De novo design of defined helical bundles in membrane environments | Zendy

Başar Bilgiçer | Zendy; Krishna Kumar | Zendy

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De novo design of defined helical bundles in membrane environments

Author(s) -

Başar Bilgiçer,

Krishna Kumar

Publication year - 2004

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.0403314101

Subject(s) - circular dichroism , transmembrane protein , chemistry , context (archaeology) , membrane , membrane protein , transmembrane domain , helix (gastropod) , protein design , förster resonance energy transfer , protein structure , biophysics , crystallography , fluorescence , biochemistry , biology , physics , paleontology , ecology , receptor , quantum mechanics , snail

Control of structure and function in membrane proteins remains a formidable challenge. We report here a new design paradigm for the self-assembly of protein components in the context of nonpolar environments of biological membranes. An incrementally staged assembly process relying on the unique properties of fluorinated amino acids was used to drive transmembrane helix-helix interactions. In the first step, hydrophobic peptides partitioned into micellar lipids. Subsequent phase separation of simultaneously hydrophobic and lipophobic fluorinated helical surfaces fueled spontaneous self-assembly of higher order oligomers. The creation of these ordered transmembrane protein ensembles is supported by gel electrophoresis, circular dichroism spectroscopy, equilibrium analytical ultracentrifugation, and fluorescence resonance energy transfer.

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