Positively charged residues, the helical conformation and the structural flexibility of the leader sequence of pALDH are important for recognition by hTom20

FEBS Letters

Volumn 461, Issue 1-2, 1999, Pages 9-12

  Schleiff, E ^a   Heard, T S ^b   Weiner, H ^b  

^a MCGILL UNIVERSITY   (Canada)

^b PURDUE UNIVERSITY   (United States)

Author keywords

Mitochondrial outer membrane; pALDH; Protein translocation Tom20

Indexed keywords

MEMBRANE RECEPTOR; PROTEIN PRECURSOR; SIGNAL PEPTIDE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; HUMAN; MITOCHONDRIAL MEMBRANE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

5' UNTRANSLATED REGIONS; ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; GLUTATHIONE TRANSFERASE; HYDROGEN-ION CONCENTRATION; LIPOSOMES; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION;

EID: 0032704556     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)01415-5     Document Type: Article

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