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Titlebook: NMR as a Structural Tool for Macromolecules; Current Status and F B. D. Nageswara Rao,Marvin D. Kemple Book 1996 Plenum Press, New York 199

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Cross-Correlations: Obstacles or Tools for Structure Determination of Biomolecules,; Runnels, 1964; Werbelow and Grant, 1977; Void and Void, 1978). In relaxation studies using double resonance experiments it has been known that the cross-correlations play significant role and cannot be ignored (Anil Kumar and Nageshwara Rao, 1968).
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NMR Structures of Proteins Involved in Signal Transduction,lecular level.. In this paper, three-dimensional structures of three proteins that are involved in signal transduction will be described, including (1) a protein tyrosine phosphatase, (2) a pleckstrin homology (PH) domain, and (3) the DNA-binding domain of a member of the . family of transcription factors, Fli-1, in the DNA-bound form.
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Structures of Multimeric Proteins by NMR,xtension of these methods to multimeric proteins and illustrate these with regard to the solution structures of two dimers (interleukin-8; Clore et al., 1990; and human macrophage inflammatory protein 1β(3; Lodi et al., 1994) and a tetramer (the oligomerization domain of p53; Clore et al., 1994, 1995a,b)
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NMR Structural Studies of Flexible Molecules,iption of structure is complicated by the inevitable population-weighted averaging of the key NMR parameters. Here we describe simple procedures for calculation of the dominant structure in the conformational ensemble of a linear peptide and for characterizing the domain motions and overall structural preferences of multidomain proteins.
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Panel Discussion,ve minute statements from the panel members about points that might be relevant to the topics of this discussion and after that we will have a general discussion. The panel members may wish to ask some questions and everybody from the audience is invited to ask questions and contribute to this discussion.
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Towards the Accurate Measurement of Internuclear Distances in Biological Macromolecules by Suppresstion between spins can be described by a master equation which for two spins A and X takes the form of two coupled differential equations describing the rate of change of the longitudinal magnetization, the Solomon equations (Solomon, 1955; Ernst et al., 1987):
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https://doi.org/10.1007/978-1-4613-0387-9Calcium; Nucleotide; Peptide; chemistry; medical physics; protein; proteins; spectroscopy
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978-1-4613-8029-0Plenum Press, New York 1996
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