Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/102346
Title: 1H, 13C and 15N chemical shift assignments for the N-terminal PAS domain of the KCNH channel from Zebrafish
Authors: Kim, Young Mee
Li, Qingxin
Ng, Hui Qi
Yoon, Ho Sup
Kang, CongBao
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Voltage-gated potassium channel
NMR
Issue Date: 2013
Source: Kim, Y. M., Li, Q., Ng, H. Q., Yoon, H. S., & Kang, C. 1H, 13C and 15N chemical shift assignments for the N-terminal PAS domain of the KCNH channel from Zebrafish. Biomolecular NMR Assignments.
Series/Report no.: Biomolecular NMR Assignments
Abstract: The KCNH channels are voltage-gated potassium channels that play important roles in heart and nerve cells. The N-terminal region of the KCNH channel contains a Per-Arnt-Sim (PAS) domain which is important for the channel gating through interaction with other regions of the channel. To study the solution structure of the N-terminal PAS domain of the KCNH channel from Zebrafish (zNTD), we over-expressed and purified zNTD. We report the resonance assignments for zNTD. The data will allow us to perform structural studies for this domain, which will provide insight into its structural basis for the molecular interaction with other regions of the KCNH channel.
URI: https://hdl.handle.net/10356/102346
http://hdl.handle.net/10220/16517
ISSN: 1874-2718
DOI: 10.1007/s12104-013-9475-5
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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