Possible Interaction: Sodium Dodecyl Sulfate and Polypeptides

“wt polypeptides are cleaved either chemically or enzymatically in the presence of SDS.”

“Reduction in the presence of SDS yielded several polypeptide bands.”

“Sodium dodecyl sulfate SDS ) has consistently been shown to induce secondary structure, particularly alpha-helices, in polypeptides , and is commonly used to model membrane and other hydrophobic environments.”

“The interaction with negatively charged SDS micelles increases the secondary and tertiary structure content of the polypeptide , while, in the case of large unilamellar vesicles and bicelles, conformational changes were observed at the terminal regions, with no significant acquisition of secondary structure motifs.”

“Comparisons of the acid-insoluble nonhistone proteins by sodium dodecylsulfate gel electrophoresis reveal significant quantitative changes in a 28,600 dalton polypeptide present in large quantities at 30, 35, and 50 days of age in the hybrid and at 40 and 45 days only in the inbred.”

“Rat brain Kv2.1 polypeptides are phosphorylated extensively, leading to a dramatically increased molecular mass on sodium dodecyl sulfate gels.”

“Commercial SDS containing contaminants other than sodium tetradecyl sulfate reduced or eliminated the immunosignal from certain polypeptides and the loss of antigenicity could not even be recovered by immunoblot under “renaturing” conditions.”

“The complexes formed between SDS and protein polypeptide showed electrophoretic mobilities virtually insensitive to the protein molecular weight.”

“Furthermore, peptide mapping performed on isolated polypeptides showed comigrating fragments on SDS‐PAGE.”

“We suggest that, due to an asymmetric distribution of amino acids in the Pr86-class molecules, SDS binding results in a lower charge to mass ratio in the native folded polypeptides and a higher charge to mass ratio upon disulfide bond reduction and unfolding of the polypeptides.”