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Questions in Proteins and Enzymes
Page 7 out of 11 Pages
- Positively charged R-groups are categorized as basic. When discussing the electrochemical gradient in a more recent lecture, the area of more positive charged has a lower pH. This indicates that this area is more ACIDIC. Why does a higher concentration of H+ make the intermembrane space more acidic? Also, how does this compare to the positively charged R-groups mentioned above in the earlier lecture on proteins? (6150 views)
- If you had to rank the primary stabilizing forces from strongest to weakest(according to how easily they are broken) what would the order be? (5423 views)
- what should we know about the protein subunits homodimer and heterodimer? (5887 views)
- If spontaneous reactions are always-or generally-catabolic, are catabolic reactions spontaneous? (7047 views)
- What are Van der Waals forces used for in a protein? (5684 views)
- What are the conditions for proteins (at the tertiary level) that lead to the formation of hydrogen bonds versus ionic bonds versus hydrophobic interactions? (5400 views)
- We know enzymes don't speed up the equilibrium of a reaction, and they work the same for the forward and reverse reaction. Does it mean that they lower the Activation Energy for each reaction, because if they worked the same for each one, couldn't they theoretically just take what they just created, and make it back into what they started with?(6149 views)
- When a protein gets denatured, does the disulfide bridge get broken too?
Isn't the disulfide bridge like a covalent bond, and in class, I remember
hearing that covalent bonds are like the strongest bond out of all the bonds
that we learned so far.(15385 views)
- Can condensation and hydrolysis reactions be considered as examples of anabolism
and catabolism, respectively?
(7496 views)
- Is the hydrophobic effect only a stabilization factor for tertiary structures?
Also, do we need to know which stability factors are predominantly associated
with which structures? (5859 views)
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