ß-globin, a subunit of hemoglobin, is a small protein
(146 amino acids) that transports oxygen throughout our bodies. This
protein has a ring-like heme group, which contains an iron atom that
binds the oxygen. This subunit also contains the glutamic acid at
position 6 that, when changed to valine, results in the sickle cell
mutation. Other changes to the β-globin subunit may also result in human
disease. Varying severities of betathalassemia can develop as a result
of a damaged or completely missing β-globin.
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.
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).
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).