Nuclear magnetic resonance analysis of protein–DNA interactions

S Campagne, V Gervais… - Journal of the Royal …, 2011 - royalsocietypublishing.org
Recent methodological and instrumental advances in solution-state nuclear magnetic
resonance have opened up the way to investigating challenging problems in structural …

Structural NMR of protein oligomers using hybrid methods

X Wang, HW Lee, Y Liu, JH Prestegard - Journal of structural biology, 2011 - Elsevier
Solving structures of native oligomeric protein complexes using traditional high-resolution
NMR techniques remains challenging. However, increased utilization of computational …

Nonthermal excitation effects mediated by sub-terahertz radiation on hydrogen exchange in ubiquitin

Y Tokunaga, M Tanaka, H Iida, M Kinoshita, Y Tojima… - Biophysical …, 2021 - cell.com
Water dynamics in the hydration layers of biomolecules play crucial roles in a wide range of
biological functions. A hydrated protein contains multiple components of diffusional and …

Theoretical analyses of the transferred cross-saturation method

M Matsumoto, T Ueda, I Shimada - Journal of Magnetic Resonance, 2010 - Elsevier
Large molecules, such as membrane proteins, play crucial roles in various biologically
important events. We have developed the transferred cross-saturation (TCS) method, which …

NMR spectroscopy for studying interactions of bioactive molecules

P Novak, T Jednačak - … -chemical methods in drug discovery and …, 2012 - books.google.com
One of the main prerequisites for the successful design of bioactive molecules and drugs is
the elucidation of the three-dimensional structure of small molecular ligands, receptors and …

Development of a method for reconstruction of crowded NMR spectra from undersampled time-domain data

T Ueda, C Yoshiura, M Matsumoto, Y Kofuku… - Journal of Biomolecular …, 2015 - Springer
NMR is a unique methodology for obtaining information about the conformational dynamics
of proteins in heterogeneous biomolecular systems. In various NMR methods, such as …

Rapid identification of protein–protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR …

Y Kodama, ML Reese, N Shimba, K Ono… - Journal of Structural …, 2011 - Elsevier
Protein–protein interactions are necessary for various cellular processes, and therefore,
information related to protein–protein interactions and structural information of complexes is …

Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique

DX Hao, C Sandström, YD Huang, L Kenne, JC Janson… - Soft Matter, 2012 - pubs.rsc.org
Protein–ligand interactions on liquid–solid interfaces governed the design of functional
biomaterials. However, accurate residue details of ligand induced protein binding and …

[HTML][HTML] ACCEPT-NMR: A New Tool for the Analysis of Crystal Contacts and Their Links to NMR Chemical Shift Perturbations

IV Sergeyev, AE McDermott - 2013 - scirp.org
We have developed an open-source cross-platform software toolkit entitled ACCEPT-NMR
(Automated Crystal Contact Extrapolation/Prediction Toolkit for NMR) as a helpful tool to …

Nuclear Magnetic Resonance Spectroscopy: A Useful Analytical Tool to Determine Different Parameters in Food Applications

M Azam, M Saeed, MH Ahmad - Advances in Noninvasive Food …, 2019 - taylorfrancis.com
Different instruments are being used to determine the qualitative and quantitative
parameters in various food applications, but rapid and noninvasive analytical methodologies …