A new artificial beta-sheet that dimerizes through parallel beta-sheet interactions.
This paper introduces a chemical model of a beta-sheet that dimerizes through parallel beta-sheet interactions in CDCl(3) solution. The model consists of two C-terminally linked dipeptides connected to a molecular template. (1)H NMR studies establish the beta-sheet folding and dimerization of the model system. This system corroborates that linking two peptide strands and blocking one edge of the assembly creates soluble, easy-to-study systems that participate in the types of interactions that occur widely in peptide and protein aggregates.
Levin
Sergiy
S
Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, USA.
Nowick
James S
JS
D008956:Models, Chemical; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins