Details
| Original language | English |
|---|---|
| Pages (from-to) | 1036-1046 |
| Number of pages | 11 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1828 |
| Issue number | 3 |
| Publication status | Published - 29 Nov 2012 |
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.
Keywords
- Chloroplasts, Free flow electrophoresis, Ionisable amino acids, Membrane protein complexes, Mitochondria, Native isoelectric point
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Biochimica et Biophysica Acta - Biomembranes, Vol. 1828, No. 3, 29.11.2012, p. 1036-1046.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Approximate calculation and experimental derivation of native isoelectric points of membrane protein complexes of Arabidopsis chloroplasts and mitochondria
AU - Behrens, Christof
AU - Hartmann, Kristina
AU - Sunderhaus, Stephanie
AU - Braun, Hans Peter
AU - Eubel, Holger
N1 - Funding information: We thank Dr. Nir Keren, Hebrew University of Jerusalem for cooperation, Michael Senkler for expert help in setting up nativepI and Marianne Langer for expert technical assistance. This joint research project was financially supported by the State of Lower-Saxony and the VolkswagenFoundation , Hannover, Germany (Project VWZN2326 ).
PY - 2012/11/29
Y1 - 2012/11/29
N2 - 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.
AB - 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.
KW - Chloroplasts
KW - Free flow electrophoresis
KW - Ionisable amino acids
KW - Membrane protein complexes
KW - Mitochondria
KW - Native isoelectric point
UR - http://www.scopus.com/inward/record.url?scp=84872120134&partnerID=8YFLogxK
U2 - 10.1016/j.bbamem.2012.11.028
DO - 10.1016/j.bbamem.2012.11.028
M3 - Article
C2 - 23201540
AN - SCOPUS:84872120134
VL - 1828
SP - 1036
EP - 1046
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 3
ER -