Jaka Kragelj
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View article: Fast MAS NMR Spectroscopy Can Identify G-Quartets and Double-Stranded Structures in Aggregates Formed by GGGGCC RNA Repeats
Fast MAS NMR Spectroscopy Can Identify G-Quartets and Double-Stranded Structures in Aggregates Formed by GGGGCC RNA Repeats Open
The expansion of GGGGCC repeats within the C9orf72 gene has been linked to amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). In neurons from patients with expanded repeats, C9orf72 GGGGCC repeat RNA predominantly forms…
View article: Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells
Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells Open
The protein α-syn adopts a wide variety of conformations including an intrinsically disordered monomeric form and an α-helical-rich membrane-associated form that is thought to play an important role in cellular membrane processes. However,…
View article: Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1
Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1 Open
Scaffold proteins are key players in many signaling pathways where they ensure spatial and temporal control of molecular interactions by simultaneous tethering of multiple signaling components. The protein JIP1 acts as a scaffold within th…
View article: Structural context modulates the conformational ensemble of the intrinsically disordered amino terminus of α-synuclein
Structural context modulates the conformational ensemble of the intrinsically disordered amino terminus of α-synuclein Open
Regions of intrinsic disorder play crucial roles in biological systems, yet they often elude characterization by conventional biophysical techniques. To capture conformational distributions across different timescales, we employed a freezi…
View article: Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells
Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells Open
The protein α-syn adopts a wide variety of conformations including an intrinsically disordered monomeric form and an α-helical rich membrane-associated form that is thought to play an important role in cellular membrane processes. However,…
View article: Conformational ensembles explain <scp>NMR</scp> spectra of frozen intrinsically disordered proteins
Conformational ensembles explain <span>NMR</span> spectra of frozen intrinsically disordered proteins Open
Protein regions which are intrinsically disordered, exist as an ensemble of rapidly interconverting structures. Cooling proteins to cryogenic temperatures for dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR studies suspen…
View article: DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular environments
DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular environments Open
With the sensitivity enhancements conferred by dynamic nuclear polarization (DNP), magic angle spinning (MAS) solid state NMR spectroscopy experiments can attain the necessary sensitivity to detect very low concentrations of proteins. This…
View article: The conformational ensemble of an intrinsically disordered protein explains peak shapes under DNP conditions
The conformational ensemble of an intrinsically disordered protein explains peak shapes under DNP conditions Open
Elucidating the conformational preferences of regions of intrinsic disorder in biologically relevant contexts represents a frontier of structural biology. The sensitivity enhancements conferred by DNP enable structural studies of proteins …
View article: Visualizing protein breathing motions associated with aromatic ring flipping
Visualizing protein breathing motions associated with aromatic ring flipping Open
Aromatic residues cluster in the core of folded proteins, where they stabilize the structure through multiple interactions. Nuclear magnetic resonance (NMR) studies in the 1970s showed that aromatic side chains can undergo ring flips—that …
View article: In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells Open
NMR has the resolution and specificity to determine atomic-level protein structures of isotopically labeled proteins in complex environments, and with the sensitivity gains conferred by dynamic nuclear polarization (DNP), NMR has the sensi…
View article: Enthalpy–Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners
Enthalpy–Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners Open
Intrinsically disordered proteins (IDPs) can engage in promiscuous interactions with their protein targets; however, it is not clear how this feature is encoded in the primary sequence of the IDPs and to what extent the surface properties …
View article: In-Cell Sensitivity-Enhanced NMR of Intact Living Mammalian Cells
In-Cell Sensitivity-Enhanced NMR of Intact Living Mammalian Cells Open
NMR has the resolution and specificity to determine atomic-level protein structures of isotopically-labeled proteins in complex environments and, with the sensitivity gains conferred by dynamic nuclear polarization (DNP), NMR has the sensi…
View article: Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability Open
Dynamic nuclear polarization (DNP) can dramatically increase the sensitivity of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy. These sensitivity gains increase as temperatures decrease and are large enough to ena…
View article: Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability
Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability Open
Dynamic nuclear polarization (DNP) can dramatically increase the sensitivity of magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy. These sensitivity gains increase as temperatures decrease and are large enough to ena…