ArticleMethods in molecular biology (Clifton, N.J.)2012
Solid-state NMR spectroscopy of protein complexes.
Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.Journal of the American Chemical Society · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics.Molecules (Basel, Switzerland) · 2023Review
- Structural basis of HIV-1 maturation inhibitor binding and activity.Nature communications · 2023Article
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies.The journal of physical chemistry. B · 2019Article
- Ca(II) and Zn(II) Cooperate To Modulate the Structure and Self-Assembly of S100A12.Biochemistry · 2019Article
- Article
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies.The journal of physical chemistry. B · 2016Article
- Combined zero-quantum and spin-diffusion mixing for efficient homonuclear correlation spectroscopy under fast MAS: broadband recoupling and detection of long-range correlations.Journal of biomolecular NMR · 2015Article
- Magic angle spinning NMR reveals sequence-dependent structural plasticity, dynamics, and the spacer peptide 1 conformation in HIV-1 capsid protein assemblies.Journal of the American Chemical Society · 2013Article
- Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.Journal of biomolecular NMR · 2013Article
- (13)C-(13)c homonuclear recoupling in solid-state nuclear magnetic resonance at a moderately high magic-angle-spinning frequency.PloS one · 2013Article
- 3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.The journal of physical chemistry. B · 2012Article
- Motions on the millisecond time scale and multiple conformations of HIV-1 capsid protein: implications for structural polymorphism of CA assemblies.Journal of the American Chemical Society · 2012Article
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10 authors.
Funding
Abstract
Protein-protein interactions are vital for many biological processes. These interactions often result in the formation of protein assemblies that are large in size, insoluble, and difficult to crystallize, and therefore are challenging to study by structure biology techniques, such as single crystal X-ray diffraction and solution NMR spectroscopy. Solid-state NMR (SSNMR) spectroscopy is emerging as a promising technique for studies of such protein assemblies because it is not limited by molecular size, solubility, or lack of long-range order. In the past several years, we have applied magic angle spinning SSNMR-based methods to study several protein complexes. In this chapter, we discuss the general SSNMR methodologies employed for structural and dynamics analyses of protein complexes with specific examples from our work on thioredoxin reassemblies, HIV-1 capsid protein assemblies, and microtubule-associated protein assemblies. We present protocols for sample preparation and characterization, pulse sequences, SSNMR spectra collection, and data analysis.
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