An NMR study of the N-terminal domain of wild-type hERG and a T65P trafficking deficient hERG mutant

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 8, 2011, Pages 2557-2565

  Gayen, Shovanlal ^a   Li, Qingxin ^a,b   Chen, Angela Shuyi ^a   Nguyen, Thi Hanh Thuy ^a   Huang, Qiwei ^a   Hill, Jeffrey ^a   Kang, Congbao ^a  

^a Agency for Science   (Singapore)

^b INSTITUTE OF BIOENGINEERING AND NANOTECHNOLOGY   (Singapore)

Author keywords

Amphipathic helix; HERG; NMR spectroscopy; PAS domain; Potassium channel; Thermal stability

Indexed keywords

BACTERIAL PROTEIN; POTASSIUM CHANNEL; POTASSIUM CHANNEL HERG; T65P PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONTROLLED STUDY; ESCHERICHIA COLI; GEL FILTRATION; GENETIC ANALYSIS; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HIGH TEMPERATURE; HUMAN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ETHER-A-GO-GO POTASSIUM CHANNELS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE;

EID: 79960103751     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23089     Document Type: Article

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