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      Surface Induced Dissociation Coupled with High Resolution Mass Spectrometry Unveils Heterogeneity of a 211 kDa Multicopper Oxidase Protein Complex

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          Mass spectrometry and protein analysis.

          Mass spectrometry is a central analytical technique for protein research and for the study of biomolecules in general. Driven by the need to identify, characterize, and quantify proteins at ever increasing sensitivity and in ever more complex samples, a wide range of new mass spectrometry-based analytical platforms and experimental strategies have emerged. Here we review recent advances in mass spectrometry instrumentation in the context of current and emerging research strategies in protein science.
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            Native mass spectrometry: a bridge between interactomics and structural biology.

            Native mass spectrometry is an emerging technology that allows the topological investigation of intact protein complexes with high sensitivity and a theoretically unrestricted mass range. This unique tool provides complementary information to established technologies in structural biology, and also provides a link to high-throughput interactomics studies, which do not generate information on exact protein complex-composition, structure or dynamics. Here I review the current state of native mass spectrometry technology and discuss several important biological applications. I also describe current experimental challenges in native mass spectrometry, encouraging readers to contribute to solutions.
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              BIOGENIC MANGANESE OXIDES: Properties and Mechanisms of Formation

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                Author and article information

                Journal
                Journal of The American Society for Mass Spectrometry
                J. Am. Soc. Mass Spectrom.
                Springer Nature
                1044-0305
                1879-1123
                April 2018
                January 31 2018
                April 2018
                : 29
                : 4
                : 723-733
                Article
                10.1007/s13361-017-1882-x
                © 2018

                http://www.springer.com/tdm

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