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12057 Ensembl ENSG00000128617 ENSMUSG00000058831 UniProt P03999 P51491 RefSeq (mRNA) NM_001708 NM_001385125 NM_007538 RefSeq (protein) NP_001699 NP_031564 Location (UCSC) Chr 7: 128.77 – 128.78 Mb Chr 6: 29.38 – 29.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Blue-sensitive opsin is a protein that in humans is encoded by the OPN1SW gene. The OPN1SW gene provides ...
Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH), and a side chain (CH 2) 4 NH 2 (which ...
Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.
14539 Ensembl ENSG00000102076 ENSMUSG00000031394 UniProt P04000 O35599 RefSeq (mRNA) NM_020061 NM_008106 RefSeq (protein) NP_064445 NP_032132 Location (UCSC) Chr X: 154.14 – 154.16 Mb Chr X: 73.17 – 73.19 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse OPN1LW is a gene on the X chromosome that encodes for long wave sensitive (LWS) opsin, or red cone photopigment. The OPN1LW gene ...
The identification of the crystal structure of squid rhodopsin [13] is likely to further our understanding of its function in this group. Arthropods use different opsins in their different eye types, but at least in Limulus the opsins expressed in the lateral and the compound eyes are 99% identical and presumably diverged recently.
The opsins in the cone cells are OPN1SW, OPN1MW, and OPN1LW. The cones form incomplete disks that are part of the plasma membrane, so that the N-terminus head extends outside of the cell. In opsins, retinal binds covalently to a lysine [16] in the seventh transmembrane helix [17] [18] [19] through a Schiff base.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino -terminal (N) end to the carboxyl -terminal (C) end.
Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by X-ray crystallography to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer. [2] KAM was first purified and characterized in Clostridium subterminale for studies of Lysine metabolism.