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The methyl side-chain of alanine is non-reactive and is therefore hardly ever directly involved in protein function. [12] Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained through the diet. Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
290 16790 Ensembl ENSG00000166825 ENSMUSG00000039062 UniProt P15144 P97449 RefSeq (mRNA) NM_001150 NM_001381923 NM_001381924 NM_008486 RefSeq (protein) NP_001141 NP_001368852 NP_001368853 NP_032512 Location (UCSC) Chr 15: 89.78 – 89.82 Mb Chr 7: 79.47 – 79.51 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl ...
The two halves of the proteins are therefore of opposite orientation in the membrane. A well-conserved region between TMSs 2 and 3 and TMSs 5 and 6 dip into the membrane, each loop forming a half TMS. [22] [23] A common amino acyl motif in these transporters is an asparagine–proline–alanine (NPA) motif. Aquaporins generally have the NPA ...
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, carboxy tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The ...
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).
Aquaporin 2 is regulated by vasopressin which, when bound to the cell-surface receptor, activates the cAMP signaling pathway. This results in aquaporin-2 containing vesicles to increase water uptake and return to circulation. Mutation of the aquaporin 2 vasopressin receptor is a cause of acquired diabetes insipidus.
Three-dimensional structure [1] of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure, and it is ...
[13] [16] Detergents can be used to render membrane proteins water-soluble, but these can also alter protein structure and function. [13] Making membrane proteins water-soluble can also be achieved through engineering the protein sequence, replacing selected hydrophobic amino acids with hydrophilic ones, taking great care to maintain secondary ...