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NMR Study of a Membrane Protein in Detergent-Free Aqueous Solution

NMR Study of a Membrane Protein in Detergent-Free Aqueous Solution

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_102_25_8893

NMR Study of a Membrane Protein in Detergent-Free Aqueous Solution

About this item

Full title

NMR Study of a Membrane Protein in Detergent-Free Aqueous Solution

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2005-06, Vol.102 (25), p.8893-8898

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the feasibility of studying the structure of APol-complexed MPs b...

Alternative Titles

Full title

NMR Study of a Membrane Protein in Detergent-Free Aqueous Solution

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pnas_primary_102_25_8893

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_102_25_8893

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0503750102

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