Results 11 to 20 of about 49,014 (224)
Frontiers in Molecular Biosciences, 2021 The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects.
Nadide Altincekic +178 more
doaj +1 more source
ssNMRlib: a comprehensive library and tool box for acquisition of solid-state nuclear magnetic resonance experiments on Bruker spectrometers [PDF]
Magnetic Resonance, 2020 We introduce ssNMRlib, a comprehensive suite of pulse sequences and jython scripts for user-friendly solid-state nuclear magnetic resonance (NMR) data acquisition, parameter optimization and storage on Bruker spectrometers.
A. Vallet +3 more
doaj +1 more source
Frontiers in Chemistry, 2020 HMGB1 is a key molecule that both triggers and sustains inflammation following infection or injury, and is involved in a large number of pathologies, including cancer.
Federica De Leo +6 more
doaj +1 more source
Recent Advances in Solid-State Nuclear Magnetic Resonance Techniques to Quantify Biomolecular Dynamics [PDF]
Analytical Chemistry, 2013 The emergence of solid-state NMR (SSNMR) techniques over the last decade has greatly expanded the range of accessible biomolecules amenable to structural study.1-2 These methods were developed and first applied to a variety of microcrystalline model proteins including BPTI,3 SH3,4-5 ubiquitin,6-7 kaliotoxin,8 and GB1.9-11 These studies demonstrated ...
Eric D, Watt, Chad M, Rienstra
openaire +2 more sources
Biophysics Reports, 2021 The assembly of biomolecular condensates is driven by liquid-liquid phase separation. To understand the structure and functions of these condensates, it is essential to characterize the underlying driving forces, e.g., protein-protein and protein-RNA interactions.
Zhang, Hanyu +9 more
openaire +2 more sources
Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density [PDF]
Journal of Biomolecular NMR, 2010 Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation.
Ferrage, Fabien +3 more
openaire +2 more sources
ACS Chemical Biology, 2023 Nuclear magnetic resonance (NMR) studies of large biomolecular machines and highly repetitive proteins remain challenging due to the difficulty of assigning frequencies to individual nuclei. Here, we present an efficient strategy to address this challenge by engineering a Pyrococcus horikoshii tRNA/alanyl-tRNA synthetase pair that enables the ...
Elena-Real, Carlos +8 more
openaire +4 more sources
Utility of methyl side chain probes for solution NMR studies of large proteins
Journal of Magnetic Resonance Open, 2023 Selective isotopic labeling of methyl side chain groups in proteins and other biomolecules, combined with advances in perdeuteration, new pulse sequences, and high field spectrometers with cryogenic probes, has revolutionized the field of solution ...
Andrew C. McShan
doaj +1 more source
Effects of NMR spectral resolution on protein structure calculation [PDF]
, 2013 Adequate digital resolution and signal sensitivity are two critical factors for protein structure determinations by solution NMR spectroscopy. The prime objective for obtaining high digital resolution is to resolve peak overlap, especially in NOESY ...
Güntert, Peter +3 more
core +9 more sources
BMC Chemistry, 2022 Nuclear Magnetic Resonance (NMR) spectroscopy is an indispensable technique for the structure elucidation of molecules and determination of their characteristic interactions.
Ali Yassin +4 more
doaj +1 more source