Determining the topology of an integral membrane protein.

N. Green*, H. Fang, K. U. Kalies, V. Canfield

*Corresponding author for this work
3 Citations (Scopus)


A variety of methods have been developed for assigning the aqueous domains of integral membrane proteins to either side of a biological membrane. Once the sequence of a protein is known from its DNA sequence it is possible to study the topology of the protein. This unit provides protocols in which the water-soluble domains can be tested for their accessibility to reagents added to membranes with a defined orientation. Tagging of hydrophilic regions of the protein with different epitopes and probing of their orientation with respect to the membrane is also described. Finally, a procedure for fusion of a reporter enzyme to truncated fragments of the protein is provided. The fusion protein is used as a sensor of sequence disposition relative to the membrane.

Original languageEnglish
JournalCurrent protocols in cell biology / editorial board, Juan S. Bonifacino ... [et al.]
VolumeChapter 5
Publication statusPublished - 05.2001

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


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