Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
AG Palmer III, CD Kroenke, JP Loria - Methods in enzymology, 2001 - Elsevier
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 …
Deviations from the ground-state structure result from chemical reactivity and conformational …
Protein dynamics from NMR
R Ishima, DA Torchia - Nature structural biology, 2000 - nature.com
This review surveys recent investigations of conformational fluctuations of proteins in
solution using NMR techniques. Advances in experimental methods have provided more …
solution using NMR techniques. Advances in experimental methods have provided more …
TDP-43 α-helical structure tunes liquid–liquid phase separation and function
Liquid–liquid phase separation (LLPS) is involved in the formation of membraneless
organelles (MLOs) associated with RNA processing. The RNA-binding protein TDP-43 is …
organelles (MLOs) associated with RNA processing. The RNA-binding protein TDP-43 is …
Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA
The nucleolus is a membrane-less organelle formed through liquid-liquid phase separation
of its components from the surrounding nucleoplasm. Here, we show that nucleophosmin …
of its components from the surrounding nucleoplasm. Here, we show that nucleophosmin …
[图书][B] Nuclear spin relaxation in liquids: theory, experiments, and applications
J Kowalewski, L Maler - 2017 - taylorfrancis.com
Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …
of the rich data it produces, and some of the most valuable data come from studies of …
Chemical exchange in biomacromolecules: past, present, and future
AG Palmer III - Journal of magnetic resonance, 2014 - Elsevier
The perspective reviews quantitative investigations of chemical exchange phenomena in
proteins and other biological macromolecules using NMR spectroscopy, particularly …
proteins and other biological macromolecules using NMR spectroscopy, particularly …
Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
VA Jarymowycz, MJ Stone - Chemical reviews, 2006 - ACS Publications
Over the past 15 years there has been an explosion of research on the dynamical properties
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …
Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy
AG Palmer, F Massi - Chemical reviews, 2006 - ACS Publications
Time-dependent dynamical properties of molecules can be quantified with atomic resolution
by using solution-state NMR spectroscopy. A variety of NMR observables, including scalar …
by using solution-state NMR spectroscopy. A variety of NMR observables, including scalar …
NMR probes of molecular dynamics: overview and comparison with other techniques
AG Palmer III - Annual review of biophysics and biomolecular …, 2001 - annualreviews.org
▪ Abstract NMR spin relaxation spectroscopy is a powerful approach for characterizing
intramolecular and overall rotational motions in proteins. This review describes experimental …
intramolecular and overall rotational motions in proteins. This review describes experimental …
The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
The static magnetic field dependence of chemical exchange linebroadening in NMR
spectroscopy is investigated theoretically and experimentally. Two-site exchange (A⇆ B) is …
spectroscopy is investigated theoretically and experimentally. Two-site exchange (A⇆ B) is …