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Open Access Membrane Proteins with β-Barrel Fold

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Porins, the major proteins found in the bacterial outer membrane, exhibit an unusual hollow β-barrel structure. This motif constitutes the scaffold for a pore that facilitates the diffusion of solutes across the membrane. OmpF porin was the first membrane protein to be crystallized many years ago at the Biozentrum in Basel. Since then a wealth of structural information at high resolution has been acquired by X-ray crystallography. Porins from E. coli turned out to be extremely robust and easy to manipulate, allowing detailed and comprehensive structure-function analysis. In particular, insight was obtained into the role of the highly charged pore constriction in OmpF porin and the 'greasy slide', a string of aromatic residues, in maltoporin.

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Keywords: MEMBRANE PROTEIN; PORIN; PROTEIN CRYSTALLOGRAPHY; SIMULATION

Document Type: Research Article

Publication date: June 1, 2001

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  • International Journal for Chemistry and Official Membership Journal of the Swiss Chemical Society (SCS) and its Divisions

    CHIMIA, a scientific journal for chemistry in the broadest sense, is published 10 times a year and covers the interests of a wide and diverse readership. Contributions from all fields of chemistry and related areas are considered for publication in the form of Review Articles and Notes. A characteristic feature of CHIMIA are the thematic issues, each devoted to an area of great current significance.



    As of December 31, 2021, CHIMIA International Journal for Chemistry will no longer be hosted on Ingenta Connect. Please contact the publisher directly for more information.
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