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.
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Which statement about N-linked glycosylation is correct?
N-linked oligosaccharides are attached to proteins one sugar at the time in the endoplasmicreticulum. |
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N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation in the endoplasmic reticulum. |
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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. |
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- Polypeptides which are normally synthesized in the endoplasmic reticulum are about20 amino acids longer when they are synthesized by ribosomes not attached to the endoplasmicreticulum, What is the significance of this increase in length?Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?Rank from left to right the compound with the most reactive chemical linkage: peptide bond, ester, ether, acid anhydride, aminoacyl-TRNA How many bacterial translation factors are "G" proteins? How many proteins are involved in the nucleotide-dependent steps of protein synthesis?
- Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylatedProtein modifications that involve disulfide bonds occur in the following;(there may be more than one answer) golgi endoplasmic reticulum ) chloroplast (plastids) peroxisome mitochondriaCheck the box under each molecule for which the statement in the first column is true. statement It usually contains several thousand adenine, thymine, cytosine, and guanine residues. It's made in the nucleus, but transported to the cytoplasm to do its job. When combined with a number of different proteins, it forms a large complex in the cytoplasm responsible for synthesizing new proteins. It does not contain instructions for making a protein. There is a specific version of it for every possible amino acid in every possible protein. ribosomal messenger transfer RNA RNA RNA 0 0 0 ☐ 0 X
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