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3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins.

ABSTRACT: Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly (13)C, (15)N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from (1)H to (13)C and (15)N to acquire two 3D experiments simultaneously. This is made possible by bidirectional polarization transfer between (13)C and (15)N and the long living (15)N z-polarization in solid state NMR. To demonstrate the power of this approach, four 3D pulse sequences (NCACX, CANCO, NCOCX, CON(CA)CX) are combined into two pulse sequences (3D DUMAS-NCACX-CANCO, 3D DUMAS-NCOCX-CON(CA)CX) that allow simultaneous acquisition of these experiments, reducing the experimental time by approximately half. Importantly, the 3D DUMAS-NCACX-CANCO experiment alone makes it possible to obtain the majority of the backbone sequential resonance assignments for microcrystalline U-(13)C,(15)N ubiquitin. The DUMAS approach is general and applicable to many 3D experiments, nearly doubling the performance of NMR spectrometers.

SUBMITTER: Gopinath T

PROVIDER: S-EPMC3487463 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature

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3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins.

Gopinath T T Veglia Gianluigi G

Journal of magnetic resonance (San Diego, Calif. : 1997) 20120426

Using the DUMAS (Dual acquisition Magic Angle Spinning) solid-state NMR approach, we created new pulse schemes that enable the simultaneous acquisition of three dimensional (3D) experiments on uniformly (13)C, (15)N labeled proteins. These new experiments exploit the simultaneous cross-polarization (SIM-CP) from (1)H to (13)C and (15)N to acquire two 3D experiments simultaneously. This is made possible by bidirectional polarization transfer between (13)C and (15)N and the long living (15)N z-pol ...[more]

PMID: 22698806

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Project description:Solid-state NMR spectroscopy is one of the most commonly used techniques to study the atomic-resolution structure and dynamics of various chemical, biological, material, and pharmaceutical systems spanning multiple forms, including crystalline, liquid crystalline, fibrous, and amorphous states. Despite the unique advantages of solid-state NMR spectroscopy, its poor spectral resolution and sensitivity have severely limited the scope of this technique. Fortunately, the recent developments in probe technology that mechanically rotate the sample fast (100 kHz and above) to obtain "solution-like" NMR spectra of solids with higher resolution and sensitivity have opened numerous avenues for the development of novel NMR techniques and their applications to study a plethora of solids including globular and membrane-associated proteins, self-assembled protein aggregates such as amyloid fibers, RNA, viral assemblies, polymorphic pharmaceuticals, metal-organic framework, bone materials, and inorganic materials. While the ultrafast-MAS continues to be developed, the minute sample quantity and radio frequency requirements, shorter recycle delays enabling fast data acquisition, the feasibility of employing proton detection, enhancement in proton spectral resolution and polarization transfer efficiency, and high sensitivity per unit sample are some of the remarkable benefits of the ultrafast-MAS technology as demonstrated by the reported studies in the literature. Although the very low sample volume and very high RF power could be limitations for some of the systems, the advantages have spurred solid-state NMR investigation into increasingly complex biological and material systems. As ultrafast-MAS NMR techniques are increasingly used in multidisciplinary research areas, further development of instrumentation, probes, and advanced methods are pursued in parallel to overcome the limitations and challenges for widespread applications. This review article is focused on providing timely comprehensive coverage of the major developments on instrumentation, theory, techniques, applications, limitations, and future scope of ultrafast-MAS technology.

Dataset Information

3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins.

Publications

3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins.

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