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Titlebook: High Resolution EPR; Applications to Meta Lawrence Berliner,Graeme‘Hanson Book 2009 Springer-Verlag New York 2009 X-ray.chemistry.dynamics.

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書(shū)目名稱(chēng)High Resolution EPR
副標(biāo)題Applications to Meta
編輯Lawrence Berliner,Graeme‘Hanson
視頻videohttp://file.papertrans.cn/427/426475/426475.mp4
概述Essential research in an area that hasn‘t been covered as a full volume for more than a decade.Includes supplementary material:
叢書(shū)名稱(chēng)Biological Magnetic Resonance
圖書(shū)封面Titlebook: High Resolution EPR; Applications to Meta Lawrence Berliner,Graeme‘Hanson Book 2009 Springer-Verlag New York 2009 X-ray.chemistry.dynamics.
描述.Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms..This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community wit
出版日期Book 2009
關(guān)鍵詞X-ray; chemistry; dynamics; magnetic resonance; medicine; proteins; spectroscopy
版次1
doihttps://doi.org/10.1007/978-0-387-84856-3
isbn_softcover978-1-4899-8345-9
isbn_ebook978-0-387-84856-3Series ISSN 0192-6020 Series E-ISSN 2512-2215
issn_series 0192-6020
copyrightSpringer-Verlag New York 2009
The information of publication is updating

書(shū)目名稱(chēng)High Resolution EPR影響因子(影響力)




書(shū)目名稱(chēng)High Resolution EPR影響因子(影響力)學(xué)科排名




書(shū)目名稱(chēng)High Resolution EPR網(wǎng)絡(luò)公開(kāi)度




書(shū)目名稱(chēng)High Resolution EPR網(wǎng)絡(luò)公開(kāi)度學(xué)科排名




書(shū)目名稱(chēng)High Resolution EPR被引頻次




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書(shū)目名稱(chēng)High Resolution EPR讀者反饋




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978-1-4899-8345-9Springer-Verlag New York 2009
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High Resolution EPR978-0-387-84856-3Series ISSN 0192-6020 Series E-ISSN 2512-2215
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Probing the Structure–Function Relationship of Heme Proteins Using Multifrequency Pulse EPR TechniquAlthough EPR has been used regularly in the study of heme proteins for more than 40 years now, the use of multifrequency and/or pulse-EPR techniques is still quite scarce. Here, a review of the use of these methods is presented, highlighting the advantages, limitations, and challenges for the future.
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Introduction,in mind particularly the conference volume, . edited by Ehrenberg, Malmstr?m, and Vanng?rd [1]. In those days the reports were all based on continuous-wave (CW) EPR, computer simulations were in their infancy, ENDOR (Electron Nuclear Double Resonance) was dominantly still, but not exclusively, found
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Advanced Pulse EPR Methods for the Characterization of Metalloproteinsf pulse EPR spectroscopy. These techniques are typically used to obtain the static spin Hamiltonian parameters of powders, frozen solutions, and single crystals. The development of new methods based on these two effects is mainly driven by the need for higher resolution, and therefore, a more accura
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