CFTR three-dimensional structure.

Robert C. Ford; James Birtley; Mark F. Rosenberg; Liang Zhang

doi:10.1007/978-1-61779-117-8_22

CFTR three-dimensional structure.

Robert C. Ford, James Birtley, Mark F. Rosenberg, Liang Zhang

Research output: Contribution to journal › Article › peer-review

Abstract

CFTR is a member of the ATP-binding cassette family of membrane proteins. This is one of the best characterised membrane protein families in terms of structure and function. CFTR operates as an ion channel, unlike nearly all other family members which are active transporters. Here, we discuss methods that have allowed such data to be obtained for CFTR.

Original language	English
Pages (from-to)	329-346
Number of pages	17
Journal	Methods in Molecular Biology
Volume	741
DOIs	https://doi.org/10.1007/978-1-61779-117-8_22
Publication status	Published - 2011

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10.1007/978-1-61779-117-8_22

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title = "CFTR three-dimensional structure.",

abstract = "CFTR is a member of the ATP-binding cassette family of membrane proteins. This is one of the best characterised membrane protein families in terms of structure and function. CFTR operates as an ion channel, unlike nearly all other family members which are active transporters. Here, we discuss methods that have allowed such data to be obtained for CFTR.",

author = "Ford, {Robert C.} and James Birtley and Rosenberg, {Mark F.} and Liang Zhang",

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doi = "10.1007/978-1-61779-117-8_22",

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AU - Ford, Robert C.

AU - Birtley, James

AU - Rosenberg, Mark F.

AU - Zhang, Liang

PY - 2011

Y1 - 2011

N2 - CFTR is a member of the ATP-binding cassette family of membrane proteins. This is one of the best characterised membrane protein families in terms of structure and function. CFTR operates as an ion channel, unlike nearly all other family members which are active transporters. Here, we discuss methods that have allowed such data to be obtained for CFTR.

AB - CFTR is a member of the ATP-binding cassette family of membrane proteins. This is one of the best characterised membrane protein families in terms of structure and function. CFTR operates as an ion channel, unlike nearly all other family members which are active transporters. Here, we discuss methods that have allowed such data to be obtained for CFTR.

U2 - 10.1007/978-1-61779-117-8_22

DO - 10.1007/978-1-61779-117-8_22

M3 - Article

C2 - 21594795

VL - 741

SP - 329

EP - 346

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -

CFTR three-dimensional structure.

Abstract

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