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 …

One of the fundamental challenges of physical biology is to understand the relationship
between protein dynamics and function. At physiological temperatures, functional motions …

Slow timescale dynamics in proteins are essential for a variety of biological functions
spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as …

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 …

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 …

We have investigated the effect of deuteration of non‐exchangeable protons on protein
global thermal stability, hydrophobicity, and local flexibility using well‐known thermostable …

In this review, we discuss the experimental static deuteron NMR techniques and
computational approaches most useful for the investigation of side-chain dynamics in …

Post-translationally modified (PTM) amyloid-β (Aβ) species can play an important role in
modulating Alzheimer's disease pathology. These relatively less populated modifications …

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 …

We conducted a detailed investigation of the dynamics of two phenylalanine side chains in
the hydrophobic core of the villin headpiece subdomain protein (HP36) in the hydrated …