Unknown

Dataset Information

0

Engineered nanostructured ?-sheet peptides protect membrane proteins.


ABSTRACT: We designed ?-strand peptides that stabilize integral membrane proteins (IMPs). ?-strand peptides self-assemble in solution as filaments and become restructured upon association with IMPs; resulting IMP-?-strand peptide complexes resisted aggregation when diluted in detergent-free buffer and were visible as stable, single particles with low detergent background in electron micrographs. ?-strand peptides enabled clear visualization of flexible conformations in the highly dynamic ATP-binding cassette (ABC) transporter MsbA.

SUBMITTER: Tao H 

PROVIDER: S-EPMC3753066 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications


We designed β-strand peptides that stabilize integral membrane proteins (IMPs). β-strand peptides self-assemble in solution as filaments and become restructured upon association with IMPs; resulting IMP-β-strand peptide complexes resisted aggregation when diluted in detergent-free buffer and were visible as stable, single particles with low detergent background in electron micrographs. β-strand peptides enabled clear visualization of flexible conformations in the highly dynamic ATP-binding casse  ...[more]

Similar Datasets

| S-EPMC3645414 | biostudies-literature
| S-EPMC5477022 | biostudies-literature
| S-EPMC9775415 | biostudies-literature
| S-EPMC3986158 | biostudies-literature
| S-EPMC3088102 | biostudies-literature
| S-EPMC4331239 | biostudies-literature
| S-EPMC5415599 | biostudies-literature
| S-EPMC8828358 | biostudies-literature
| S-EPMC2596933 | biostudies-literature
| S-EPMC2854864 | biostudies-literature