Beta Sheet Models - with Side Chains (BS)
These protein models illustrate how the linear polypeptide chain in an amino acid sequence folds into the stable β-sheet structure to form a protein’s secondary structure.
Both ß-sheet plaster models are derived from amino acids 14-32 and 120-127 of the green fluorescent protein. Two of the strands in this model are anti-parallel with respect to each other, while 2 strands are parallel. One model of this set includes side chains. The other model does not, allowing students to focus on the hydrogen bonding between backbone atoms that stabilizes this secondary structure.
They are made of plaster in ball and stick format and follows the standard CPK color scheme. They will break if dropped, held tightly or handled roughly. Their PDB file is 1EMB.pdb.
The β-Sheet Models are most effective when used in conjunction with 3-D Molecular Designs’ Alpha Helix Models and Alpha Helix Beta Sheet Construction Kit©.
CONTENTS:
The models are made of plaster in ball and stick format and follows the standard CPK color scheme. They will break if dropped, held tightly or handled roughly.
* The displayed value refers to the BS without Side Chains model.
