Pascal Heimer
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View article: Effect of Conformational Diversity on the Bioactivity of µ-Conotoxin PIIIA Disulfide Isomers
Effect of Conformational Diversity on the Bioactivity of µ-Conotoxin PIIIA Disulfide Isomers Open
Cyclic µ-conotoxin PIIIA, a potent blocker of skeletal muscle voltage-gated sodium channel NaV1.4, is a 22mer peptide stabilized by three disulfide bonds. Combining electrophysiological measurements with molecular docking and dynamic simul…
View article: Insights into the Folding of Disulfide-Rich μ-Conotoxins
Insights into the Folding of Disulfide-Rich μ-Conotoxins Open
The study of protein conformations using molecular dynamics (MD) simulations has been in place for decades. A major contribution to the structural stability and native conformation of a protein is made by the primary sequence and disulfide…
View article: Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities Open
Peptides with a high number of cysteines are usually influenced regarding the three-dimensional structure by their disulfide connectivity. It is thus highly important to avoid undesired disulfide bond formation during peptide synthesis, be…
View article: Front Cover: Deciphering Specificity Determinants for FR900359‐Derived G<sub>q</sub>α Inhibitors Based on Computational and Structure–Activity Studies (ChemMedChem 16/2018)
Front Cover: Deciphering Specificity Determinants for FR900359‐Derived G<sub>q</sub>α Inhibitors Based on Computational and Structure–Activity Studies (ChemMedChem 16/2018) Open
The Front Cover shows the depsipeptide FR900359 which can be isolated from the traditional Chinese medicine plant Ardisia crenata. It represents, together with the related YM254890, the most efficient compound to inhibit the activity of th…