1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning
T Le Marchand, T Schubeis, M Bonaccorsi… - Chemical …, 2022 - ACS Publications
Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …
ago, 1H detection has evolved into the most efficient approach for investigation of …
NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function
TR Alderson, LE Kay - Cell, 2021 - cell.com
Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …
malfunctions can cause disease, it is necessary to describe their three-dimensional …
Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation
Membrane encapsulation is frequently used by the cell to sequester biomolecules and
compartmentalize their function. Cells also concentrate molecules into phase-separated …
compartmentalize their function. Cells also concentrate molecules into phase-separated …
The ensemble nature of allostery
Allostery is the process by which biological macromolecules (mostly proteins) transmit the
effect of binding at one site to another, often distal, functional site, allowing for regulation of …
effect of binding at one site to another, often distal, functional site, allowing for regulation of …
Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants
Despite the prominent role of the K-Ras protein in many different types of human cancer,
major gaps in atomic-level information severely limit our understanding of its functions in …
major gaps in atomic-level information severely limit our understanding of its functions in …
An introduction to NMR-based approaches for measuring protein dynamics
IR Kleckner, MP Foster - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2011 - Elsevier
Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …
characterized by a set of conformations that undergo continuous exchange within a …
Studying “invisible” excited protein states in slow exchange with a major state conformation
P Vallurupalli, G Bouvignies, LE Kay - Journal of the American …, 2012 - ACS Publications
Ever since its initial development, solution NMR spectroscopy has been used as a tool to
study conformational exchange. Although many systems are amenable to relaxation …
study conformational exchange. Although many systems are amenable to relaxation …
Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules …
Understanding the function of biological macromolecules and their complexes at the
physicochemical level requires knowledge of both their structure and dynamics …
physicochemical level requires knowledge of both their structure and dynamics …
Intrinsic dynamics of an enzyme underlies catalysis
EZ Eisenmesser, O Millet, W Labeikovsky… - Nature, 2005 - nature.com
A unique feature of chemical catalysis mediated by enzymes is that the catalytically reactive
atoms are embedded within a folded protein. Although current understanding of enzyme …
atoms are embedded within a folded protein. Although current understanding of enzyme …
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis
Conformational dynamics play a key role in enzyme catalysis. Although protein motions
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …