The 1962 Nobel Prize in Chemistry was awarded jointly to Max Ferdinand Perutz and John Cowdery Kendrew "for their studies of the structures of globular proteins". Max Ferdinand Perutz solved the structure of hemoglobin in 1959.
Both 4'' models are made of plaster by rapid prototyping and should be handled with care. They will break if dropped, held tightly or handled roughly. Its PDB file is 2HHB.pdb.
Corresponds with ß-Globin Folding Kit©
Our first dual-purpose, 3-D model of ß-globin can be used alone to illustrate protein structure, physiology and the lasting effects of a single amino acid mutation on a protein, or as an accurate smaller scale template for 3D Molecular Designs’ ß-Globin Folding Kit©.
This alpha carbon backbone, 3-D protein model features the heme group with its iron atom which binds oxygen; the sickle cell mutation; and selected charged, hydrophobic and hydrophilic side chains. The β-globin protein is colored blue, green, and red from the N-terminus to the C-terminus, to coordinate with three fragments in ß- Globin Folding Kit©. The heme group is shown in yellow, with the iron atom highlighted in orange in the center. Select side chains are displayed in ball-and-stick format and CPK coloring scheme (Lys17, Tyr35, His63, Phe71, Phe85, Glu90, His92, Phe103, Leu106, Glu121, Lys132, Val137, Lys144).
β-Globin Folding Kit© Teacher Resources
Corresponds with Map of the Human ß-Globin Gene©
Our second ß-globin 3-D protein model is a colorful addition to your lessons about physiology, protein structure and bioinformatics. It can stand alone as an illustrative model, or as a companion model for the Map of the Human ß-Globin Gene©.
The 3 colors of the alpha carbon backbone correspond to the 3 exons in the gene. Selected side chains on the protein model indicate mutations that are noted on the Teacher Map of the Human ß-Globin Gene©. The model also features the heme group with its iron atom-binding oxygen. This β-Globin Mini Model may be used to discuss protein structure, physiology, and the lasting effects of a single amino acid mutation on a protein. The β-globin protein is colored yellow, cyan, and magenta from the N-terminus to the C terminus. The heme group is shown in the CPK coloring scheme, with the iron atom highlighted in orange in the center. Select side chains are displayed in ball-and-stick format and CPK coloring scheme (Glu6, Glu26, His63, His92, Gln131, His146).
Map of the Human ß-Globin Gene© Teacher Resources