Evidence that the translocon may function as a hydropathy partitioning filter

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 10, 2010, Pages 1995-1998

  Mulvihill, Cory M ^a,b   Deber, Charles M ^a,b  

^a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Cystic fibrosis transmembrane conductance Regulator (CFTR); Hydropathy; Membrane proteins; RP HPLC; Translocon

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; MEMBRANE PROTEIN; TRANSLOCON; TRANSMEMBRANE CONDUCTANCE REGULATOR; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; LIPID BILAYER; PEPTIDE;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; CONTROLLED STUDY; DNA HAIRPIN; DNA HELIX; GENE MUTATION; HYDROPHOBICITY; IN VIVO STUDY; LIPID BILAYER; MEMBRANE TRANSPORT; PHASE PARTITIONING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTON TRANSPORT; QUANTITATIVE ANALYSIS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SOLVATION; AMINO ACID SEQUENCE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MOLECULAR GENETICS; MUTATION; PROCEDURES; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HUMANS; HYDROPHOBICITY; LIPID BILAYERS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;

EID: 77955664628     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.07.007     Document Type: Article

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