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This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini. [4] Since the globin fold contains only helices, it is classified as an all-alpha protein fold. The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the ...
Schematic representation of a protein electrophoresis gel. All globulins fall into one of the following three categories : Alpha globulins; Beta globulins; Gamma globulins (one group of gamma globulins is the immunoglobulins, which are also known as "antibodies")
Hemoglobin (haemoglobin, [a] Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells.Almost all vertebrates contain hemoglobin, [3] with the sole exception of the fish family Channichthyidae. [4]
Globin synthesis takes place in the ribosomes which are located within the cytosol. Two globin chains that have heme groups combine to form hemoglobin. One of the chains is an alpha chain and the other is a non-alpha chain. Non-alpha chain nature in hemoglobin molecules varies due to different variables.
Schematic representation of a protein electrophoresis gel. Alpha globulins are a group of globular proteins in plasma [1] that are highly mobile in alkaline or electrically charged solutions.
A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O 2 transport. [1] Other functions performed include O 2 storage, CO 2 transport, and transportation of substances other than respiratory gases.
The human β-globin locus is composed of five genes located on a short region of chromosome 11, responsible for the creation of the beta parts (roughly half) of the oxygen transport protein Haemoglobin. This locus contains not only the beta globin gene but also delta, gamma-A, gamma-G, and epsilon globin.
The molecular mechanism behind this effect is the steric organization of the globin chain; a histidine residue, located adjacent to the heme group, becomes positively charged under acidic conditions (which are caused by dissolved CO 2 in working muscles, etc.), releasing oxygen from the heme group.