한국자기공명학회논문지 (Journal of the Korean Magnetic Resonance Society)

한국자기공명학회 (Korean Magnetic Resonance Society)
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Syndecan-4 cytoplasmic domain could disturb the multilamellar vesicle

  • Kim, Suhk-Mann (Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University)
  • 발행 : 2009.06.20
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초록

Syndecan-4 cytoplasmic domain was tested to confirm the interactions with the bilayer membrane using $^{31}P$ solid-state NMR measurements. Syndecan-4 was known as a coreceptor with integrins in the cell adhesion. The syndecan-4 V region is not understood of its functional roles and tested its ability of the interaction with multilamellar vesicles. The $^{31}P$ powder pattern was dramatically changed and showed isotropic peak which imply the bilayer membrane changed its topology to the micelle-like structure. Especially, phosphatidylcholine membrane was affected this effect more than phosphatidylethanolamine membrane.

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참고문헌

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피인용 문헌

  1. Optimization of Expression, Purification, and NMR Measurement for Structural Studies of Syndecan-4 Transmembrane Region vol.15, pp.1, 2011, https://doi.org/10.6564/JKMRS.2011.15.1.025
  2. Applications of NMR spectroscopy based metabolomics: a review vol.17, pp.1, 2013, https://doi.org/10.6564/JKMRS.2013.17.1.001