Rengifo, Anthony Sementilli, Youngsun Kim, Chen Liang, Noel Xiang'An Li, Anil K. The Helical Structure of Surfactant Peptide KL4 When Bound to POPC: POPG Lipid Vesicles. Chain-Folding Structure of a Semicrystalline Polymer in Bulk Crystals Determined by 13C–13C Double Quantum NMR.
Structural Unit of Polymer Crystallization in Dilute Solution As Studied by Solid-State NMR and 13C Isotope Labeling. Shijun Wang, Shichen Yuan, Wei Chen, Yang Zhou, You-lee Hong, Toshikazu Miyoshi.The Journal of Physical Chemistry B 2020, 124 Structure of a Parkinson’s Disease-Involved α-Synuclein Peptide Is Modulated by Membrane Composition and Physical State. Benjamin Martial, Gabrielle Raîche-Marcoux, Thierry Lefèvre, Pierre Audet, Normand Voyer, Michèle Auger.This article is cited by 12 publications. We also illustrate the ability of DQ-DRAWS to distinguish between structures in heterogeneous samples. This approach is considerably more sensitive for determining structure in helices and has comparable accuracy for β-sheet and extended conformations relative to other methods. It is shown how a simple choice of isotopic labels and experimental conditions allows accurate measurement of backbone secondary structures without any prior knowledge. Here, we explore the accuracies of the assumptions made in interpreting DQ-DRAWS data and demonstrate their fidelity in measuring torsion angles corresponding to a variety of secondary structures irrespective of hydrogen-bonding patterns. By allowing this DQ coherence to evolve, it is possible to measure the relative orientations of the CSA tensors and subsequently use this information to determine the Ramachandran torsion angles φ and ψ. Dipolar recoupling with a windowless sequence (DRAWS) has proven to be an effective pulse sequence for exciting double-quantum (DQ) coherences between adjacent carbonyl carbons along the peptide backbone. Additionally, the efficiency with which these dipolar recoupling experiments suppress the deleterious effects of chemical shift anisotropy (CSA) at high magnetic field strengths varies. However, many of these techniques measure only one torsion angle or are accurate for only certain classes of secondary structure. Several approaches for utilizing dipolar recoupling solid-state NMR (ssNMR) techniques to determine local structure at high resolution in peptides and proteins have been developed.
0 kommentar(er)
