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Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. [1] There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. [2]
Most of them are water-soluble outer membrane proteins and frequently bind hydrophobic ligands in the barrel center, as in lipocalins. Others span cell membranes and are commonly found in porins . Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria. [ 1 ]
As of January 2013 less than 0.1% of protein structures determined were membrane proteins despite being 20–30% of the total proteome. [15] Due to this difficulty and the importance of this class of proteins methods of protein structure prediction based on hydropathy plots, the positive inside rule and other methods have been developed. [16 ...
The protein is made up of at least three different subunits and varies according to the species of algae that produces it. The subunit structure of the most common R-PE is (αβ) 6 γ. The α subunit has two phycoerythrobilins (PEB), the β subunit has 2 or 3 PEBs and one phycourobilin (PUB), while the different gamma subunits are reported to ...
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 ...
Schematic diagram of the 2D structure of aquaporin 1 depicting the six transmembrane alpha-helices and the five interhelical loop regions A-E The 3D structure of aquaporin Z highlighting the 'hourglass'-shaped water channel that cuts through the center of the protein. Aquaporin proteins are composed of a bundle of six transmembrane α-helices ...
The generation of a protein sequence is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed. [39]
The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins. In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure.