Related Experiment Video
Updated: May 3, 2026

A High-throughput Calcium-flux Assay to Study NMDA-receptors with Sensitivity to Glycine/D-serine and Glutamate
Published on: July 10, 2018
Stimuli-responsivity of secondary structures of glycopolypeptides derived from poly(L-glutamate-co-allylglycine)
Kai-Steffen Krannig1, Jing Sun, Helmut Schlaad
1Max Planck Institute of Colloids and Interfaces , Department of Colloid Chemistry, Research Campus Golm, 14424 Potsdam, Germany.
Abstract:
Copolypeptides containing L-glutamate and various amounts of either D-/DL-/L-allylglycine or D-/DL-/L-(3-(β-D-glucopyranosyl)thio)propylglycine defect units were studied by circular dichroism (CD) and infrared (FT-IR) spectroscopy according to their secondary structures in dependence of pH and temperature. All samples adopt random coil conformation at high pH and α-helix at low pH without evidence for β-sheet formation. Folding into the α-helix structure is strongly affected by the number and configuration of allylglycine defects (which intrinsically stabilize β-sheets). Helix folding is facilitated upon the attachment of D-glucopyranose to the L- (but not the D-) allylglycine units, which is attributed to a different secondary structure preference of the L-(3-(β-D-glucopyranosyl)thio)propylglycine (L: random coil; D: β-sheet) and a majority rule effect.
Related Concept Videos
Proteoglycans
Protein Glycosylation
Glycosylation occurs in...
Protein Folding Quality Check in the RER
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Glycosaminoglycans
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
Protein Organization
The primary structure of a protein is its amino acid sequence....

