proteins
1. What are proteins? How can
the proteindiversity of living
beings beexplained?
2. What is the importance of
proteins for living beings?
3. What is the constitutional
unit of proteins?
4. What is an oligopeptide?
How is it different from a
polypeptide?
5. How many are the known
amino acids that form proteins
in living beings?
6. Does every amino acid have
a central carbon? To which
organic group is that central
carbon bound?
7. How can amine groups be
classified?
8. What is the structural
representation of a carboxyl
group?
9. What is the structural flat
representation of an amino
acid molecule?
10.What is the importance of
the –R group (variable
radical) in an amino acid
molecule?
11.How can the binding of
twoaminoacidsfor the
peptideformationbe
described?
12. What is the binding
between two amino acids
called?
13. Do the –R groups bound to
the central carbons participate
in the union between amino
acids?
14. Do the –H groups bound to
the central carbons participate
in the peptide bond?
15. Do the amine and the
carboxyl groups attached to
central carbons participate in
the union between amino
acids?
16. Does the chemical reaction
to unite amino acids
incorporate or liberate atoms?
What are the chemical entities
incorporated or liberated in
this reaction?
17. Are there different
proteins made by the same
total number of amino acids?
18. Are proteins with the
same number of each different
amino acid that form them
necessarily identical proteins?
19. What is the essential
condition for a protein to be
identical to another protein?
20. What is the primary
structure of a protein? What is
the importance of the primary
structure?
21. What is the secondary
structure of a protein?
22. What is the difference
between the alpha-helix and
the beta-sheet protein
conformations?
23. What is the tertiary
structure of a protein? What
are the main types of tertiary
structure?
24. What is the quaternary
structure of a protein? Do all
proteins have quaternary
structure?
25. What is protein
denaturation? Is there any
change in the primary
structure when a protein is
denatured?
26. How can denaturation be
classified regarding its
reversibility?
27. What are some factors
that can lead to protein
denaturation?
28. Is it expected that a
change in the primary, in the
secondary or in the tertiary
structure of a protein will
produce more functional
consequences?
29. In sicklecell anemia, a
hereditary disease,there is
substitution of one amino acid
by another in one of the four
polypeptide chains of
hemoglobin. In this case are
all of the structural levels of
the protein modified?
30. What is the difference
between essential and natural
amino acids?
31. What are respectively
some remarkable functions of
myosin, CD4, albumin, keratin,
immunoglobulin, reverse
transcriptase, hemoglobin and
insulin?