What modification of the Lamin A protein results in its targeting to the nuclear envelope (what type of tail gets added once the protein has reached the nucleus)? a fatty acid (famesyl group) phosphate group N-linked oligosaccharide Ubiquitin group
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Which covalent modification of proteins is correctly linked to its function? Polyubiquitin attachment drives assembly of quaternary structure and multi-protein complexes. Palmitoyl attachment causes protein degradation. Acetyl attachment to chromatin proteins (histones) helps to activate genes (affect transcription). Monoubiquitin attachment causes protein degradation.
Sri K.
Trimming of polypeptide chains This includes removal of the formyl group or the entire formylmethionine from bacterial proteins or acetylation in eukaryotes. Attachment of carbohydrate side chains Addition of functional groups such as methyl group, phosphate group Removal of targeting sequence Hydroxyl group can change the conformation of protein, which could affect its function or level of activity. Coupling with cofactors This typically occurs on cell surface proteins and can be used as identifying marks. Removal and/or modification of the N-terminal amino acid Enzymatic cleavage of some proteins, such as insulin, allows them to adopt their active conformation. Modification of individual amino acids Proteins whose functions are needed in a particular location in the cell (at the cell surface or in a particular organelle) include sequences that serve as routing tags that assure the proteins are correctly delivered. Once properly delivered, the tags are removed. Some proteins, such as hemoglobin, require non-proteinaceous elements for activity. In hemoglobin, it is the iron-containing heme group that actually binds to the oxygen.
Adi S.
Proteins are made in the cytoplasm on the class of ribosomes. In the nuclear protein targeting pathway, the signal sequence tells them to go to the nucleus. These proteins contain a region called the signal sequence, followed by bonding of an initial bond to a cytoplasmic protein called (very specific name), and then bonding of a protein called (very specific name) to form a dimer. The dimer is then passed to the nuclear protein (very specific name), resulting in the formation of a trimer. The trimer enters the nucleoplasm through a channel in the nuclear membrane. The trimer binds to the nucleoplasm, and the molecule (name) is released. Once inside, the two cytoplasmic proteins immediately bind to the trimer, driven by a concentration gradient in proteins. The trimer is concentrated on the side of the nuclear membrane. The molecule binds to the trimer and is transported to its destination. The major function of these proteins is (describe). Specifically, lamins are found in the nucleus of cells.
Shyam P.
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