期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 84, 期 3, 页码 349-359出版社
WILEY
DOI: 10.1002/prot.24981
关键词
membrane-binding sites; liposome; molecular orientation; protein-membrane interaction; secondary structures; synchrotron-radiation circular dichroism
资金
- Ministry of Education, Science, Sports, and Culture of Japan [22870021]
- Grants-in-Aid for Scientific Research [22870021, 15K07028] Funding Source: KAKEN
Knowledge of the conformations of a water-soluble protein bound to a membrane is important for understanding the membrane-interaction mechanisms and the membrane-mediated functions of the protein. In this study we applied vacuum-ultraviolet circular-dichroism (VUVCD) and linear-dichroism (LD) spectroscopy to analyze the conformations of alactalbumin (LA), thioredoxin (Trx), and beta-lactoglobulin (LG) bound to phosphatidylglycerol liposomes. The VUVCD analysis coupled with a neural-network analysis showed that these three proteins have characteristic helix-rich conformations involving several helical segments, of which two amphiphilic or hydrophobic segments take part in interactions with the liposome. The LD analysis predicted the average orientations of these helix segments on the liposome: two amphiphilic helices parallel to the liposome surface for LA, two hydrophobic helices perpendicular to the liposome surface for Trx, and a hydrophobic helix perpendicular to and an amphiphilic helix parallel to the liposome surface for LG. This sequence-level information about the secondary structures and orientations was used to formulate interaction models of the three proteins at the membrane surface. This study demonstrates the validity of a combination of VUVCD and LD spectroscopy in conformational analyses of membrane-binding proteins, which are difficult targets for X-ray crystallography and nuclear magnetic resonance spectroscopy.
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