Shape Changes of Giant Unilamellar Vesicles of Phosphatidylcholine Induced by a De Novo Designed Peptide Interacting with Their Membrane Interface-Reference-Cited by-同舟云学术

Shape Changes of Giant Unilamellar Vesicles of Phosphatidylcholine Induced by a De Novo Designed Peptide Interacting with Their Membrane Interface

Published:2002-11-13 Issue:25 Volume:18 Page:9638-9641
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Yamashita Yuko¹,Masum Shah Md.¹,Tanaka Tomoki¹,Yamazaki Masahito¹

Affiliation:

1. Department of Physics, Faculty of Science, Shizuoka University, Shizuoka, 422-8529, Japan, and Material Science, Graduate School of Science and Engineering, Shizuoka University, 422-8529, Japan

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la0265124

Reference15 articles.

1. Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin

2. Membrane Binding of Myristylated Peptides Corresponding to the NH2 Terminus of Src

3. Intermembrane distance in multilamellar vesicles of phosphatidylcholine depends on the interaction free energy between solvents and the hydrophilic segments of the membrane surface

4. Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure

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