[HTML][HTML] Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems

S Schütz, R Sprangers - Progress in nuclear magnetic resonance …, 2020 - Elsevier
A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …

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 …

Visualizing transient dark states by NMR spectroscopy

NJ Anthis, GM Clore - Quarterly Reviews of Biophysics, 2015 - cambridge.org
Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …

Solution NMR spectroscopy for the study of enzyme allostery

GP Lisi, JP Loria - Chemical reviews, 2016 - ACS Publications
Allostery is a ubiquitous biological regulatory process in which distant binding sites within a
protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions …

Detection of allosteric signal transmission by information-theoretic analysis of protein dynamics

A Pandini, A Fornili, F Fraternali, J Kleinjung - Biophysical Journal, 2012 - cell.com
Methods First, MD ensembles are mapped onto a canonical set of representative fragments,
ie a set of discrete 4-residue states [3]. By this map**, the contribution of rigid fragment …

[BOK][B] Einführung in die Physik und Chemie der Grenzflächen und Kolloide

JG Lauth, J Kowalczyk - 2016 - Springer
Die Chemie und Physik der Grenzflächen und Kolloide gehört klassisch in das Gebiet der
Festkörperphysik einerseits und der Thermodynamik andererseits. Erst seit Ende der 1990er …

A suite of 19F based relaxation dispersion experiments to assess biomolecular motions

JH Overbeck, W Kremer, R Sprangers - Journal of biomolecular NMR, 2020 - Springer
Proteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of
conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to …

[HTML][HTML] Automated assignment of methyl NMR spectra from large proteins

I Pritišanac, TR Alderson, P Güntert - Progress in nuclear magnetic …, 2020 - Elsevier
As structural biology trends towards larger and more complex biomolecular targets, a
detailed understanding of their interactions and underlying structures and dynamics is …

Excited states of nucleic acids probed by proton relaxation dispersion NMR spectroscopy

MA Juen, CH Wunderlich, F Nußbaumer… - Angewandte …, 2016 - Wiley Online Library
In this work an improved stable isotope labeling protocol for nucleic acids is introduced. The
novel building blocks eliminate/minimize homonuclear 13C and 1H scalar couplings thus …

Observation of sub-microsecond protein methyl-side chain dynamics by nanoparticle-assisted NMR spin relaxation

X **ang, AL Hansen, L Yu, G Jameson… - Journal of the …, 2021 - ACS Publications
Amino-acid side-chain properties in proteins are key determinants of protein function. NMR
spin relaxation of side chains is an important source of information about local protein …