger-Phosphite Reaction of Azides for the Phosphorylation of Proteins. Angew Chem Int Ed 2009, 48: 1–6 Prescher JA, Bertozzi CR: Chemistry in living systems. Nature Chem Biol 2005, 1(1), 13-21 Chin J, Santoro S, Martin A, King D, Wang L, Schultz P: Addition of p-Azido-L-phenylalanine to the Genetic Code of Escherichia coli. J Am Chem Soc 2002, 124(31), 9026-9027 © 2011 NanoTemper Technologies GmbH

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