Results 231 to 240 of about 4,121,048 (281)
Clathrate hydrate crystallization
Abstract Clathrate hydrate crystallization has been an area of interest to chemical engineers from the point of view of crystal structure, thermophysical properties, phase equilibria, kinetics, industrial applications, and environmental (climate change) implications.
Peter Englezos
wiley +1 more source
Proton NMR Revisited: Negative Time Reconstruction Transforms Pure Shift and 2D J‐Spectroscopy
Negative time signal reconstruction of NMR data acquired in a modified spin echo distills complex spectra into enhanced resolution multiplets and a pure shift spectrum. Experiments typically take only 2 min, with sensitivity an order of magnitude better than current methods, making routine acquisition of pure shift NMR spectra practical. Proton nuclear
Gareth A. Morris +4 more
wiley +1 more source
ABSTRACT Alzheimer's disease (AD) is a progressive neurodegenerative disease, and cholinergic dysfunction is considered one of the fundamental pathological factors of this disease. Guided by the clinically used acetylcholinesterase (AChE) inhibitor donepezil, we explored trimetazidine dihydrochloride as an accessible starting scaffold to generate ...
Muhammed Oğuzhan Doğan +6 more
wiley +1 more source
Hydroxamic Acids as HDAC Inhibitor Drug Leads for Malaria
ABSTRACT Malaria is a global health threat, with an estimated 282 million cases and 610,000 malaria‐associated deaths reported in 2024. Most mortality is due to infection by Plasmodium falciparum parasites, with the highest burden occurring in Sub‐Saharan Africa.
Wisam A. Dawood +7 more
wiley +1 more source
Lipidic Phase Membrane Protein Serial Femtosecond Crystallography [PDF]
X-ray free electron laser (X-FEL)-based serial femtosecond crystallography is an emerging method with potential to rapidly advance the challenging field of membrane protein structural biology.
Sascha Epp +2 more
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Hydration in protein crystallography
Progress in Biophysics and Molecular Biology, 1995Water in close proximity to the protein surface is fundamental to protein folding, stability, recognition and activity. Protein structures studied by diffraction methods show ordered water molecules around some charged, polar, and non-polar (hydrophobic) amino acids, although the later are only observed when they are at the interface between symmetry ...
B P, Schoenborn, A, Garcia, R, Knott
openaire +2 more sources
Racemic Protein Crystallography
Annual Review of Biophysics, 2012Although natural proteins are chiral and are all of one “handedness,” their mirror image forms can be prepared by chemical synthesis. This opens up new opportunities for protein crystallography. A racemic mixture of the enantiomeric forms of a protein molecule can crystallize in ways that natural proteins cannot.
Todd O, Yeates, Stephen B H, Kent
openaire +2 more sources

