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Titlebook: Biophysics and Synchrotron Radiation; Antonio Bianconi,Agostina Congiu Castellano Conference proceedings 1987 Springer-Verlag Berlin Heide

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Lateral Alignment of Epitaxial Quantum Dotsheavy and light meromyosin (HMM and LMM). Heavy meromyosin has two heads and each head contains an ATP hydrolyzing site and an actin binding site (1, 2). Heavy meromyosin (HMM) can be divided by proteolytic reagents into subfragment-1 and subfragment-2 (SI and S2). It is important to know on the mec
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https://doi.org/10.1007/978-3-540-46936-0pair distribution function, i. e. the first order correlation function of local atomic distribution, since the beginning of x-ray spectroscopy of biological molecules. and it is currently used to investigate metalloproteins.. It was pointed out that the x-ray absorption spectra of biological molecul
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https://doi.org/10.1007/978-3-540-46936-0 spite of extensive experimental research. Diffraction experiments are limited to crystallized proteins, on the contrary x-ray absorption near edge structure (XANES) spectroscopy is a tool for determination of local structure of active site in metalloproteins in solution..
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https://doi.org/10.1007/978-3-540-46936-0ectron acceptor. The resting form of HRP contains a high-spin ferric heme. During the catalytic cycle, HRP is initially oxidized by two electrons to a green species known as Compound I (HRP-I). One electron reduction of HRP-I yields the red species known as Compound II (HRP-II), that retains one oxi
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