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Amphipols: Polymers that Keep Membrane Proteins Soluble in Aqueous Solutions
Amphipols are a new class of surfactants that make it possible to handle membrane proteins in detergent-free aqueous solution as though they were soluble proteins. The strongly hydrophilic backbone of these polymers is grafted with hydrophobic chains, making them amphiphilic. Amphipols are able to s...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS 1996-12, Vol.93 (26), p.15047-15050 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c523t-2854eec1785691eaed388032d10440de8a4df9fa9925bc5742d9207970b0530e3 |
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| cites | cdi_FETCH-LOGICAL-c523t-2854eec1785691eaed388032d10440de8a4df9fa9925bc5742d9207970b0530e3 |
| container_end_page | 15050 |
| container_issue | 26 |
| container_start_page | 15047 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 93 |
| creator | Tribet, Christophe Audebert, Roland Popot, Jean-Luc |
| description | Amphipols are a new class of surfactants that make it possible to handle membrane proteins in detergent-free aqueous solution as though they were soluble proteins. The strongly hydrophilic backbone of these polymers is grafted with hydrophobic chains, making them amphiphilic. Amphipols are able to stabilize in aqueous solution under their native state four well-characterized integral membrane proteins: (i) bacteriorhodopsin, (ii) a bacterial photosynthetic reaction center, (iii) cytochrome b6f, and (iv) matrix porin. |
| doi_str_mv | 10.1073/pnas.93.26.15047 |
| format | article |
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Audebert, Roland ; Popot, Jean-Luc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-2854eec1785691eaed388032d10440de8a4df9fa9925bc5742d9207970b0530e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Aqueous solutions</topic><topic>Bacterial Outer Membrane Proteins - chemistry</topic><topic>Bacterial Outer Membrane Proteins - isolation & purification</topic><topic>Bacteriorhodopsins</topic><topic>Bacteriorhodopsins - chemistry</topic><topic>Bacteriorhodopsins - isolation & purification</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chlamydomonas reinhardtii - metabolism</topic><topic>Cytochrome b Group - chemistry</topic><topic>Cytochrome b Group - isolation & purification</topic><topic>Cytochrome b6f Complex</topic><topic>Cytochromes</topic><topic>Detergents</topic><topic>Drug Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Halobacterium - metabolism</topic><topic>Kinetics</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membranes</topic><topic>Models, Structural</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Polymers</topic><topic>Porins</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Rhodobacter sphaeroides</topic><topic>Solubility</topic><topic>Surface-Active Agents - chemical synthesis</topic><topic>Time Factors</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tribet, Christophe</creatorcontrib><creatorcontrib>Audebert, Roland</creatorcontrib><creatorcontrib>Popot, Jean-Luc</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tribet, Christophe</au><au>Audebert, Roland</au><au>Popot, Jean-Luc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amphipols: Polymers that Keep Membrane Proteins Soluble in Aqueous Solutions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-12-24</date><risdate>1996</risdate><volume>93</volume><issue>26</issue><spage>15047</spage><epage>15050</epage><pages>15047-15050</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Amphipols are a new class of surfactants that make it possible to handle membrane proteins in detergent-free aqueous solution as though they were soluble proteins. 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| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1996-12, Vol.93 (26), p.15047-15050 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_93_26_15047 |
| source | PubMed Central(OpenAccess); JSTOR Archival Journals and Primary Sources Collection |
| subjects | Animals Aqueous solutions Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - isolation & purification Bacteriorhodopsins Bacteriorhodopsins - chemistry Bacteriorhodopsins - isolation & purification Biochemistry Biological Sciences Chlamydomonas reinhardtii Chlamydomonas reinhardtii - metabolism Cytochrome b Group - chemistry Cytochrome b Group - isolation & purification Cytochrome b6f Complex Cytochromes Detergents Drug Stability Escherichia coli Escherichia coli - metabolism Halobacterium - metabolism Kinetics Membrane proteins Membrane Proteins - chemistry Membranes Models, Structural Molecules Monomers Polymers Porins Protein Structure, Secondary Proteins Rhodobacter sphaeroides Solubility Surface-Active Agents - chemical synthesis Time Factors Water |
| title | Amphipols: Polymers that Keep Membrane Proteins Soluble in Aqueous Solutions |
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