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Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus...

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_26056273

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops

About this item

Full title

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2015-06, Vol.112 (26), p.7978-7983

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Despite the ubiquity of helical membrane proteins in nature and their pharmacological importance, the mechanisms guiding their folding remain unclear. We performed kinetic folding and unfolding experiments on 69mutants (engineered every 2–3 residues throughout the 178-residue transmembrane domain) of GlpG, a membrane-embedded rhomboid protease from...

Alternative Titles

Full title

Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmed_primary_26056273

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_26056273

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1424751112

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