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18453 Ensembl ENSG00000185624 ENSMUSG00000025130 UniProt P07237 P09103 RefSeq (mRNA) NM_000918 NM_011032 RefSeq (protein) NP_000909 NP_035162 Location (UCSC) Chr 17: 81.84 – 81.86 Mb Chr 11: 120.45 – 120.46 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein disulfide-isomerase, also known as the beta- subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans ...
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]
In the second row are the maximal subgroups; their intersection (the Frattini subgroup) is the central element in the third row. So Dih 4 has only one non-generating element beyond e . In mathematics , particularly in group theory , the Frattini subgroup Φ ( G ) {\displaystyle \Phi (G)} of a group G is the intersection of all maximal subgroups ...
This lists the character tables for the more common molecular point groups used in the study of molecular symmetry.These tables are based on the group-theoretical treatment of the symmetry operations present in common molecules, and are useful in molecular spectroscopy and quantum chemistry.
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 ]
Protein subfamily is a level of protein classification, based on their close evolutionary relationship. It is below the larger levels of protein superfamily and protein family. [1] Proteins typically share greater sequence and function similarities with other subfamily members than they do with members of their wider family.
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
The rough secondary-structure content of a biopolymer (e.g., "this protein is 40% α-helix and 20% β-sheet.") can be estimated spectroscopically. [15] For proteins, a common method is far-ultraviolet (far-UV, 170–250 nm) circular dichroism. A pronounced double minimum at 208 and 222 nm indicate α-helical structure, whereas a single minimum ...