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Title 

Rapid exploration of the folding topology of helical membrane proteins using paramagnetic perturbation

Authors 

K J YeoH Y KimY P KimE HwangMyung Hee KimC CheongS ChoeY H Jeon

Publisher 

Cold Spring Harbor Laboratory Press

Issue Date 

2010

Citation 

Protein Science, vol. 19, no. 12, pp. 2409-2417

Keywords 

Folding topologyHelical membrane proteinHistidine kinaseNMR spectroscopyParamagnetic relaxation enhancement

Abstract 

An understanding of the folding states of α-helical membrane proteins in detergent systems is important for functional and structural studies of these proteins. Here, we present a rapid and simple method for identification of the folding topology and assembly of transmembrane helices using paramagnetic perturbation in nuclear magnetic resonance spectroscopy. By monitoring the perturbation of signals from glycine residues located at specific sites, the folding topology and the assembly of transmembrane helices of membrane proteins were easily identified without time-consuming backbone assignment. This method is validated with Mistic (membrane-integrating sequence for translation of integral membrane protein constructs) of known structure as a reference protein. The folding topologies of two bacterial histidine kinase membrane proteins (SCO3062 and YbdK) were investigated by this method in dodecyl phosphocholine (DPC) micelles. Combing with analytical ultracentrifugation, we identified that the transmembrane domain of YbdK is present as a parallel dimer in DPC micelle. In contrast, the interaction of transmembrane domain of SCO3062 is not maintained in DPC micelle due to disruption of native structure of the periplasmic domain by DPC micelle.

ISSN 

0961-8368

Link 

http://dx.doi.org/10.1002/pro.521

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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