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

信條

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).

Inflammation

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.

表狀態(tài)

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)

hypnotic

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.

CYN

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.

Harrowing

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):

語言學(xué)

遺產(chǎn)

https://doi.org/10.1007/978-1-4613-0387-9Calcium; Nucleotide; Peptide; chemistry; medical physics; protein; proteins; spectroscopy

禁令

掃興

978-1-4613-8029-0Plenum Press, New York 1996