Titlebook: NMR in the Life Sciences; E. Morton Bradbury,Claudio Nicolini Book 1986 Springer Science+Business Media New York 1986 MR imaging.NMR.biome

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書目名稱NMR in the Life Sciences影響因子(影響力)




書目名稱NMR in the Life Sciences影響因子(影響力)學(xué)科排名




書目名稱NMR in the Life Sciences網(wǎng)絡(luò)公開度




書目名稱NMR in the Life Sciences網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱NMR in the Life Sciences被引頻次




書目名稱NMR in the Life Sciences被引頻次學(xué)科排名




書目名稱NMR in the Life Sciences年度引用




書目名稱NMR in the Life Sciences年度引用學(xué)科排名




書目名稱NMR in the Life Sciences讀者反饋




書目名稱NMR in the Life Sciences讀者反饋學(xué)科排名

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Insatiable

Determination of Macromolecular Structure and Dynamics by NMR,nstraints, such as the assumption that a single rigid structure exists in solution which can be calculated from the data by minimizing either an error function or the energy of the structure. The danger of such procedures has been discussed elsewhere [8, 9, 10].

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形容詞

Proton-NMR of Nuclei, Cell and Intact Tissue in Normal and Abnormal States: Significance of Relaxat (6), have been correlated with cellular changes in water concentration (7). More importantly, it has been found (7) that prior to mitosis an increase in relaxation times of water protons preceeds by 4 hours the increase in water concentration, suggesting that a change in the physical state of water may preceed cell division.

dearth

Volume Selection Strategies for , Biological Spectroscopy,ield gradients. These techniques offer complementary advantages and often can be combined to suit a particular application. There follows a brief description of several methods which use these basic volume selection techniques in various combinations.

親屬

Signal, Noise and R. F. Power in Magnetic Resonance Imaging, Finally, the dangers of excessive power deposition in a patient are highlighted, and the use of a field in the range 0.5 to 1 Tesla advocated as giving good signal-to-noise ratio and versatility while not exceeding recommended power limits.

mendacity

Genetic Methods in High-Resolution NMR Studies of Proteins, the introduction of nuclear spin labels has facilitated the identification of individual residues (6–9). In this paper we describe how the techniques of molecular biology may be employed to facilitate the NMR study of large proteins. Illustrative examples will be taken from our studies of the bacteriophage λ repressor (10–12).

殘忍

Special Problems of NMR in H2O Solution,00% H.O. The latter is necessary if you want to observe exchangeable protons in a macromolecule, or if for some reason replacement of H.O by D.O is impractical. The large narrow HDO or H.O signal, equivalent to up to 100 molar proton concentration, presents various problems which will be outlined here, together with partial solutions.

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