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Titlebook: Distance Measurements in Biological Systems by EPR; Lawrence J. Berliner,Gareth R. Eaton,Sandra S. Eat Book 2000 Springer Science+Business

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書目名稱Distance Measurements in Biological Systems by EPR
編輯Lawrence J. Berliner,Gareth R. Eaton,Sandra S. Eat
視頻videohttp://file.papertrans.cn/282/281670/281670.mp4
叢書名稱Biological Magnetic Resonance
圖書封面Titlebook: Distance Measurements in Biological Systems by EPR;  Lawrence J. Berliner,Gareth R. Eaton,Sandra S. Eat Book 2000 Springer Science+Business
描述Distance measurements in biological systems by EPR The foundation for understanding function and dynamics of biological systems is knowledge of their structure. Many experimental methodologies are used for determination of structure, each with special utility. Volumes in this series on Biological Magnetic Resonance emphasize the methods that involve magnetic resonance. This volume seeks to provide a critical evaluation of EPR methods for determining the distances between two unpaired electrons. The editors invited the authors to make this a very practical book, with specific numerical examples of how experimental data is worked up to produce a distance estimate, and realistic assessments of uncertainties and of the range of applicability, along with examples of the power of the technique to answer biological problems. The first chapter is an overview, by two of the editors, of EPR methods to determine distances, with a focus on the range of applicability. The next chapter, also by the Batons, reviews what is known about electron spin relaxation times that are needed in estimating distances between spins or in selecting appropriate temperatures for particular experiments. Albert Bet
出版日期Book 2000
關(guān)鍵詞electron spin; electron spin echo; magnetic resonance; spectra; spectroscopy
版次1
doihttps://doi.org/10.1007/b111467
isbn_softcover978-1-4757-0575-1
isbn_ebook978-0-306-47109-4Series ISSN 0192-6020 Series E-ISSN 2512-2215
issn_series 0192-6020
copyrightSpringer Science+Business Media New York 2000
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NoC-Aware Computational Sprintingvantages for biomolecular labeling, its incorporation presents unique challenges in peptide synthesis and design. This chapter will briefly describe synthesis of TOAC-containing peptides, placement within peptide secondary structure, spectroscopy and recent applications.
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The Darwinian Tradition in Context distance distributions even at the lower end of this distance range by overcoming dead time problems. The measurement of ion cluster sizes and intercluster distances in ionomers is described to exemplify application of this method to a problem for which other methods for distance determination fail.
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Structural Information from CW-EPR Spectra of Dipolar Coupled Nitroxide Spin Labels,urther refinement of these methods for future applications are described. Reliable structural information can be obtained for interelectron distances ranging from 5 to 20 ? and up to 25 ? using perdeuterated probes.
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