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Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironme...

Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironme...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_24760278

Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironment during the growth of single transmembrane α-helical peptide crystals

About this item

Full title

Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironment during the growth of single transmembrane α-helical peptide crystals

Publisher

THE ROYAL SOCIETY

Journal title

Philosophical transactions of the Royal Society of London. Series A: Mathematical, physical, and engineering sciences, 2016-07, Vol.374 (2072), p.1-17

Language

English

Formats

Publication information

Publisher

THE ROYAL SOCIETY

More information

Scope and Contents

Contents

The proposed mechanism for in meso crystallization of transmembrane proteins suggests that a protein or peptide is initially uniformly dispersed in the lipid self-assembly cubic phase but that crystals grow from a local lamellar phase, which acts as a conduit between the crystal and the bulk cubic phase. However, there is very limited experimental...

Alternative Titles

Full title

Exploring the in meso crystallization mechanism by characterizing the lipid mesophase microenvironment during the growth of single transmembrane α-helical peptide crystals

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_jstor_primary_24760278

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_24760278

Other Identifiers

ISSN

1364-503X

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