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In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins). Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. [ 1 ]
Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow spherical nanocage with ... subjects with impaired heme synthesis. ...
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils.It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm.
Usually, proteins are dissolved in plasma and globulin is one of them. The protein serum consists of the serum protein which is about 6 to 8 g/dl then albumin makes 3.5 to 5.0 g/dl then the rest should be the globulins. The section where globulins fractions are located is made up of proteins, enzymes, and immunoglobulins.
The structure of human SUMO1 is depicted on the right. It shows SUMO1 as a globular protein with both ends of the amino acid chain (shown in red and blue) sticking out of the protein's centre. The spherical core consists of an alpha helix and a beta sheet. The diagrams shown are based on an NMR analysis of the protein in solution.
Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. [1] It was discovered and named by Hideo Mōri in 1968. [2]
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 first protein fold discovered (myoglobin was the first protein whose structure was solved).
These traits are similar to those observed in the transient intermediate states found during the folding of certain proteins, especially globular proteins that undergo hydrophobic collapse, and therefore the term "molten globule" is also used to refer to certain protein folding intermediates corresponding to the narrowing region of the folding ...