Publications by authors named "Brent Runge"
Traditional protein structure determination by magic angle spinning (MAS) solid-state NMR spectroscopy primarily relies on interatomic distances up to 8 Å, extracted from C-, N-, and H-based dipolar-based correlation experiments. Here, we show that F fast (60 kHz) MAS NMR spectroscopy can supply additional, longer distances. Using 4F-Trp,U-C,N crystalline agglutinin (OAA), we demonstrate that judiciously designed 2D and 3D F-based dipolar correlation experiments such as (H)CF, (H)CHF, and FF can yield interatomic distances in the 8-16 Å range.
View Article and Find Full Text PDFObtaining atomic-level information on components in the cell is a major focus in structural biology. Elucidating specific structural and dynamic features of proteins and their interactions in the cellular context is crucial for understanding cellular processes. We introduce F dynamic nuclear polarization (DNP) combined with fast magic-angle-spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy as a powerful technique to study proteins in mammalian cells.
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- * Researchers used advanced techniques like solid-state magic angle spinning NMR and X-ray diffraction to determine the detailed atomic structure of the N protein, revealing insights about its flexibility and binding to RNA.
- * The findings provide valuable information for designing effective therapies against SARS-CoV-2 by targeting the structure of the nucleocapsid protein.
Article Synopsis
- Reverse transcription, crucial for HIV-1 replication, depends on the import of deoxynucleotide triphosphates (dNTPs) through a channel in the viral capsid.
- Molecular dynamics simulations show that cooperative binding of nucleotides in the capsid enhances the passive entry of dNTPs, while certain molecules like inositol hexakisphosphate (IP6) increase this import, and benzenehexacarboxylic acid (BHC) decreases it.
- The study utilized various microscopy techniques and virological assays to demonstrate how these interactions impact HIV-1's ability to stabilize its capsid and perform reverse transcription.
Article Synopsis
- Researchers have developed a new HCN CPMAS probe that increases sensitivity in MAS NMR experiments by 3-4 times, allowing for better analysis of complex biological systems.
- This probe operates with its sample coil and electronics at cryogenic temperatures while maintaining the sample at normal temperatures, which enhances data collection for 2D and 3D experiments.
- The technology has shown promising results with difficult samples, such as protein assemblies and prion fibrils, suggesting it could greatly benefit studies involving low-sensitivity biological systems.
The host factor protein TRIM5α plays an important role in restricting the host range of HIV-1, interfering with the integrity of the HIV-1 capsid. TRIM5 triggers an antiviral innate immune response by functioning as a capsid pattern recognition receptor, although the precise mechanism by which the restriction is imposed is not completely understood. Here we used an integrated magic-angle spinning nuclear magnetic resonance and molecular dynamics simulations approach to characterize, at atomic resolution, the dynamics of the capsid's hexameric and pentameric building blocks, and the interactions with TRIM5α in the assembled capsid.
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