Approximate calculation and experimental derivation of native isoelectric points of membrane protein complexes of Arabidopsis chloroplasts and mitochondria

verfasst von

Christof Behrens, Kristina Hartmann, Stephanie Sunderhaus, Hans Peter Braun, Holger Eubel

Abstract

Electric charges are important intrinsic properties of proteins. They directly affect functionality and also mediate interactions with other molecules such as cofactors, substrates and regulators of enzymatic activity, with lipids as well as other proteins. As such, analysis of the electric properties of proteins gives rise to improved understanding of the mechanism by which proteins fulfil their specific functions. This is not only true for singular proteins but also applies for defined assemblies of proteins, protein complexes and supercomplexes. Charges in proteins often are a consequence of the presence of basic and acidic amino acid residues within polypeptide chains. In liquid phase, charge distributions of proteins change in response to the pH of their environment. The interdependence of protein charge and the surrounding pH is best described by the isoelectric point, which is notoriously difficult to obtain for native protein complexes. Here, experimentally derived native isoelectric points (npIs) for a range mitochondrial and plastid protein complexes are provided. In addition, for four complexes, npIs were calculated by a novel approach which yields results largely matching the experimental npIs.

Organisationseinheit(en)

Institut für Pflanzengenetik

Externe Organisation(en)

Gelcompany GmbH

Typ

Artikel

Journal

Biochimica et Biophysica Acta - Biomembranes

Band

1828

Seiten

1036-1046

Anzahl der Seiten

11

ISSN

0005-2736

Publikationsdatum

29.11.2012

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Biophysik, Biochemie, Zellbiologie

Elektronische Version(en)

https://doi.org/10.1016/j.bbamem.2012.11.028 (Zugang: Offen)