Check 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
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- Check the box under each molecule for which the statement in the first column is true. statement It communicates genetic information from the chromosomes to the cellular "factories" responsible for synthesizing new proteins. It does not contain instructions for making a protein. It usually contains several hundred amino acid resides. 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. ribosomal RNA 0 transfer messenger RNA RNA n [] 0Check the box under each molecule for which the statement in the first column is true. statement It transfers instructions for making a new protein from the nucleus to ribosomes out in the cytoplasm. When attached to a ribosome, each codon specifies the next amino acid in a protein under construction. It usually contains several thousand adenine, uracil, cytosine, and guanine residues. It's secreted by the adrenal cortex, but transported throughout the body 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. transfer messenger ribosomal RNA RNA RNA 0 [] n UGlycophorins are a type of membrane protein found on red blood cells. They allow red blood cells to circulate through the blood vessels without sticking to the walls of the blood vessels or to other cells. Describe how a glycophorin protein would be synthesized by the cell. Include What parts of the cell are involved and what happens at each location. The process of protein synthesis (i.e. transcription, translation, etc).
- protein that charges its conformation ( and often its activity) when it binds a regulatory molecule or when it is covalently modified. Ligase Regular site Lysozyme Protein subunit Protein domainThe compartmentalization (division) of eukaryotic cells allows many processes to function properly. Summarize how proteins based on peroxisomal proteins get to the right place.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…
- Protein modifications that involve disulfide bonds occur in the following;(there may be more than one answer) golgi endoplasmic reticulum ) chloroplast (plastids) peroxisome mitochondriaHere 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 phosphorylatedRank 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?
- 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.A type of protein that associate with DNA, in Eukaryotes cell to compact the protein is Histamine. True FalseUbiquitin binds to newly synthesized proteins at the ribosome to assist in the protein folding process. True Or False