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Which of the following statements best defines the nature of a \"modular domain\" found in a protein, and its function ? A globular region or a protein that is related to globular structures in other proteins. A sequence or amino acids identical to those in other proteins, which performs a similar function. A sequence of amino acids identical to those found in other proteins. Which performs a similar function. A sequence of amino acids that shares significant conservation with regions of amino acids, and which confers a common or related function upon each protein. A sequence of amino acids that can undergo a conformational change similar to mat found in other proteins that contain me same \"module\" of ammo acids. A sequence of amino acids in a protein that can be duplicated many times in the protein. which allow the protein to fold in a specific conformation. Select the correct phrase to complete the sentence. \"For the a subunit of a trimeric G protein, ...\" a G-protein-coupled receptor (GPCR) acts as a guanine nucleotide exchange factor (GEF). whereas a regulator of G protein signaling (RGS) can act as a GTPase-activating protein (GAP). a GPCR acts as a GAP, whereas an RGS can act as a GEF both a GPCR and an RGS can act as a GEF both a GPCR and an RGS can act as a GAP. A specific heterotrimeric G-protein is associated with a GPCR whose ligand causes a reduction in blood pressure. A person has accidently ingested a drug that irreversibly binds and activates this GPCR The person has passed out and has been taken to the emergency room of a hospital where you are the physician that must select a drug to combat the symptoms displayed by the person Knowing the identity of the drug and its mechanism of action, which of the following options would you choose to try to reverse the drug\'s effect as quickly as possible ? Treat with a drug that stimulates the G-protein\'s gap activity. Treat with a drug that increases expression of me GPCR Treat with a drug that inhibits the G-protein\'s RGS. Treat with a drug that stimulates the GPCR\'s GRK activity Treat with a drug that inhibits me GPCR s GRK activity. Which of the following is unlikely to be involved in a signaling process that causes a rapid change in the cytoskeleton ? Cdc42 Calmodulin An gene regulator protein. A gene regulatory protein Cytosolic proteins containing PH domains. Which of the following modifications does not involve covalent modification of a protein ? Phosphorylation of multiple serine and threonine ammo acids distributed throughout me protein. Modification of an EF-hand domain in a protein by binding to calcium. Dephosphorylation of a single tyrosine in a protein. Myristoylation of a protein and phosphorylation of three tyrosine amino acids. Myristoylation only of me protein.

Solution

5. Covalent modification involves the mutual sharing of electrons and form or breaks the perminant bond. Where as in non covalent modifications, there is no electron sharing occurs and no perminant bond occurs. These are temporary interactions. So the Second one is the Answer.: Modification of an EF hand domain in a protein by binding to Calcium

4. Answer is 4. Gene regulatory protein has no role in Cytoskeliton regulation

1. Answer is 4. Modular domains, which are the subunits of a protein, moderate these proteininteractions by identifying short peptide sequences. These peptide sequences determine the binding partners of each protein. One of the more prominent domainsis the SH2 domain.

2. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein\'s subunit, together with the bound GTP, can then dissociate from the and subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the subunit type. Answer is the 1

For a direct link for the image: https://s15.postimg.org/rzhhq7y2z/image.png Which of the following statements best defines the nature of a \

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