The intermembrane space domain of Tim23 is intrinsically disordered with a distinct binding region for presequences

Protein Science

Volumn 19, Issue 11, 2010, Pages 2045-2054

  De La Cruz, Laura ^a   Bajaj, Rakhi ^a   Becker, Stefan ^a   Zweckstetter, Markus ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Mitochondria; NMR spectroscopy; Protein import; Tim23

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; MONOMER; PROTEIN TIM23; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; MEMBRANE TRANSPORT; MITOCHONDRIAL MEMBRANE; NUCLEAR MAGNETIC RESONANCE; OUTER MEMBRANE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN TARGETING; TITRIMETRY;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE ANNOTATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 78349234993     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.482     Document Type: Article

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