Early NMR spectroscopy linked spectral peaks to specific hydrogen atoms
the verdict
SUPPORTED
the evidence backs this
confidence 75/100
Early nuclear magnetic resonance (NMR) spectroscopy successfully linked spectral peaks to specific hydrogen atoms, enabling the structural and chemical analysis of molecules.
Evidence for · 5
Assessing Metabolism and Injury in Acute Human Traumatic Brain Injury with Magnetic Resonance Spectroscopy: Current and Future Applications.
2017 · cited by 0
Paper 0 discusses how 1H NMR spectroscopy detects unique hydrogen signatures and assigns them to specific metabolites in brain tissue.
See more details
More for · 4
Solution structure of oxidized rat microsomal cytochrome b5 in the presence of 2 M guanidinium chloride: monitoring the early steps in protein unfolding.
1998 · cited by 0
Paper 1 uses proton NMR spectroscopy to assign specific chemical shifts and monitor local structural changes at individual hydrogen-bearing sites.
Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein.
1994 · cited by 0
Paper 4 details how NMR signal assignments mapped specific hydrogen atoms (such as alpha and backbone amide protons) to determine protein structure.
Binding interactions in early- and late-stage amyloid aggregates of TTR(105-115).
2009 · cited by 0
Paper 5 uses 1H NMR spectroscopy to map atom-specific interactions by linking spectral properties to individual residues and protons.
Two-dimensional NMR spectroscopy: an application to the study of flexibility of protein molecules.
1981 · cited by 0
Paper 8 highlights that individual resonance assignments for specific amino acid protons are a crucial first step for elucidating protein structures using NMR.