The role of conserved histidines in the structure and stability of human papillomavirus type 16 E2 DNA-binding domain

Biochemistry

Volumn 46, Issue 5, 2007, Pages 1402-1411

  Bose, Kakoli ^a   Yoder, Nicholas C ^b   Kumar, Krishna ^b   Baleja, James D ^a  

^a TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b TUFTS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIODIVERSITY; DIMERS; DNA SEQUENCES; MUTAGENS; PH EFFECTS; VIRUSES;

DNA-BINDING DOMAIN (DBD); HUMAN PAPILLOMAVIRUS; NEUTRAL ALANINES; TERTIARY STRUCTURES;

PROTEINS;

ALANINE; GLYCOPROTEIN E2; HISTIDINE; MUTANT PROTEIN;

ACIDIFICATION; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIMERIZATION; DNA BINDING MOTIF; HUMAN PAPILLOMAVIRUS TYPE 16; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; VIRUS REPLICATION; VIRUS TRANSCRIPTION;

AMINO ACID SUBSTITUTION; BINDING SITES; CONSERVED SEQUENCE; DIMERIZATION; DNA-BINDING PROTEINS; HISTIDINE; HUMAN PAPILLOMAVIRUS 16; HUMANS; HYDROGEN-ION CONCENTRATION; ONCOGENE PROTEINS, VIRAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING;

HUMAN PAPILLOMAVIRUS TYPE 16; PAPILLOMAVIRIDAE;

EID: 33846804381     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0611255     Document Type: Article

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