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Questions in Proteins and Enzymes
Page 1 out of 11 Pages
- If an R group on an amino acid is charged positive or negative, does the entire amino acid have that charge? Would aspartic acid have a negative charge and lysine have a positive charge?(19737 views)
- Can you please further explain how secondary structure of Proteins really works? On the slides is says that the folding occurring in the second structure is independent of R groups...what does that mean? And finally could you please explain the main difference in the folding between the secondary and tertiary structure.(21576 views)
- It says in the Purves textbook on page 41, under "The Primary structure of a protein is its amino acid sequence" that: The peptide backbone of this primary structure consists of a repeating sequence of three (-N-C-C-): the N from the amino group, the alpha carbon, and the C from the carboxl group of each amino acid. I dont remember you mentioning anything about this carbon in the middle being an "Alpha" carbon. Is this "alpha" title important, or should we just recognize that it is a carbon in the middle of each amino acid.(21547 views)
- I know that proteins are put together by condensation reactions, however, I am confused about the N --> C direction complex. When an N terminus and C terminus are combined, which way are more added on? I heard in class that you only add the incoming amino to carboxyl-terminus. So would the addition be: C<--N-C(20668 views)
- I think Im just misinterpreting information, or possibly over thinking the structures of proteins- nevertheless, from the readings in the book I got the idea that for a protein to function in a certain way it had to go through all four folding stages (i.e. the way a protein is folded determines what it does). However, in lecture on friday, we talked about how many proteins stop at various levels of structures. If that is the case, then what do proteins do at the primary structure or secondary structure?(18239 views)
- With all these different side chains, the "basic" and "acidic" side chains are throwing me off. How can you recognize either one?(18420 views)
- I was wondering, in the enzyme, is the binding site where the noncompetitive inhibitor the same as the allosteric site for allosteric inhibitors?(18008 views)
- From the notes: Catabolic (E-releasing) reactions require a certain amount of energy to get started. -Could come from heat but why not? (I'm confused by this sentence. could you explain once again?)(17886 views)
- Regarding amino acid R groups, hydrophobic non-polar groups should only have C-H bonds? When the bond contains O, is it polar?(18135 views)
- Are we required to memorize the the structures of all 20 amino acids? Or is there an easier way?(181397 views)
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