ArticleProtein science : a publication of the Protein Society2012
Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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70 citing papers in PubMed, 156 citations in OpenAlex.
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- Hydrophobicity causes anomalous migration of cystine/glutamate antiporter SLC7A11 in SDS-PAGE with low acrylamide concentration.FEBS open bio · 2025Article
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- Phosphoserine Aminotransferase Pathogenetic Variants in Serine Deficiency Disorders: A Functional Characterization.Biomolecules · 2023Article
- Proteins in human body fluids contain in vivo antigen analog of the melibiose-derived glycation product: MAGE.Scientific reports · 2022Article
- Investigations on the substrate binding sites of hemolysin B, an ABC transporter, of a type 1 secretion system.Frontiers in microbiology · 2022Article
- Synthesis, LC-MS/MS analysis, and biological evaluation of two vaccine candidates against ticks based on the antigenic P0 peptide from R. sanguineus linked to the p64K carrier protein from Neisseria meningitidis.Analytical and bioanalytical chemistry · 2021Article
- A molecular dynamics study of protein denaturation induced by sulfonate-based surfactants.Journal of molecular modeling · 2021Article
10 more citing papers are in PubMed but not listed here.
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9 authors at 3 institutions in 1 country.
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Abstract
The amino acid substitution or post-translational modification of a cytosolic protein can cause unpredictable changes to its electrophoretic mobility during SDS-PAGE. This type of "gel shifting" has perplexed biochemists and biologists for decades. We identify a mechanism for "gel shifting" that predominates among a set of ALS (amyotrophic lateral sclerosis) mutant hSOD1 (superoxide dismutase) proteins, post-translationally modified hSOD1 proteins, and homologous SOD1 proteins from different organisms. By first comparing how 39 amino acid substitutions throughout hSOD1 affected SDS-PAGE migration, we found that substitutions that caused gel shifting occurred within a single polyacidic domain (residues ~80-101), and were nonisoelectric. Substitutions that decreased the net negative charge of domain 80-101 increased migration; only one substitution increased net negative charge and slowed migration. Capillary electrophoresis, circular dichroism, and size exclusion chromatography demonstrated that amino acid substitutions increase migration during SDS-PAGE by promoting the binding of three to four additional SDS molecules, without significantly altering the secondary structure or Stokes radius of hSOD1-SDS complexes. The high negative charge of domain 80-101 is required for SOD1 gel shifting: neutralizing the polyacidic domain (via chimeric mouse-human SOD1 fusion proteins) inhibited amino acid substitutions from causing gel shifting. These results demonstrate that the pattern of gel shifting for mutant cytosolic proteins can be used to: (i) identify domains in the primary structure that control interactions between denatured cytosolic proteins and SDS and (ii) identify a predominant chemical mechanism for the interaction (e.g., hydrophobic vs. electrostatic).
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