Search results
Results from the WOW.Com Content Network
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. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
1071 n/a Ensembl ENSG00000087237 n/a UniProt P11597 n/a RefSeq (mRNA) NM_000078 NM_001286085 n/a RefSeq (protein) NP_000069 NP_001273014 n/a Location (UCSC) Chr 16: 56.96 – 56.98 Mb n/a PubMed search n/a Wikidata View/Edit Human Cholesteryl ester transfer protein (CETP), also called plasma lipid transfer protein, is a plasma protein that facilitates the transport of cholesteryl esters and ...
590 12038 Ensembl ENSG00000114200 ENSMUSG00000027792 UniProt P06276 Q03311 RefSeq (mRNA) NM_000055 NM_009738 RefSeq (protein) NP_000046 NP_033868 Location (UCSC) Chr 3: 165.77 – 165.84 Mb Chr 3: 73.54 – 73.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Butyrylcholinesterase (HGNC symbol BCHE ; EC 3.1.1.8), also known as BChE, BuChE, BuChase, pseudocholinesterase, or plasma ...
Furthermore, the TetM protein is found to allow aminoacyl-tRNA molecules to bind to the ribosomal acceptor site, despite being concentrated with tetracyclines that would typically inhibit such actions. The TetM protein is regarded as a ribosomal protection protein, exhibiting GTPase activity that is dependent upon ribosomes.
Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 [1] by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. [2] Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A. [3]
[5] [6] The protein is also historically known as serine esterase 1 (SES1), monocyte esterase and cholesterol ester hydrolase (CEH). Three transcript variants encoding three different isoforms have been found for this gene. [6] The various protein products from isoform a, b and c range in size from 568, 567 and 566 amino acids long, respectively.
Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase. The addition of peroxide with the glutamyl-375 and aspartyl-225 of lactoperoxidase forms ester bonds between these amino acid residues and the heme 1- and 5-methyl groups, respectively. [19]
Phosphatidylserine (PS) is the major acidic phospholipid class that accounts for 13–15% of the phospholipids in the human cerebral cortex. [7] In the plasma membrane, PS is localized exclusively in the cytoplasmic leaflet where it forms part of protein docking sites necessary for the activation of several key signaling pathways.