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Proteins have been studied and recognized since the 1700s by Antoine Fourcroy and others, [1] [2] who often collectively called them "albumins", or "albuminous materials" (Eiweisskörper, in German). [2] Gluten, for example, was first separated from wheat in published research around 1747, and later determined to exist in many plants. [1]
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multi-protein complexes. [14] Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules ...
The classic cadherins (E-, N-and P-) are concentrated at the intermediate cell junctions, which link to the actin filament network through specific linking proteins called catenins. [18] Cadherins are notable in embryonic development. For example, cadherins are crucial in gastrulation for the formation of the mesoderm, endoderm, and ectoderm ...
Proteins in human: There are about ~20,000 protein coding genes in the standard human genome. (Roughly ~1200 already have Wikipedia articles - the Gene Wiki - about them) if we are Including splice variants, there could be as many as 500,000 unique human proteins [ 16 ]
Modified amino acids are sometimes observed in proteins; this is usually the result of enzymatic modification after translation (protein synthesis). For example, phosphorylation of serine by kinases and dephosphorylation by phosphatases is an important control mechanism in the cell cycle. Only two amino acids other than the standard twenty are ...
A protein superfamily is the largest grouping of proteins for which common ancestry can be inferred (see homology). Usually this common ancestry is inferred from structural alignment [ 1 ] and mechanistic similarity, even if no sequence similarity is evident. [ 2 ]
The protein is located in the inner mitochondrial membrane and transports phosphate ions for use in oxidative phosphorylation. It became known as the phosphate-hydroxide antiporter, or mitochondrial phosphate carrier protein, and was the first example of an antiporter identified in living cells. [13] [14]