Protein modifications occurring in the Golgi apparatus include: removal of sialic acid BiP-mediated protein folding removal of the signal peptide ubiquitination modification of high-mannose and complex N-linked oligosaccharides
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Protein modifications occurring in the Golgi apparatus include:
- removal of sialic acid
- BiP-mediated protein folding
- removal of the signal peptide
- ubiquitination
- modification of high-mannose and complex N-linked oligosaccharides
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- Match the post-translational protein modification to its function. Creates new binding sites by neutralizing positive charges Form protein complexes through quatenary structures Protein localization in the endomembrane system Targets proteins for degradation Creates new binding sites by adding negative charges Lipid anchors Glycosylation Alkylation Polymerization Phosphorylation Aceylation Ubiquitination…Please draw or trace a pathway of any protein from translation to the plasma membrane. Name the protein (make sure it is a transemembrane protein). The protein in question must also have seceral protein modifications including, but not limited to, N-linked glycosylation, cysteine disulfide bonds, lipid modifications, and 3-D foldingMicrofilaments work together with the protein blank to cause movement in cells. provide two examples:
- If you want to engineer a cytoplasmic protein to become a peroxisomal protein, which of the following amino acid sequences would you need to add? A signal sequence to its N-terminus and a KDEL sequence to its C-terminus An SKL sequence to its C-terminus A signal sequence to its C-terminus and a KDEL sequence to its N-terminus A signal sequence to its N-terminus and an SKL sequence to its C-terminus A KDEL sequence to its C-terminusgene normally contains an N' terminal ER signal sequence and an internal stop transfer sequence. The ER signal sequence is recognized and used during the protein trafficking process, as normal. After translation is completed a signal peptidase enzyme cleaves the N' ER signal sequence but the internal sequence is not cleaved. Which of the following figures best represents the orientation of the protein product after translation? N Extracellular Extracellular Extracellular Extracellular -N' C' N Lumen Lumen Lumen Lumen N' A В CA peripheral protein, which is not integral to the cell membrane, is also called: a multi-pass transmembrane protein (like band 3.0 protein) a single-pass transmembrane protein (like glycophorin A) a monolayer-associated protein (like the COX-1 protein) a protein-attached protein (like cytochrome c) a lipid-linked protein (like the Ras protein)
- Place the following steps of the bacterial protein synthesis in their correct order? Peptide bond formation at the peptidyl-transferase center. Binding of MRNA and initiator formyl-methionyl-IRNAMet to the 30S ribosomal subunit, Aminoacylation and formylation of the initiator tRNAMet Joining of the 30S and the 50S ribosomal subunits, Release Factor (RF) dependent hydrolysis of the peptidyl RNA and release of the fully synthesized polypeptide from the ribosome. Elongation Factor G (EF G) dependent translocation of the ribosome by one codon along the MRNA Elongation Factor Tu (EF-Tu) dependent delivery of an aminoacyl-IRNA to the ribosomal A siteParamecium caudatum is a unicellular organism that can phagocytose and digest a bacterium using hydrolytic enzymes. Proteases are one example of hydrolytic enzymes that can break down proteins into polypeptides and amino acids. Name all of the organelles involved, in the order that the protease will go through. from its synthesis to its final destination. Note that this protease needs to be modified through the addition of a carbohydrate in order to be functional.Protein modifications that involve disulfide bonds occur in the following;(there may be more than one answer) golgi endoplasmic reticulum ) chloroplast (plastids) peroxisome mitochondria
- Which statement about N-linked glycosylation is correct? N-linked oligosaccharides are attached to proteins one sugar at the time in the endoplasmicreticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation in the endoplasmic reticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation inthe cytoplasm. N-linked sugars are attached to proteins as a 14 residue oligosaccharide after translation inthe Golgi apparatus.Select the true statements regarding the control of proteins in the cell. Sequestering of proteins in lysozomes is common in cells that function to secrete singaling molecules. Access to monomers is a method of controling polymer synthesis used in the cell post-translation. Phosphorylation involves post-translational control of protein shape and therefore activity. Allosteric activation of proteins is a form of pre-translational control.List three potential organelle destinations for a free ribosome (cytosolic-produced) protein via transmembrane protein translocation: