Solid state nuclear magnetic resonance最新文献

This study builds upon our prior researches and seeks to investigate and clarify the influences of various characteristics of hydrogen bonds (H-bonds) and charge transfer (CT) interactions, which were detected within the inhibitor binding pockets (labeled as the QM models I–IV) of MraY_AA–capuramycin, MraY_AA–carbacaprazamycin, MraY_AA–3′-hydroxymureidomycin A, and MraY_AA–muraymycin D2 complexes by QTAIM and NBO analyses from DFT QM/MM MD calculations, on the ¹⁷O chemical shielding (CS) and electric field gradient (EFG) tensors of carboxylate (Oδ), carbonyl (C═O), and hydroxyl (O–H) oxygens in these models. The ¹⁷O CS and EFG tensors of these three types of oxygens in QM models I–IV were calculated at the M06-2X/6-31G** level by including the solvent effects using the polarizable continuum model. From the computed ¹⁷O CS and EFG tensors in these models, it was found that the nuclear shielding, σ_iso, for carboxylate or carbonyl oxygen increases (shielding effect) as the H-bond length decreases and the percentage p-character of n_Oδ/n_C═O lone pair partner in the CT interaction enhances. In contrast, the σ_iso (¹⁷O–H) decreases (deshielding effect) with a reduction in the H-bond length as well as with an enhancement in percentage s-character of the n_OH lone pair/σ*_O–H antibond. By reducing the H-bond length or by increasing p-character of the n_Oδ/n_C═O lone pair, the ¹⁷Oδ/¹⁷O═C quadrupole coupling constant smoothly decreases, while the ¹⁷Oδ/¹⁷O═C asymmetry parameter smoothly increases. Moreover, these calculated parameters are in a good agreement with the experimental values. The information garnered here is valuable particularly for further understanding of empirical correlations between ¹⁷O NMR spectroscopic and H-bonding characteristics in the protein–ligand complexes.

In this work, we elucidated the structural organization of stimuli-responsive peptide-polydiacetylene (PDA) conjugates that can self-assemble as 1D nanostructures under neutral aqueous conditions. The amino acid sequences bear positively or negatively charged domains at the periphery of the peptide segments to promote solubility in water while also driving assembly of the individual and combined components into β-sheets. The photopolymerization of PDA, as well as the sensitivity of the resulting optical properties of the polymeric material to external stimuli, highly depends on the structural organization of the assembly of amphiphilic peptide-diacetylene units into 1D-nanostructures. Solid-state NMR measurements on ¹³C-labeled and ¹⁵N-labeled samples show that positively charged and negatively charged peptide amphiphiles are each capable of self-assembly, but self-assembly favors antiparallel β-sheet structure. When positively and negatively charged peptide amphiphiles interact in stoichiometric solutions, cooperative coassembly dominates over self-assembly, resulting in the desired parallel β-sheet structure with a concomitant increase in structural order. These results reveal that rational placement of oppositely charged residues can control β-strand organization in a peptide amphiphile coassembly, which would have implications on the adaptive properties of stimuli-responsive biomaterials such as the peptide-PDAs studied here.

Planewave-corrected methods have proven effective for accurately modeling nuclear magnetic resonance (NMR) parameters in crystalline systems. Recent work extended the application of planewave-corrected calculations beyond the second row, predicting EFG tensor parameters for ³⁵Cl using a simple molecular correction to projector augmented-wave (PAW) density functional theory (DFT). Here we extend this work using fragment and cluster-based calculations coupled with polarizable continuum (PCM) methods to improve further the accuracy of planewave-corrected ³⁵Cl EFG tensor calculations. Benchmark data from a test set comprised of 105 individual ³⁵Cl EFG tensor principal components for chlorine-containing molecular crystals and crystalline chloride salts shows fragment-corrected planewave calculations using the PBE0 hybrid density functional improve the accuracy of predicted EFG tensor components by 30 % relative to traditional planewave calculations. We compare the influence of different geometry optimization methods and density functionals on the accuracy of predicted ³⁵Cl EFG tensor parameters. Four cases of spectral assignment are presented to demonstrate the utility of improving the accuracy of predicted ³⁵Cl EFG tensor parameters.

While syringyl units are the most abundant monolignols in hardwood lignin, their phenolic (i.e. hydroxyl) end group concentration has not been measured. In two uniformly ¹³C-enriched young hardwoods, from beech and oak, the syringyl units were quantitatively investigated by advanced solid-state ¹³C NMR. Small signals of OH-terminated syringyl units were resolved in spectrally edited two-dimensional ¹³C–¹³C NMR spectra of the two hardwoods. Their distinct peak positions predicted based on literature data were validated via the abundant OH-terminated syringyl units in hydrolyzed ¹³C-beechwood. In a two-dimensional ¹³C–¹³C exchange spectrum with diagonal-ridge suppression, a well-resolved peak of phenolic syringyl units was observed at the characteristic C–H peak position of syringyl rings, without significant overlap from guaiacyl peaks. Accurate ¹³C chemical shifts of regular and end-group syringyl units were obtained. Through spectrally edited 2D NMR after ¹H inversion recovery, phenols of condensed tannin complexed with arginine were carefully analyzed and shown to overlap minimally with signals from phenolic syringyl units. The local structure and resulting spin dynamics of ether (chain) and hydroxyl (end-group) syringyl units are nearly the same, enabling quantification by peak integration or deconvolution, which shows that phenolic syringyl end groups account for 2 ± 1 % of syringyl units in beechwood and 5 ± 2 % in oakwood. The observed low end-group concentration needs to be taken into account in realistic molecular models of hardwood lignin structure.