Format

Send to

Choose Destination
See comment in PubMed Commons below
Protein Expr Purif. 2011 Apr;76(2):205-10. doi: 10.1016/j.pep.2010.11.007. Epub 2010 Nov 16.

Expression, purification, detergent screening and solution NMR backbone assignment of the human potassium channel accessory subunit MiRP1.

Author information

  • 1Hefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, PR China.

Abstract

MiRP1 (MinK related protein 1) is a membrane protein in the KCNE family. It can associate with and modulate various voltage gated potassium channels. Mutations in human MiRP1 have been found to cause many congenital and acquired long QT syndromes, which are potentially life-threatening cardiac arrhythmias. Here, human MiRP1 was over-expressed in Escherichia coli, purified and eluted into different detergents. Two dimensional (1)H-(15)N correlated solution nuclear magnetic resonance (NMR) spectra of the human MiRP1 in four different detergent micelles indicated that high resolution solution NMR spectrum can be obtained for human MiRP1 in detergent lyso-myristoylphosphatidylglycerol (LMPG). Circular dichroism (CD) spectroscopy of human MiRP1 indicated a high content of alpha-helical secondary structure in LMPG. Backbone assignments of most MiRP1 residues were achieved through a series of triple resonance NMR experiments. Secondary structure analysis based on backbone chemical shifts showed several stretches of alpha-helices along the primary sequence of MiRP1 in LMPG.

Copyright © 2010 Elsevier Inc. All rights reserved.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk