Studying Molecular 3D Structure and Dynamics by High-Resolution Solid-State NMR:  Application to l-Tyrosine-Ethylester

Abstract

A unified approach to the study of 3D conformation and molecular dynamics using magic-angle-spinning solid-state NMR is demonstrated on a uniformly 13C-labeled sample of L-tyrosine-ethylester.

High‐Resolution Solid‐State NMR Studies on Uniformly [13C,15N]‐Labeled Ubiquitin

“…Figure 2 shows an NCA-type spectrum obtained on UBI-P with an 800 MHz instrument. Additional experiments using variable 1 H decoupling strength reveal that the detected 15 N line width (0.8 ppm) is sensitive to the 1 H r.f. decoupling field strength in the 70-95 kHz range.…”

“…Such efforts have given rise to a handful of 3D structures ranging from two-and three-residue peptides to small proteins. [3,[11][12][13] In particular, we have shown [13][14][15] that 3D molecular structures can be constructed through the use of a single, uniformly labeled sample.…”

“…We conclude that the influence of sample preparation on 3D protein structure determination in solids is [ Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly [ 13 C, 15 N]-labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the construction of 3D molecular structure and study the influence of solid-phase protein preparation on solid-state NMR spectra. A comparative analysis of 13 C', 13 Ca, and 13 Cb resonance frequencies suggests that 13 C chemical-shift variations are most likely to occur in protein regions that exhibit an enhanced degree of molecular mobility.…”

A Combined Solid‐State NMR and MD Characterization of the Stability and Dynamics of the HET‐s(218‐289) Prion in its Amyloid Conformation

“…C a correlation spectrum of HET-sA C H T U N G T R E N N U N G (218-289) amyloid fibrils recorded on a 850 MHz spectrometer. The experiment is based on dipole-mediated polarization transfer, and therefore, only residues with high-order parameters [25,26] S 2 (on the NMR timescale of ms) give rise to signals. Typical observed line widths were 0.9 ppm and 0.5 ppm for 15 N and 13 C, respectively.…”

Investigation of Ligand‐Receptor Systems by High‐Resolution Solid‐State NMR: Recent Progress and Perspectives

“…In both cases, the three-dimensional molecular structure was obtained from a single, uniformly-labeled sample. For example, in Figure 3A the 3D structure of l-Tyrosine ethyl ester determined from a single uniformly labeled sample [26] is shown. The corresponding CHHC data set shows a ( construct the 3D structure of the molecule in the polycrystalline state.…”