The Chemistry of Phospholipid Binding by the Saccharomyces cerevisiae Phosphatidylinositol Transfer Protein Sec14p as Determined by EPR Spectroscopy
Smirnova, T. I., Chadwick, T. G., MacArthur, R., Poluektov, O., Song, L., Ryan, M. M., … Bankaitis, V. A. (2006, September 23). Journal of Biological Chemistry, Vol. 281, pp. 34897–34908.
MeSH headings : Binding Sites; Gene Expression Regulation; Models, Molecular; Molecular Structure; Phosphatidylcholines / chemistry; Phosphatidylcholines / metabolism; Phospholipid Transfer Proteins / chemistry; Phospholipid Transfer Proteins / metabolism; Phospholipids / chemistry; Phospholipids / metabolism; Protein Binding; Saccharomyces cerevisiae / metabolism; Saccharomyces cerevisiae Proteins / chemistry; Saccharomyces cerevisiae Proteins / metabolism; Spectrometry, Mass, Electrospray Ionization / methods
topics (OpenAlex): Electron Spin Resonance Studies; Photosynthetic Processes and Mechanisms; Insect and Pesticide Research
TL;DR:
The application of EPR spectroscopy is described to probe the local dynamics and the electrostatic microenvironment of phosphatidylcholine bound by Sec14p in a soluble protein-PtdCho complex and suggests a headgroup-out orientation ofSec14p-bound PtdCho.
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