By using only half of the total evolution time for dephasing pulses, C{N} rotational-echo double resonance (REDOR) for clusters of C spins (RDX) results in the same universal REDOR behavior as observed for isolated C-N pairs. RDX combines Hahn echoes with solid echoes to suppress interference from scalar J couplings. This is crucial for long evolution times. The modified version (which we call RDX24) makes RDX quantitative for C clusters. We apply this scheme to human embryonic kidney cells labeled in culture by L-[C -N]-glutamine. We quantitatively characterize three separate nitrogen isotopic enrichments for: (i) the alpha nitrogens of glutamine residues in proteins (including the residues of the five amino acids synthesized from glutamine); (ii) the alpha nitrogens of the five amino-acid residues synthesized from glucose, together with those of the nine essential amino acids added to the growth medium; and (iii) the side-chain nitrogens of glutamine (and of asparagine derived from glutamine).
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http://dx.doi.org/10.1016/j.jmr.2021.107043 | DOI Listing |
Proc Natl Acad Sci U S A
December 2024
Department of Chemistry, Michigan State University, East Lansing, MI 48824.
HIV, like other membrane-enveloped viruses, has protein spikes that include a fusion peptide (Fp) segment that binds the host cell membrane and plays a critical role in fusion (joining) viral and cell membranes. The HIV Fp is the ~23 N-terminal residues of the gp41 spike protein. Fp adopts intermolecular antiparallel β sheet structure when lipid fraction cholesterol ≈0.
View Article and Find Full Text PDFLangmuir
October 2024
Department of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Dr., San Diego, California 92182-1030, United States.
JACS Au
September 2024
School of Chemistry, Faculty of Exact sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
The development of robust NMR methodologies to probe dynamics on the atomic scale is vital to elucidate the close relations between structure, motion, and function in biological systems. Here, we present an automated protocol to measure, using magic-angle spinning NMR, the effective C-N dipolar coupling constants between multiple spin pairs simultaneously with high accuracy. We use the experimental dipolar coupling constants to quantify the order parameters of multiple C-N bonds in the thousands of identical copies of the coat protein in intact fd-Y21M filamentous bacteriophage virus and describe its overall dynamics on the submillisecond time scale.
View Article and Find Full Text PDFACS Nano
August 2024
Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada.
Inorganic colloidal cesium lead halide perovskite nanocrystals (NCs) encapsulated by surface capping ligands exhibit tremendous potential in optoelectronic applications, with their surface structure playing a pivotal role in enhancing their photophysical properties. Soy lecithin, a tightly binding zwitterionic surface-capping ligand, has recently facilitated the high-yield synthesis of stable ultraconcentrated and ultradilute colloids of CsPbX NCs, unlocking a myriad of potential device applications. However, the atomic-level understanding of the ligand-terminated surface structure remains uncertain.
View Article and Find Full Text PDFJ Phys Chem B
June 2024
School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
Q11 peptide nanofibers are used as a biomaterial for applications such as antigen presentation and tissue engineering, yet detailed knowledge of molecular-level structure has not been reported. The Q11 peptide sequence was designed using heuristics-based patterning of hydrophobic and polar amino acids with oppositely charged amino acids placed at opposite ends of the sequence to promote antiparallel β-sheet formation. In this work, we employed solid-state nuclear magnetic resonance spectroscopy (NMR) to evaluate whether the molecular organization within Q11 self-assembled peptide nanofibers is consistent with the expectations of the peptide designers.
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