Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins

R Verardi, NJ Traaseth, LR Masterson… - Isotope labeling in …, 2012 - Springer
In this chapter, we summarize the isotopic labeling strategies used to obtain high-quality
solution and solid-state NMR spectra of biological samples, with emphasis on integral …

Direct observation of hierarchical protein dynamics

JR Lewandowski, ME Halse, M Blackledge, L Emsley - Science, 2015 - science.org
One of the fundamental challenges of physical biology is to understand the relationship
between protein dynamics and function. At physiological temperatures, functional motions …

Static solid-state 2H NMR methods in studies of protein side-chain dynamics

L Vugmeyster, D Ostrovsky - Progress in Nuclear Magnetic Resonance …, 2017 - Elsevier
In this review, we discuss the experimental static deuteron NMR techniques and
computational approaches most useful for the investigation of side-chain dynamics in …

Peptide and protein dynamics and low-temperature/DNP magic angle spinning NMR

QZ Ni, E Markhasin, TV Can, B Corzilius… - The Journal of …, 2017 - ACS Publications
In DNP MAS NMR experiments at∼ 80–110 K, the structurally important− 13CH3 and−
15NH3+ signals in MAS spectra of biological samples disappear due to the interference of …

Deuteration of nonexchangeable protons on proteins affects their thermal stability, side‐chain dynamics, and hydrophobicity

PJ Nichols, I Falconer, A Griffin, C Mant… - Protein …, 2020 - Wiley Online Library
We have investigated the effect of deuteration of non‐exchangeable protons on protein
global thermal stability, hydrophobicity, and local flexibility using well‐known thermostable …

Modulation of aggregation and structural polymorphisms of β-amyloid fibrils in cellular environments by pyroglutamate-3 variant cross-seeding

L Cruceta, Y Sun, JM Kenyaga, D Ostrovsky… - Journal of Biological …, 2023 - jbc.org
Amyloidogenic deposition of β-amyloid (Aβ) peptides in human brain involves not only the
wild-type Aβ (wt-Aβ) sequences, but also posttranslationally modified Aβ (PTM-Aβ) variants …

[HTML][HTML] Flexibility and solvation of amyloid-β hydrophobic core

L Vugmeyster, MA Clark, IB Falconer… - Journal of Biological …, 2016 - Elsevier
Amyloid fibril deposits found in Alzheimer disease patients are composed of amyloid-β (Aβ)
protein forming a number of hydrophobic interfaces that are believed to be mostly rigid. We …

Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins

L Vugmeyster - Solid state nuclear magnetic resonance, 2021 - Elsevier
Slow timescale dynamics in proteins are essential for a variety of biological functions
spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as …

Effect of Cross-Seeding of Wild-Type Amyloid-β1–40 Peptides with Post-translationally Modified Fibrils on Internal Dynamics of the Fibrils Using Deuterium Solid …

A Rodgers, M Sawaged, D Ostrovsky… - The Journal of …, 2023 - ACS Publications
Post-translationally modified (PTM) amyloid-β (Aβ) species can play an important role in
modulating Alzheimer's disease pathology. These relatively less populated modifications …

Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils

DF Au, D Ostrovsky, R Fu, L Vugmeyster - Journal of Biological Chemistry, 2019 - jbc.org
Amyloid fibril deposits observed in Alzheimer's disease comprise amyloid-β (Aβ) protein
possessing a structured hydrophobic core and a disordered N-terminal domain (residues 1 …