The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes

Biochemistry

Volumn 43, Issue 38, 2004, Pages 11992-11997

  Knapp, Stefan ^a   Müller, Susanne ^b   Digilio, Giuseppe ^c   Bonaldi, Tiziana ^b   Bianchi, Marco E ^d   Musco, Giovanna ^e  

^a PFIZER INC   (United States)

^b SAN RAFFAELE HOSPITAL   (Italy)

^c Bioindustry Park del Canavese   (Italy)

^d VITA SALUTE SAN RAFFAELE UNIVERSITY   (Italy)

^e DULBECCO TELETHON INSTITUTE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; DATA REDUCTION; DISSOCIATION; DNA; NUCLEAR MAGNETIC RESONANCE; SPECTROSCOPIC ANALYSIS; THERMODYNAMIC STABILITY;

BINDING PROPERTIES; FLEXIBLE SEGMENTS; PEPTIDES;

PROTEINS;

CHROMOSOME PROTEIN; HIGH MOBILITY GROUP B1 PROTEIN;

ARTICLE; BINDING AFFINITY; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; HIGH MOBILITY GROUP BOX DOMAIN; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; THERMOSTABILITY;

EID: 4644335083     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049364k     Document Type: Article

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