BCH exam 1 Question and answers verified to pass 2025
1. Catabolism energy releasing
2. Anabolism energy using
3. free energy (delta G) Direction of reactions as they go toward equilibrium
4. negative free energy change spontaneous, exergonic
5. Delta G nought -RTlnKeq
6. Non spontaneous reactions do not occur on their own and require an input of
energy
7. enzyme effect on energy Lower the activation energy
8. dipole moment separation and magnitude of the charges in polar
molecules
9. hydrophobic effect tendency of nonpolar substances to aggregate in aqueou
solution and exclude water molecules
10. entropy of water increases as ordered crystal lattice is dissolved (ice —>
water)
11. hydrogen bonding strong type of intermolecular dipole-dipole attraction. Occu
between hydrogen and F, O or N
12. Biological Relevance of -hydroxyl group of an alcohol and water
Hy- drogen Bonds
-between peptide groups in polypeptides
-between complementary bases of DNA
13. ionization of water H2O --> H+ + OH-
14. equilibrium constant Keq = [H+][OH-]/[H2O]
equa- tion
15. pH formula -log[H+]
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,BCH exam 1 Question and answers verified to pass 2025
16. buffering capacity the ability of a substance to resist changes in pH
17. When is buffering pH = pKa
capacity greatest?
18. Buffer systems in vivo
are based on phosphate, bicarbonate, histidine
19. Acidosis pH < 7.35
20. Alkalosis pH > 7.45
21. Blood pH buffers plasma proteins, hemoglobin, and carbonic acid
22. non-chiral amino acid Glycine
23. Almost all AAs are in this form L-form
24. non polar amino acids hydrophobic
25. polar amino acids serine, threonine, asparagine, glutamine, cysteine
26. aromatic amino acids phenylalanine, tyrosine, tryptophan
27. charged amino acids aspartate, glutamate, lysine, arginine, histidine
28. The amino acid with a Histidine
pKa near neutral pH
29. Reversible Modifications
of Amino Acids phosphorylation, methylation, acetylation
30. At acidic pH, the
carboxyl group is
and the protonated, cationic
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,BCH exam 1 Question and answers verified to pass 2025
amino acid is in the
form.
31. At neutral pH, the deprotonated, protonated
carboxyl group is but
the amino group is .
32. At basic pH the amino acid
is in this form Anionic
33. when does a zwitterion
pre- dominate? neutral pH
34. Ionizable Amino Acids DR CHEKY
35. protein synthesis is Requires activation with ATP
unfavor- able
36. peptide functions hormones, neuropeptides, antibiotics, protection
37. Cofactors nonprotein enzyme helpers (metal ions or organic
molecules)
38. Coenzymes organic cofactors (NAD+)
39. Prosthetic groups cofactors that bind to the enzyme by strong covalent bon
40. gel filtration chromatography separated based on size, larger ones elute first
41. anion exchange anions stick to sides (cations elute first)
42. cation exchange cations stick to sides (anions elute first)
43. affinity chromatography Protein of interest is eluted by ligand solution
44. Ni-NTA nickel nitrilotriacetate, an aflnity ligand for His-tagged
proteins
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1. Catabolism energy releasing
2. Anabolism energy using
3. free energy (delta G) Direction of reactions as they go toward equilibrium
4. negative free energy change spontaneous, exergonic
5. Delta G nought -RTlnKeq
6. Non spontaneous reactions do not occur on their own and require an input of
energy
7. enzyme effect on energy Lower the activation energy
8. dipole moment separation and magnitude of the charges in polar
molecules
9. hydrophobic effect tendency of nonpolar substances to aggregate in aqueou
solution and exclude water molecules
10. entropy of water increases as ordered crystal lattice is dissolved (ice —>
water)
11. hydrogen bonding strong type of intermolecular dipole-dipole attraction. Occu
between hydrogen and F, O or N
12. Biological Relevance of -hydroxyl group of an alcohol and water
Hy- drogen Bonds
-between peptide groups in polypeptides
-between complementary bases of DNA
13. ionization of water H2O --> H+ + OH-
14. equilibrium constant Keq = [H+][OH-]/[H2O]
equa- tion
15. pH formula -log[H+]
1/
21
,BCH exam 1 Question and answers verified to pass 2025
16. buffering capacity the ability of a substance to resist changes in pH
17. When is buffering pH = pKa
capacity greatest?
18. Buffer systems in vivo
are based on phosphate, bicarbonate, histidine
19. Acidosis pH < 7.35
20. Alkalosis pH > 7.45
21. Blood pH buffers plasma proteins, hemoglobin, and carbonic acid
22. non-chiral amino acid Glycine
23. Almost all AAs are in this form L-form
24. non polar amino acids hydrophobic
25. polar amino acids serine, threonine, asparagine, glutamine, cysteine
26. aromatic amino acids phenylalanine, tyrosine, tryptophan
27. charged amino acids aspartate, glutamate, lysine, arginine, histidine
28. The amino acid with a Histidine
pKa near neutral pH
29. Reversible Modifications
of Amino Acids phosphorylation, methylation, acetylation
30. At acidic pH, the
carboxyl group is
and the protonated, cationic
2/
21
,BCH exam 1 Question and answers verified to pass 2025
amino acid is in the
form.
31. At neutral pH, the deprotonated, protonated
carboxyl group is but
the amino group is .
32. At basic pH the amino acid
is in this form Anionic
33. when does a zwitterion
pre- dominate? neutral pH
34. Ionizable Amino Acids DR CHEKY
35. protein synthesis is Requires activation with ATP
unfavor- able
36. peptide functions hormones, neuropeptides, antibiotics, protection
37. Cofactors nonprotein enzyme helpers (metal ions or organic
molecules)
38. Coenzymes organic cofactors (NAD+)
39. Prosthetic groups cofactors that bind to the enzyme by strong covalent bon
40. gel filtration chromatography separated based on size, larger ones elute first
41. anion exchange anions stick to sides (cations elute first)
42. cation exchange cations stick to sides (anions elute first)
43. affinity chromatography Protein of interest is eluted by ligand solution
44. Ni-NTA nickel nitrilotriacetate, an aflnity ligand for His-tagged
proteins
3/
21
