Hello,
a)Covalent modifications are used mainly to alter the activity of a protein.The two most common types of reversible covalent modification of proteins used for regulation are acetylation and phosphorylation.For example acetylation oh histone(Proteins used for packaging of DNA).
b)Active form of chymotrysin is formed when disulfide bond between arginie-15 and isoleucine-16 present in chymotrypsinogen is cleaved by the enzyme trypsin.
Hope this helps.
Regulation a) Please list two types of reversible covalent modification of proteins used for regulation b)...
thats all the information that he gave us to solve the question. Thank you for trying anyways X C E Question 23 1 pts The free-energy changes for the transfer of individual amino acid residues from a hydrophobic to an aqueous environment are given as follows: Amino acid AG of transfer (kJ/mol Proline -0.8 -12.6 Histidine 6.7 Alanine Methionine 14.3 Based on this information, which of these amino acid pairs is MOST likely to be represented in membrane-spanning alpha helices?...
1. According to the paper, what does lactate dehydrogenase (LDH) do and what does it allow to happen within the myofiber? (5 points) 2. According to the paper, what is the major disadvantage of relying on glycolysis during high-intensity exercise? (5 points) 3. Using Figure 1 in the paper, briefly describe the different sources of ATP production at 50% versus 90% AND explain whether you believe this depiction of ATP production applies to a Type IIX myofiber in a human....