NMR of proteins and nucleic acids
By Geoffrey I. Webb, Stephen Matthews. 2005
261 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b3d464b170d47c36537b762e6858f1b36419954e
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In Molecular Biology
Citations in the corpus
- 3D structure of Alzheimer's amyloid-β(1–42) fibrils (2005, unknown): “The calculation of protein structures from NMR-derived UPLs is a well established technique (25).”
- Coherent two-dimensional optical spectroscopy. (2008, methodology): “In NMR spectroscopy, such efforts led to developing a variety of 2D NMR techniques such as NOESY (Nuclear Overhauser Enhancement Spectroscopy) and COSY (correlation spectroscopy) methods among many others, and they have been extensively used to study structural and dynamical properties of proteins i”
- Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. (2004, unknown): “Two-dimensional NOESY, total correlation spectroscopy (TOCSY) (21), and 15N-filtered NOESY and TOCSY spectra were acquired as described (22).”
- Solution NMR-derived global fold of a monomeric 82-kDa enzyme. (2005, unknown): “N spectroscopy is one of the most powerful techniques for the study of protein structure and dynamics (1).”