Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity

Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity

Integral membrane proteins of the aquaporin family facilitate rapid water flux across cellular membranes in all domains of life. Although the water-conducting pore is clearly defined in an aquaporin monomer, all aquaporins assemble into stable tetramers. In order to investigate the role of protomer&...

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Bibliographic Details
Main Authors: Noreen Klein, Margareta Trefz, Dirk Schneider
Format: Article
Language:English
Published: MDPI AG 2019-02-01
Series:International Journal of Molecular Sciences
Subjects:
aquaglyceroporin
covalent linkage
GlpF
homooligomer
membrane protein
protein folding
tetramer
interaction
Online Access:https://www.mdpi.com/1422-0067/20/4/927

Internet

https://www.mdpi.com/1422-0067/20/4/927

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