NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker

Biochemical and Biophysical Research Communications

Volumn 403, Issue 1, 2010, Pages 126-132

  Li, Qingxin ^a,b   Gayen, Shovanlal ^a   Chen, Angela Shuyi ^a   Huang, Qiwei ^a   Raida, Manfred ^a   Kang, CongBao ^a  

^a Agency for Science   (Singapore)

^b INSTITUTE OF BIOENGINEERING AND NANOTECHNOLOGY   (Singapore)

Author keywords

Amphipathic helix; CD; HERG; NMR spectroscopy; PAS domain; Potassium channel

Indexed keywords

POTASSIUM CHANNEL HERG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CIRCULAR DICHROISM; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; GENE OVEREXPRESSION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; ULTRAVIOLET RADIATION;

ETHER-A-GO-GO POTASSIUM CHANNELS; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

ESCHERICHIA COLI;

EID: 78649713129     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.10.132     Document Type: Article

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