BRAINSCAPE1
Bio 2100 Exam 1 review (UVA) Exam with
complete solutions latest version
1. Rules of hydrophobia/philia: 1. Depends on the R group!!!!
2. If a side chain has a charge it is hydrophilic
3. If there is polar covalent bonds in the side-chain it is hydrophilic
a. O > N > C = H
4. If primarily carbon-hydrogen (non-polar covalent) it is hydrophobic
a. Also generally very long-side note: non-polar look for CH, polar look for O or N in groups, charges will say + or -
2. Monomer: the subunit that serves as the building block of a polymer
3. Residue: a monomer that is now a polymer is referred to as a residue
4. Peptide: short chain of amino acids
5. Polypeptide: long chain of amino acids
6. Protein: A biologically functional molecule consisting of one or more polypeptides folded or coiled into a specific
3-dimensional structure
7. Hydrolosis: A chemical reaction that breaks bonds between two molecules by the addition of water; functions
in disassembly of polymers to monomers.
8. Dehydration: A chemical reaction in which two molecules become covalently bonded to each other with the
removal of a water
9. Chaperone proteins: Ensure proper folding, fixes improper folding protect protein, protect protein,
prevent problems/restoration of function
Interact w proteins that are not properly folded, helps them achieve proper folding, does not determine what the proper
folding is
DO NOT dictate function
10. Primary protein structure: The level of protein structure referring to the specific linear sequence of
amino acids
, BRAINSCAPE1
11. secondary protein structure: Reregions of repetitive coiling or folding of the polypeptide backbone
of the protein due to hydrogen bonding between the constituents of the backbone (not the side chains)
12. Tertiary protein structure: the overall shape of a protein molecule due to interactions of amino acid
side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges
13. Quarternary protein structure: the particular shape of a complex, aggregate protein, defined by the
characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide
14. Glycoprotein: A protein with one or more covalently attached carbohydrates
15. Cytosol: Dense protein solution that membrane bound compartments sit/float in
16. Cytoplasm: Everything within plasma membrane except nucleus
Bio 2100 Exam 1 review (UVA) Exam with
complete solutions latest version
1. Rules of hydrophobia/philia: 1. Depends on the R group!!!!
2. If a side chain has a charge it is hydrophilic
3. If there is polar covalent bonds in the side-chain it is hydrophilic
a. O > N > C = H
4. If primarily carbon-hydrogen (non-polar covalent) it is hydrophobic
a. Also generally very long-side note: non-polar look for CH, polar look for O or N in groups, charges will say + or -
2. Monomer: the subunit that serves as the building block of a polymer
3. Residue: a monomer that is now a polymer is referred to as a residue
4. Peptide: short chain of amino acids
5. Polypeptide: long chain of amino acids
6. Protein: A biologically functional molecule consisting of one or more polypeptides folded or coiled into a specific
3-dimensional structure
7. Hydrolosis: A chemical reaction that breaks bonds between two molecules by the addition of water; functions
in disassembly of polymers to monomers.
8. Dehydration: A chemical reaction in which two molecules become covalently bonded to each other with the
removal of a water
9. Chaperone proteins: Ensure proper folding, fixes improper folding protect protein, protect protein,
prevent problems/restoration of function
Interact w proteins that are not properly folded, helps them achieve proper folding, does not determine what the proper
folding is
DO NOT dictate function
10. Primary protein structure: The level of protein structure referring to the specific linear sequence of
amino acids
, BRAINSCAPE1
11. secondary protein structure: Reregions of repetitive coiling or folding of the polypeptide backbone
of the protein due to hydrogen bonding between the constituents of the backbone (not the side chains)
12. Tertiary protein structure: the overall shape of a protein molecule due to interactions of amino acid
side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges
13. Quarternary protein structure: the particular shape of a complex, aggregate protein, defined by the
characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide
14. Glycoprotein: A protein with one or more covalently attached carbohydrates
15. Cytosol: Dense protein solution that membrane bound compartments sit/float in
16. Cytoplasm: Everything within plasma membrane except nucleus
