Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

Protein function depends on transitions from the ground state to higher energy states.
Deviations from the ground-state structure result from chemical reactivity and conformational …

Membrane encapsulation is frequently used by the cell to sequester biomolecules and
compartmentalize their function. Cells also concentrate molecules into phase-separated …

This review surveys recent investigations of conformational fluctuations of proteins in
solution using NMR techniques. Advances in experimental methods have provided more …

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique that can be used
to investigate the structure, dynamics, and chemical kinetics of a wide range of biochemical …

▪ Abstract NMR spin relaxation spectroscopy is a powerful approach for characterizing
intramolecular and overall rotational motions in proteins. This review describes experimental …

Chemical shifts are the universal language of nuclear magnetic resonance (NMR). They
communicate in a simple way detailed molecular information that almost every chemist can …

The chemical shift of a nucleus, i, in a molecule arises from the nuclear shielding effect of an
applied magnetic field, caused by an induced magnetic field resulting from circulation of …

Rational drug design is predicated on knowledge of the three-dimensional structure of the
protein− ligand complex and the thermodynamics of ligand binding. Despite the …

Herein we describe the program FAST-Modelfree for the fully automated, high throughput
analysis of NMR spin-relaxation data. This program interfaces with the program Modelfree …