Nonionic homopolymeric amphipols: Application to membrane protein folding, cell-free synthesis, and solution nuclear magnetic resonance

Biochemistry

Volumn 51, Issue 7, 2012, Pages 1416-1430

  Bazzacco, Paola ^a   Billon Denis, Emmanuelle ^a   Sharma, K Shivaji ^b,c   Catoire, Laurent J ^a   Mary, Sophie ^a   Le Bon, Christel ^a   Point, Elodie ^a   Banères, Jean Louis ^a   Durand, Grégory ^a,b   Zito, Francesca ^a   Pucci, Bernard ^a,b   Popot, Jean Luc ^a  

^a CNRS   (France)

^b UNIVERSITY OF AVIGNON   (France)

^c UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE PROTON; AMPHIPOL; BACTERIORHODOPSIN (BR); BIOPHYSICAL PROPERTIES; CELL-FREE; CHLAMYDOMONAS REINHARDTII; CYTOCHROME B; G PROTEIN COUPLED RECEPTORS; GHRELIN; HETERONUCLEAR SINGLE-QUANTUM COHERENCES; MEMBRANE PROTEINS; NATIVE STATE; NONIONIC; PHOTOCYCLES;

AMIDES; BIOLOGICAL MEMBRANES; ESCHERICHIA COLI; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; QUANTUM THEORY;

BIOSYNTHESIS;

AMIDE; BACTERIAL PROTEIN; BACTERIORHODOPSIN; BETA ARRESTIN 2; CYTOCHROME B6F; GHRELIN RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); MEMBRANE PROTEIN; MONOMER; NONIONIC AMPHIPOL; POLYMER; PROTEIN OMPX; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; CHLAMYDOMONAS REINHARDTII; COMPLEX FORMATION; CONTROLLED STUDY; ESCHERICHIA COLI; HALOBACTERIUM SALINARUM; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; SOLVENT EFFECT; SULFONATION; SYNTHESIS;

BACTERIORHODOPSINS; BUFFERS; CELL-FREE SYSTEM; CHLAMYDOMONAS REINHARDTII; CYTOCHROMES B6; ESCHERICHIA COLI; GHRELIN; GLYCOSYLATION; GTP-BINDING PROTEINS; HALOBACTERIUM SALINARUM; IONS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; POLYMERS; PROPYLAMINES; PROTEIN FOLDING; RECEPTORS, GHRELIN;

EID: 84857421428     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201862v     Document Type: Article

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