UW Bio 200 Exam 1 Questions and
Answers
5 core concepts - ANS--information flow
-structure function
-energy transformation
-evolution
-systems
amino acid polarity - ANS-
electronegativities of organic atoms - ANS-C~H<N<O
How to tell if a molecule is hydrophobic or hydrophilic - ANS-Non-polar: hydrophobic
Polar: hydrophilic
Types of bonds and stored potential energy - ANS-High to low
Covalent bonds:
peptide
disulfide bridge:
Ionic Bonds:
Hydrophobic interactions:
Hydrophilic interactions:
H bonds
ribosome - ANS-site of protein synthesis
tRNA - ANS-transfer RNA; type of RNA that carries amino acids to the ribosome
ribosome E, P, and A sites - ANS-E: exit site
P: holds tRNA with growing polypeptide chain
A: holds aminoacyl tRNA (acceptor site)
ribosome binding site - ANS-a sequence of nucleotides upstream of the start codon of
an mRNA transcript that is responsible for the recruitment of a ribosome during the
initiation of protein translation
codon/anti-codon - ANS-A codon is a three-base sequence (three nitrogen bases in a
row) on mRNA. It calls for a specific amino acid to be brought to the growing
polypeptide. An anticodon is a three-base sequence on tRNA. It matches the codon.
, release factor - ANS-Proteins that can trigger termination of RNA translation when a
ribosome reaches a stop codon.
start codon/stop codon - ANS-A codon that either starts or stops the transcription
process
Start: AUG (met)
Stop: UAA UAG UGA
amino acid - ANS-Building blocks of protein
aminoacyl tRNA synthetase - ANS-During protein synthesis, an enzyme that attaches
the correct amino acid to a tRNA molecule to form a "charged" aminoacyl-tRNA.
translocation of the ribosome - ANS-simultaneous movement of two tRNAs with the
mRNA by one codon
levels of protein structure - ANS-primary, secondary, tertiary, quaternary
peptide synthesis - ANS-condensation reaction of the upstream carboxyl group of one
amino acid to the downstream amino group of another
how to identify potential for hydrogen bond formation between R groups, amino groups
and carbonyl groups - ANS-sharing of a hydrogen atom covalently attached to an
electronegative element (typically O-H and N-H groups) between a lone pair of
electrons on another electronegative element
impact of different types of mutations on protein structure - ANS--Silent mutation: when
a mutation occurs but it has no effect on the protein. multiple codons may result to the
same amino acid
Missense mutation: when the substitution results to a different amino acid
Nonsense mutation: when a stop codon replaces what is supposed to be a codon for an
amino acid. When a stop codon is reached, the translation is stopped prematurely and
the protein is not formed.
Frameshift mutation: when an extra nucleic acid is inserted or deleted. This has severe
effects as it will not only change one amino acid, but the rest of the remaining amino
acids will be affected.
impact of changes in protein structure on function - ANS-Gain/change of function: a
mutation could increase the function of a protein, or it could also acquire a new function
due to changes in its amino acid sequence
Loss of function: The change in at a single point could affect the entire function of the
protein. For instance, a single change can remove the ability of a receptor to bind to it. It
is also possible that a change in some residues would change the polarity of the protein,
and hence reduce its function. Nonsense mutations essentially stop protein synthesis
prematurely.
Answers
5 core concepts - ANS--information flow
-structure function
-energy transformation
-evolution
-systems
amino acid polarity - ANS-
electronegativities of organic atoms - ANS-C~H<N<O
How to tell if a molecule is hydrophobic or hydrophilic - ANS-Non-polar: hydrophobic
Polar: hydrophilic
Types of bonds and stored potential energy - ANS-High to low
Covalent bonds:
peptide
disulfide bridge:
Ionic Bonds:
Hydrophobic interactions:
Hydrophilic interactions:
H bonds
ribosome - ANS-site of protein synthesis
tRNA - ANS-transfer RNA; type of RNA that carries amino acids to the ribosome
ribosome E, P, and A sites - ANS-E: exit site
P: holds tRNA with growing polypeptide chain
A: holds aminoacyl tRNA (acceptor site)
ribosome binding site - ANS-a sequence of nucleotides upstream of the start codon of
an mRNA transcript that is responsible for the recruitment of a ribosome during the
initiation of protein translation
codon/anti-codon - ANS-A codon is a three-base sequence (three nitrogen bases in a
row) on mRNA. It calls for a specific amino acid to be brought to the growing
polypeptide. An anticodon is a three-base sequence on tRNA. It matches the codon.
, release factor - ANS-Proteins that can trigger termination of RNA translation when a
ribosome reaches a stop codon.
start codon/stop codon - ANS-A codon that either starts or stops the transcription
process
Start: AUG (met)
Stop: UAA UAG UGA
amino acid - ANS-Building blocks of protein
aminoacyl tRNA synthetase - ANS-During protein synthesis, an enzyme that attaches
the correct amino acid to a tRNA molecule to form a "charged" aminoacyl-tRNA.
translocation of the ribosome - ANS-simultaneous movement of two tRNAs with the
mRNA by one codon
levels of protein structure - ANS-primary, secondary, tertiary, quaternary
peptide synthesis - ANS-condensation reaction of the upstream carboxyl group of one
amino acid to the downstream amino group of another
how to identify potential for hydrogen bond formation between R groups, amino groups
and carbonyl groups - ANS-sharing of a hydrogen atom covalently attached to an
electronegative element (typically O-H and N-H groups) between a lone pair of
electrons on another electronegative element
impact of different types of mutations on protein structure - ANS--Silent mutation: when
a mutation occurs but it has no effect on the protein. multiple codons may result to the
same amino acid
Missense mutation: when the substitution results to a different amino acid
Nonsense mutation: when a stop codon replaces what is supposed to be a codon for an
amino acid. When a stop codon is reached, the translation is stopped prematurely and
the protein is not formed.
Frameshift mutation: when an extra nucleic acid is inserted or deleted. This has severe
effects as it will not only change one amino acid, but the rest of the remaining amino
acids will be affected.
impact of changes in protein structure on function - ANS-Gain/change of function: a
mutation could increase the function of a protein, or it could also acquire a new function
due to changes in its amino acid sequence
Loss of function: The change in at a single point could affect the entire function of the
protein. For instance, a single change can remove the ability of a receptor to bind to it. It
is also possible that a change in some residues would change the polarity of the protein,
and hence reduce its function. Nonsense mutations essentially stop protein synthesis
prematurely.
