BIO 201 CHAPTER 2
1. amino acid structure: a carboxyl group, amine group, and R group
2. peptide bond: The chemical bond that forms between the carboxyl group of oneamino acid
and the amino group of another amino acid
3. conformation of protein: the spatial arrangement of atoms in a protein or anypart of a
protein
4. denaturation of protein: disrupts the secondary, tertiary, or quaternary struc-ture of a
protein
5. primary protein structure: sequence of a chain of amino acids
6. secondary protein structure: coiling or folding of a polypeptide due to H-bond-ing between
amino acids
alpha helix or beta pleated sheet
7. tertiary protein structure: 3D folding pattern of a protein due to side chaininteractions
8. quaternary protein structure: 2+ protein chains forming functional protein
9. fibrous protein: slender filaments, better suited for roles in muscle contractionand skin
strengthening
10. globular proteins: these are compact, embedded in cell membrane, movefreely in bodily
fluid
11. enzyme: protein that acts as a biological catalyst
12. catalyst: substance that speeds up the rate of a chemical reaction
13. enzyme actions: speeds up chemical reactions in the cell (make,break,changebonds)
14. enzyme regulation: temperature and pH (very sensitive!)
15. nucleic acid function/structure: made from nucleotides, store and transfergenetic
information
16. nucleotide structure: 5 carbon sugar, phosphate group, nitrogenous base
17. DNA nitrogenous bases: Adenine, Thymine, Cytosine, Guanine
18. RNA nitrogenous bases: Adenine, Uracil, Guanine, Cytosine
19. ATP Structure: adenine, ribose, 3 phosphate groups
20. ATP Purpose in Body: energy storage and transferpowering cellular processes
recyclable energy carrier
21. DNA v. RNA: DNA is a double-stranded molecule that stores genetic informa-tion, using
the bases adenine, thymine, cytosine, and guanine.
1. amino acid structure: a carboxyl group, amine group, and R group
2. peptide bond: The chemical bond that forms between the carboxyl group of oneamino acid
and the amino group of another amino acid
3. conformation of protein: the spatial arrangement of atoms in a protein or anypart of a
protein
4. denaturation of protein: disrupts the secondary, tertiary, or quaternary struc-ture of a
protein
5. primary protein structure: sequence of a chain of amino acids
6. secondary protein structure: coiling or folding of a polypeptide due to H-bond-ing between
amino acids
alpha helix or beta pleated sheet
7. tertiary protein structure: 3D folding pattern of a protein due to side chaininteractions
8. quaternary protein structure: 2+ protein chains forming functional protein
9. fibrous protein: slender filaments, better suited for roles in muscle contractionand skin
strengthening
10. globular proteins: these are compact, embedded in cell membrane, movefreely in bodily
fluid
11. enzyme: protein that acts as a biological catalyst
12. catalyst: substance that speeds up the rate of a chemical reaction
13. enzyme actions: speeds up chemical reactions in the cell (make,break,changebonds)
14. enzyme regulation: temperature and pH (very sensitive!)
15. nucleic acid function/structure: made from nucleotides, store and transfergenetic
information
16. nucleotide structure: 5 carbon sugar, phosphate group, nitrogenous base
17. DNA nitrogenous bases: Adenine, Thymine, Cytosine, Guanine
18. RNA nitrogenous bases: Adenine, Uracil, Guanine, Cytosine
19. ATP Structure: adenine, ribose, 3 phosphate groups
20. ATP Purpose in Body: energy storage and transferpowering cellular processes
recyclable energy carrier
21. DNA v. RNA: DNA is a double-stranded molecule that stores genetic informa-tion, using
the bases adenine, thymine, cytosine, and guanine.
