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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 ]
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.
Albumin is a family of globular proteins, the most common of which are the serum albumins. All of the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not ...
The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group.
11657 Ensembl ENSG00000163631 ENSMUSG00000029368 UniProt P02768 P07724 RefSeq (mRNA) NM_000477 NM_009654 RefSeq (protein) NP_000468 NP_033784 Location (UCSC) Chr 4: 73.4 – 73.42 Mb Chr 5: 90.61 – 90.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma ; it ...
Aromatic amino acids stabilize folded structures of many proteins. [ 4 ] [ 5 ] Aromatic residues are found predominantly sequestered within the cores of globular proteins , although often comprise key portions of protein-protein or protein- ligand interaction interfaces on the protein surface.
The first protein to have its amino acid chain sequenced was insulin, by Frederick Sanger, in 1949. Sanger correctly determined the amino acid sequence of insulin, thus conclusively demonstrating that proteins consisted of linear polymers of amino acids rather than branched chains, colloids, or cyclols. [21]
Protein structures range in size from tens to several thousand amino acids. [2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.