pstair-peptide and kinetensin

pstair-peptide has been researched along with kinetensin* in 1 studies

Other Studies

1 other study(ies) available for pstair-peptide and kinetensin

ArticleYear
Electrostatic control of peptide side-chain reactivity using amphiphilic homopolymer-based supramolecular assemblies.
    Journal of the American Chemical Society, 2013, Sep-25, Volume: 135, Issue:38

    Supramolecular assemblies formed by amphiphilic homopolymers with negatively charged groups in the hydrophilic segment have been designed to enable high labeling selectivity toward reactive side chain functional groups in peptides. The negatively charged interiors of the supramolecular assemblies are found to block the reactivity of protonated amines that would otherwise be reactive in aqueous solution, while maintaining the reactivity of nonprotonated amines. Simple changes to the pH of the assemblies' interiors allow control over the reactivity of different functional groups in a manner that is dependent on the pKa of a given peptide functional group. The labeling studies carried out in positively charged supramolecular assemblies and free buffer solution show that, even when the amine is protonated, labeling selectivity exists only when complementary electrostatic interactions are present, thereby demonstrating the electrostatically controlled nature of these reactions.

    Topics: Amyloid beta-Peptides; Benzoates; CDC2 Protein Kinase; Diethyl Pyrocarbonate; Hydrogen-Ion Concentration; Micelles; Oligopeptides; Peptide Fragments; Peptides; Polymers; Quaternary Ammonium Compounds; Static Electricity; Succinimides; Tandem Mass Spectrometry

2013