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Titlebook: Mass Spectrometry of Proteins and Peptides; John R. Chapman Book 20001st edition Humana Press 2000

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書目名稱Mass Spectrometry of Proteins and Peptides
編輯John R. Chapman
視頻videohttp://file.papertrans.cn/626/625282/625282.mp4
概述Includes supplementary material:
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Mass Spectrometry of Proteins and Peptides;  John R. Chapman Book 20001st edition Humana Press 2000
描述Little more than three years down the line and I am already writing the Preface to a second volume to follow Protein and Peptide Analysis by Mass . What has happened in between these times to make this second venture worthwhile? New types of mass spectrometric instrumentation have appeared so that new techniques have become possible and existing techniques have become much more feasible. More particularly, however, the newer ionization te- niques, introduced for the analysis of high molecular weight materials, have now been thoroughly used and studied. As a result, there has been an en- mous improvement in the associated sample handling technology so that these methods are now routinely applied to much smaller sample amounts as well as to more intractable samples. Again, this particular community of mass spectrometry users has both increased in number and diversified. And, riding this wave of acceptance, leaders in the field have set their sights on more complex problems: molecular interaction, ion structures, quantitation, and kinetics are just a few of the newer areas reported in Mass Spectrometry of Proteins and Peptides. As with the first volume, one purpose of this collection,
出版日期Book 20001st edition
版次1
doihttps://doi.org/10.1385/1592590454
isbn_ebook978-1-59259-045-2Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2000
The information of publication is updating

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Investigating the Higher Order Structure of Proteins,n deuteration. Since deuterium weighs 1 Dalton more than protium, hydrogen exchange in proteins can also be detected by mass spectrometry. This approach is complementary to NMR in some respects and clearly advantageous in others.
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Preparation and Mass Spectrometric Analysis of S-Nitrosohemoglobin,ion .,., there is considerably less data on NO-Cys interactions. One reason is the labile nature of nitrosothiols RSNOs, which are unstable in aqueous solution. It has been assumed that the lability of RSNOs is due to their propensity to undergo homolytic cleavage of the S-N bond with release of NO ..
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