Define the following terms:a. proproteinb. preproproteinc. disulfide exchanged. proline hydroxylatione. proteolytic cleavage

Digoxin, a toxin derived from the foxglove (shown), can be used to treat heart disorders such as atrial fibrillation. Digoxin's mechanism of action is to inhibit the Na+/K+ ATPase. Which of the following is the most likely side effect of Digoxin treatment? O Failure to transport glucose into cells while fasting (not eating) O Failure to transport Ht into lysosomes using direct active transport O Failure to transport glucose into cells after a meal O Failure to secrete pancreatic digestive enzymes in response to eating

Why are proteins unfolded in order to enter the mitohondria during post-translational transport? Which transport proteins do they enter through? Is it a receptor? Does it take energy to bring the unfolded protein in? What kind of proteins are brought into the mitochondria and why? Also, why are the proteins folded back up once it enters the mitochindria? Please help me understand this a little bit better...Thank you

Which of the following is an example of an unacceptable missense? a. HbA is converted to Hb Hikari, where the beta chain Lysine at #61 is replaced by Asparagine.   b. Hb A, is converted to Hb M (Boston) where the alpha chain Histidine at #58 is replaced by Tyrosine.   c. Hb A is converted to Hb S, where the beta chain Glutamate at #6 is replaced by Valine.

Lysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified as a(an) O A. salt bridge, oxidoreductase O B. peptide bond; hydrolase OC. glycosidic linkage; oxidoreductase O D. glycosidic linkage, hydrolase O E. peptide bond; transferase

Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…

If X: is a nucleophile that attacks ATP, use arrows to show the location of attack and draw the structure of the products of a phosphorylation reaction with ATP (do not draw the adenosine portion, but simply use the word “adenosine” in your structure.

Describe the importance of ubiquitin-dependent degradation of soluble proteins.

The nuclear import of proteins larger than 40 kDa requires the presence of what amino acid sequence? Describe the mechanism of nuclear import. How are nuclear transport receptors able to get through the nuclear pore complex?

To examine: Whether the statement "protein tyrosine phosphatases display exquisite specificity for their substrates, unlike most serine/threonine protein phosphatases, which have rather broad specificity" is true or false.