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Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite - ScienceDirect.com
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite - ScienceDirect.com

Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite ScienceDirect.com Read here
0 Replies | 57 Views
NMR solution structure determination of large RNA-protein complexes - ScienceDirect.com
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar NMR solution structure determination of large RNA-protein complexes - ScienceDirect.com

NMR solution structure determination of large RNA-protein complexes ScienceDirect.com Read here
0 Replies | 86 Views
[NMR paper] Genetically encoded site-specific (19)F unnatural amino acid incorporation in V. natriegens for in-cell NMR analysis
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar Genetically encoded site-specific (19)F unnatural amino acid incorporation in V. natriegens for in-cell NMR analysis

Nuclear magnetic resonance (NMR) spectroscopy NMR is a well-established technique for probing protein structure, dynamics and conformational changes. Taking advantage of the high signal sensitivity and broad chemical shift range of ^(19)F nuclei, ^(19)F NMR has been applied to investigate protein function at atomic resolution. In this report, we extend the unnatural amino acid site-specific incorporation into V. natriegens, an alternate protein expression system. The unnatural amino acid...

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0 Replies | 112 Views
[NMR paper] NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4
Mar 09, 2024 - 12:05 AM - by nmrlearner
nmrlearner's Avatar NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4

KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the ¹H, ^(13)C and ^(15)N resonance assignments for the BRCT domain of KKT4...

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0 Replies | 240 Views
[NMR paper] High-efficiency low-power (13)C-(15)N cross polarization in MAS NMR
Mar 09, 2024 - 12:05 AM - by nmrlearner
nmrlearner's Avatar High-efficiency low-power (13)C-(15)N cross polarization in MAS NMR

Biomolecular solid-state magic angle spinning (MAS) NMR spectroscopy frequently relies on selective ^(13)C-^(15)N magnetization transfers, for various kinds of correlation experiments. Introduced in 1998, spectrally induced filtering in combination with cross polarization (SPECIFIC-CP) is a selective heteronuclear magnetization transfer experiment widely used for biological applications. At MAS frequencies below 20 kHz, commonly used for ^(13)C-detected MAS NMR experiments, SPECIFIC-CP transfer...

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0 Replies | 53 Views
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation - ScienceDirect.com
Mar 07, 2024 - 10:30 PM - by nmrlearner
nmrlearner's Avatar Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation - ScienceDirect.com

Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation ScienceDirect.com Read here
0 Replies | 84 Views
[NMR paper] In-cell NMR suggests that DNA i-motif levels are strongly depleted in living human cells
Mar 06, 2024 - 5:10 PM - by nmrlearner
nmrlearner's Avatar In-cell NMR suggests that DNA i-motif levels are strongly depleted in living human cells

I-Motifs (iM) are non-canonical DNA structures potentially forming in the accessible, single-stranded, cytosine-rich genomic regions with regulatory roles. Chromatin, protein interactions, and intracellular properties seem to govern iM formation at sites with i-motif formation propensity (iMFPS) in human cells, yet their specific contributions remain unclear. Using in-cell NMR with oligonucleotide iMFPS models, we monitor iM-associated structural equilibria in asynchronous and cell...

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0 Replies | 50 Views
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