Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding

Biochemistry

Volumn 44, Issue 22, 2005, Pages 8117-8125

  Zhang, Xuecheng ^a   Xu, Yingqi ^a   Zhang, Jiahai ^a   Wu, Jihui ^a   Shi, Yunyu ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CONFORMATIONS; FUNCTIONS; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS; POLYPEPTIDES; PROTEINS; PROTONS;

ACID-UNFOLDED STATE; CHEMICAL SHIFT; PROTEIN FOLDING; SPECTRAL DENSITY FUNCTION;

AMINO ACIDS;

ACID; AMIDE; HUMAN UPSTREAM BINDING FACTOR; POLYPEPTIDE; PROTON; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

ARTICLE; DENSITY; HIGH MOBILITY GROUP BOX DOMAIN; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE;

AMINO ACID SEQUENCE; CARBON ISOTOPES; HMG-BOX DOMAINS; HMGB1 PROTEIN; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; POL1 TRANSCRIPTION INITIATION COMPLEX PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTONS; TEMPERATURE; THERMODYNAMICS;

EID: 20144365610     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0501939     Document Type: Article

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