1. Effect of N- and C-terminal functional groups on the stability of collagen triple helices
- Author
-
Helma Wennemers, Pascal J. Schmidt, Jasmine Egli, and Roman S. Erdmann
- Subjects
Thermal denaturation ,Protein Denaturation ,Stereochemistry ,Carboxylic acid ,Collagen helix ,Carboxylic Acids ,010402 general chemistry ,01 natural sciences ,Protein Structure, Secondary ,Catalysis ,chemistry.chemical_compound ,Protein structure ,Materials Chemistry ,Moiety ,Ammonium ,Carboxylate ,chemistry.chemical_classification ,Protein Stability ,010405 organic chemistry ,Temperature ,Metals and Alloys ,General Chemistry ,Hydrogen-Ion Concentration ,3. Good health ,0104 chemical sciences ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,chemistry ,Ceramics and Composites ,Collagen ,Triple helix - Abstract
The effect of charged versus neutral N- and C-termini on the stability of the collagen triple helix was examined. Thermal denaturation studies at different pH with collagen model peptides showed that an ammonium group at the N-terminus destabilizes the triple helix more than a carboxylate at the C-terminus. A neutral carboxylic acid stabilizes the triple helix more than an amido moiety at the C-terminus.
- Published
- 2017
- Full Text
- View/download PDF