Q20 Consider the structure of calmodulin.Identify the correct statements about calmodulin.Calmodulin contains a central, flexible ß sheet thatenables it to wrap around another protein, inhibitingthe protein's activity.Calmodulin contains two Ca²+ binding sites.Calmodulin is a structural subunit of proteins suchas CaM kinase.A calcium ion is bound in the loop of an EF hand.Each calcium-binding domain in calmodulin isformed from a helix-loop-helix motif.Binding of Ca²+ activates calmodulin.m

Calmodulin is a Ca2+ binding protein. It associates with many other proteins and thereby regulates…

Answered: Consider the structure of calmodulin.…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Below is an image of a calcium binding site on the calmodulin protein. What statement is correct regarding this Ca2+ binding? 140 ASN 136 GL IL 29 131 GL 132 133 Time left 1:1 O a. deprotonated acidic side chains are important for Ca2+ binding O b. Ca2+ binding usually does not result in conformational changes in a protein O c. deprotonated basic residues are important for Ca2+ binding O d. Ca2+ binding to proteins is usually done by coordination with one side chain
Many proteins are attached to the membrane phospholipids via a covalently linked polysaccharide. Which of the following would be an example? Glycophosphatidylehanolamine anchors O All of the other are correct O Glycophosphatidylinositol anchors O Glycophosphatidylcholine anchors
Inside of skeletal muscle cells are voltage-controlled calcium ion (Ca2+) gate proteins. These are integral for the contraction mechanisms of skeletal muscle. A picture of them is shown below. These are regulated by voltage, as indicated above. How would voltage serve to open or close these gates? Voltage is a component of hydrogen bonds, which is necessary to maintain the secondary structure of the protein; without voltage, the protein starts to chemically degrade. Voltage actually does not serve as the direct mechanism of opening or closing gated proteins. Changing the voltage changes whether the R groups are charged or not, which alters the actual primary structure of the protein Changing voltage changes the nature of the tertiary structure, causing the protein to change its shape to open or close.
ILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALE
Classify the fold of each protein. Classify the fold of each domain asall a (or mostly a), all b (or mostly b), a/b, or a+b.. 1. Firmicute collagen-binding protein (1FCB): 2. Bat glycosyltransferase (2BGT): 3. Proteobacterial nitrite sensor (3PNS):
A certain protein is used to activate myosin. If the protein is treated with B-mercaptoethanol, it will not activate myosin. What can you say about the structure of this protein? O The peptide is denatured by B-mercaptoethanol O The peptide does not have a thermodynamically stable configuration O The peptide contains more than one distinct chain O The peptide contains disulfide bonds required for activity
Select statements that accurately describe receptor tyrosine kinases (RTKs). Some RTKs are dimeric in the presence of a ligand. GTPase activity is required for autophosphorylation (cross-phosphorylation). The structure includes a transmembrane helix. The intracellular domain has kinase domains. The a subunit contains seven a helices that span the membrane. A ligand binds to the extracellular domain.
Activation of phosphatidylinositol-3-kinase (PI3K) stimulate protein-protein interactions. True or False
provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)
Please note whether each protein is either a Kinase (K), ATPase (A), GTPase (G), Membrane protein (M). Some proteins may need more than one letter: Dynamin [Choose ] Porin [Choose ] EGF Receptor [Choose ] CD4 [Choose ] P-glycoprotein [Choose ] Rho [Choose ] <
When a trimeric G protein is activated by GPCR? The three subunit of the G protein remain tightly associated with each other; the GDP bound to the a subunit is phosphorylated to form bound GTP; it dissociates into a free B subunit and an ay subunit Options: hydrolyzed, cleaves, phosphorylate, dephosphorylates, folds, glycosates; gtp, gdp, cgmp, atp, adp, camp; cleaves, phosphorylation, dephosphorylation, unfolds, glcosylates, deglycosylate; leucine kinases, glycine kinase, Tyrosine kinases, valine kinase; triimetization, dimerization, monomerization
Which of the following is true of oxytocin? Multiple Choice The paraventricular nuclei are neurons where oxytocin is synthesized. Phenylalanine and arginine are the amino acids present in oxytocin. Oxytocin is essential for water conservation throughout life. Oxytocin is not a polypeptide.

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