The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains

BMC Biochemistry

Volumn 10, Issue 1, 2009, Pages

  Richardson, Lynn Gl ^a,b,c   Jelokhani Niaraki, Masoud ^a   Smith, Matthew D ^a  

^a WILFRID LAURIER UNIVERSITY   (Canada)

^b UNIVERSITY OF WATERLOO   (Canada)

^c UNIVERSITY OF GUELPH   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN PRECURSOR; PROTEIN TOC 132; PROTEIN TOC 159; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ARABIDOPSIS PROTEIN; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; TOC159 PROTEIN, ARABIDOPSIS; TRIFLUOROETHANOL;

ARABIDOPSIS; ARTICLE; CHLOROPLAST; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PHYSICAL CHEMISTRY; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY; CHEMISTRY; GENETICS; METABOLISM; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

ARABIDOPSIS;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CHLOROPLASTS; CIRCULAR DICHROISM; GTP PHOSPHOHYDROLASES; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TEMPERATURE; TRIFLUOROETHANOL;

EID: 74949125046     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-10-35     Document Type: Article

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