NMR spectroscopic elucidation of the B-Z transition of a DNA double helix induced by the Zα domain of human ADAR1

Journal of the American Chemical Society

Volumn 131, Issue 32, 2009, Pages 11485-11491

  Kang, Young Min ^a   Bang, Jongchul ^b   Lee, Eun Hae ^a   Ahn, Hee Chul ^c   Seo, Yeo Jin ^a   Kyeong, Kyu Kim ^d   Kim, Yang Gyun ^e   Choi, Byong Seok ^b   Lee, Joon Hwa ^a  

^a Gyeongsang National University   (South Korea)

^b Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^c Korea Institute of Science and Technology   (South Korea)

^d Sungkyunkwan University School of Medicine   (South Korea)

^e Sungkyunkwan University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

2-FOLD SYMMETRY; BINDING AFFINITIES; CIRCULAR DICHROISM; COCRYSTAL STRUCTURE; DNA BINDING DOMAIN; DNA COMPLEX; DNA DOUBLE HELICES; DOUBLE STRANDED DNA; DOUBLE-STRANDED RNA; HELICAL AXIS; INOSINE; INTERMEDIATE STATE; MOLAR RATIO; PRE-MRNA; RNA EDITING; SPECTROSCOPIC ELUCIDATION; TRANSITION MECHANISM;

BINDING ENERGY; DICHROISM; DNA; DYES; GENES; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RNA;

NUCLEIC ACIDS;

CYSTEINYLGLYCYLCYSTEINYLGLYCYLCYSTEINYLGLYCINE; DEAMINASE; DNA B; DNA Z; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; DOUBLE STRANDED RNA DEAMINASE 1; GLYCINE; MONOMER; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; DNA HELIX; DNA SEQUENCE; HUMAN; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHASE TRANSITION; PROTEIN CONFORMATION; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; RNA STRUCTURE;

ADENOSINE DEAMINASE; BINDING SITES; DNA; DNA, Z-FORM; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

EID: 68849083095     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja902654u     Document Type: Article

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