Activity-dependent neurotrophic factor, ADNF, determines the structure characteristicsof Colivelin, a fusion protein of ADNF9 and Humanin analog

Journal of Peptide Science

Volumn 14, Issue 5, 2008, Pages 631-636

  Arakawa, Tsutomu ^a   Niikura, Takako ^b,d   Arisaka, Fumio ^c   Kita, Yoshiko ^b  

^a ALLIANCE PROTEIN LABORATORIES   (United States)

^b KEIO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c Tokyo Institute of Technology ^*  (Japan)

^d GEORGETOWN UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

ADNF; Circular dichroism; Colivelin; Fusion peptide; Humanin; Sedimentation analysis

Indexed keywords

ACTIVITY DEPENDENT NEUROTROPHIC FACTOR; ACTIVITY DEPENDENT NEUROTROPHIC FACTOR 9 HUMANIN FUSION PROTEIN; COLIVELIN; HYBRID PROTEIN; MONOMER; NEUROTROPHIC FACTOR; PHOSPHATE BUFFERED SALINE; WATER;

AMINO ACID COMPOSITION; ARTICLE; CIRCULAR DICHROISM; NEUROPROTECTION; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEDIMENTATION RATE; STRUCTURE ANALYSIS; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; DRUG STABILITY; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MULTIPROTEIN COMPLEXES; NERVE TISSUE PROTEINS; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; ULTRACENTRIFUGATION;

EID: 44349146630     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.959     Document Type: Article

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