Structural study of caveolin-1 intramembrane domain by circular dichroism and nuclear magnetic resonance.

@article{Yang2015StructuralSO,
  title={Structural study of caveolin-1 intramembrane domain by circular dichroism and nuclear magnetic resonance.},
  author={Guanhua Yang and Zhe Dong and Haoran Xu and Chunyu Wang and Yao Amber Li and Zhengqiang Li and Fei Li},
  journal={Biopolymers},
  year={2015},
  volume={104 1},
  pages={
          11-20
        }
}
Caveolin-1 is a main structural component of caveolae and essential for the invagination of caveolae by forming a hairpin-shaped structure in the membrane-inserting domain (residues, 102-122). In this article, we determined the tertiary structures of the peptides comprising residues 93-126 and 101-126 of caveolin-1 in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) aqueous solution and sodium dodecyl sulfate (SDS) micelles, respectively, by nuclear magnetic resonance (NMR) study. The self-association… CONTINUE READING
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References

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Biopolymers (Peptide Science

  • Yang
  • Biochemistry
  • 2012
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