NMR of plant proteins

Kaas, Quentin and Craik, David J. (2013) NMR of plant proteins. Progress in Nuclear Magnetic Resonance Spectroscopy, 71 1-34. doi:10.1016/j.pnmrs.2013.01.003

Author Kaas, Quentin
Craik, David J.
Title NMR of plant proteins
Journal name Progress in Nuclear Magnetic Resonance Spectroscopy   Check publisher's open access policy
ISSN 0079-6565
Publication date 2013-05-01
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.pnmrs.2013.01.003
Volume 71
Start page 1
End page 34
Total pages 34
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted abstract
A study was conducted to demonstrate the use of NMR as a as a tool to determine the structures, folding behavior, dynamics, and interactions of plant proteins. Investigations revealed that one-dimensional (1D) spectra were useful for rapid characterization of the folding or structure of smaller proteins. Correct folding was associated with sharp spectral lines and good dispersion of the amide signals or the observation of some upfield-shifted methyl groups. Upfield or down field dispersion of the α-H shifts provided a measure of helical or β-sheet secondary structure. A quick measure of the folding of proteins was also obtained from the pattern of chemical shifts in two-dimensional (2D) HSQC spectra for larger proteins. This was conveniently done with 15N-labeled samples, but the sensitivity of modern instruments equipped with cryo-probes allowed 2D HSQC spectra to be recorded for natural abundance samples.
Keyword Conformation
Protein characterization
Protein interactions
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
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