BMSC 200 Midterm Exam Questions
with Correct Answers
What amino acids can be phosphorylated? - ANSWER-serine, threonine, tyrosine
what amino acid(s) have a sulfer group - ANSWER-methionine and cysteine
what amino acid comes around and links to the amino group - ANSWER-proline
alanine 3 letter code - ANSWER-ala
alanine single letter code - ANSWER-A
Valine (3 letter code) - ANSWER-val
Valine single letter - ANSWER-V
leucine 3 letter code - ANSWER-Leu
leucine single letter code - ANSWER-L
isoleucine 3 letter code - ANSWER-Ile
isoleucine single letter code - ANSWER-I
proline 3 letter code - ANSWER-pro
proline single letter code - ANSWER-P
methionine 3 letter code - ANSWER-met
methionine single letter code - ANSWER-m
what amino acids are one ring structures - ANSWER-tyrosine, and phenylalanine
what amino acid is a two ring structure - ANSWER-tryptophan
what is the largest amino acid - ANSWER-Tryptophan
how do you tell between larger mass of amino acids - ANSWER-what ever has an
extra hydrogen bonding group. Means its slightly more polar as well.
what are the 3 amino acids with hydroxyl group - ANSWER-tyrosine, serine,
threonine
,what happens to the 3 amino acids with extra hydroxyl groups - ANSWER-they get
post translation modification of the residues
tyrosine 3 letter code - ANSWER-tyr
tyrosine one letter code - ANSWER-Y
phenylalanine one letter code - ANSWER-F
phenylalanine 3 letter code - ANSWER-Phe
tryptophan 3 letter code - ANSWER-Trp
tryptophan one letter code - ANSWER-W
post-translational modification - ANSWER-changes made to polypeptides following
translation
what is most important in post-translation modification - ANSWER-phosphorylation in
terms of frequency and biological event
how many proteins are there compared to phosphorylation events - ANSWER-
20,000 proteins and 100,000 phosphorylation events
what adds phosphoryl groups - ANSWER-kinases
how many different kinases are there - ANSWER-516
phosphatases - ANSWER-are opposing enzymes that remove phosphoryl groups.
kinase phosphorylation - ANSWER-example of a post-translational enzymatic
modification
kinase phorylates are - ANSWER-the hydroxyl groups containing amino acids, try,
ser,thr.
reverisble modifications to control what protien doing. regulate every cellular event
this group has hydrogens but no charges on the sidechain - ANSWER-polar,
uncharged
these two amino acids can go under modification of phosphorylation of their hydroxyl
groups on their side chains - ANSWER-serine and threonine
if glutamine has one more carbon in length than asparagine who has the larger
molecular weight between the two. - ANSWER-glutamine
what are the two amino acids that have a sulfur group - ANSWER-methinine and
cystine
, what is the difference between cystine and methinine - ANSWER-cystine's sulfer
group is exposed and methinine's sufler group is not. This allows cystine to create
covalently linked disulfide bonds from 2 cystines.
why are disulfide bonds important - ANSWER-Protein stabilization and inter and intra
molecular bonding
what does adding heat do to covalent peptide bonds - ANSWER-the covalent
peptide bonds are easy to disrupt when you add heat. Thats why proteins unfold like
when you cook an egg
have people tried to fold back proteins - ANSWER-yes the ALS they used an egg
model to try and treat critical diesease.
extremophiles it is possible to? - ANSWER-stable protein structure
what can two cysteines form only when what happens - ANSWER-can form covalent
disulfide bonds only if their side chains are close together
what is an exmaple where we need a disulfide bond - ANSWER-keratin (hair nails.)
Rhinosasours has really strong disulfide bonds for their horns
what has 2 polypeptides linked covalently with disulfide bonds - ANSWER-insulin
how do disulfide bonds form - ANSWER-By the oxidation of sulfhydryl groups (two
cysteines)
can disulfide be intra or intermolecular - ANSWER-it can be both inter or intra
what amino acids have long side chains - ANSWER-lysine and arginine
why is the two amino acids positively charge - ANSWER-they end in a quindido and
methyl group which both carry a positive charge as a side chain
what amino group has the potential to be in the postively charged group and what is
the pka? - ANSWER-histidine, it ends in the enizadol group (ring structure). Pka is
around 6
with histidine what does pH>pKa mean and why - ANSWER-the ph of the cell is 7
and the emidazol pka is 6 so yeah. because hisitide has more unportanated
histodenes
what is a special ability of histidine - ANSWER-it has the ability to change
protonation
what is the difference between the two negatively charged aspartic and glutamic acid
- ANSWER-glutamate is one carbon longer longer on the side chain
with Correct Answers
What amino acids can be phosphorylated? - ANSWER-serine, threonine, tyrosine
what amino acid(s) have a sulfer group - ANSWER-methionine and cysteine
what amino acid comes around and links to the amino group - ANSWER-proline
alanine 3 letter code - ANSWER-ala
alanine single letter code - ANSWER-A
Valine (3 letter code) - ANSWER-val
Valine single letter - ANSWER-V
leucine 3 letter code - ANSWER-Leu
leucine single letter code - ANSWER-L
isoleucine 3 letter code - ANSWER-Ile
isoleucine single letter code - ANSWER-I
proline 3 letter code - ANSWER-pro
proline single letter code - ANSWER-P
methionine 3 letter code - ANSWER-met
methionine single letter code - ANSWER-m
what amino acids are one ring structures - ANSWER-tyrosine, and phenylalanine
what amino acid is a two ring structure - ANSWER-tryptophan
what is the largest amino acid - ANSWER-Tryptophan
how do you tell between larger mass of amino acids - ANSWER-what ever has an
extra hydrogen bonding group. Means its slightly more polar as well.
what are the 3 amino acids with hydroxyl group - ANSWER-tyrosine, serine,
threonine
,what happens to the 3 amino acids with extra hydroxyl groups - ANSWER-they get
post translation modification of the residues
tyrosine 3 letter code - ANSWER-tyr
tyrosine one letter code - ANSWER-Y
phenylalanine one letter code - ANSWER-F
phenylalanine 3 letter code - ANSWER-Phe
tryptophan 3 letter code - ANSWER-Trp
tryptophan one letter code - ANSWER-W
post-translational modification - ANSWER-changes made to polypeptides following
translation
what is most important in post-translation modification - ANSWER-phosphorylation in
terms of frequency and biological event
how many proteins are there compared to phosphorylation events - ANSWER-
20,000 proteins and 100,000 phosphorylation events
what adds phosphoryl groups - ANSWER-kinases
how many different kinases are there - ANSWER-516
phosphatases - ANSWER-are opposing enzymes that remove phosphoryl groups.
kinase phosphorylation - ANSWER-example of a post-translational enzymatic
modification
kinase phorylates are - ANSWER-the hydroxyl groups containing amino acids, try,
ser,thr.
reverisble modifications to control what protien doing. regulate every cellular event
this group has hydrogens but no charges on the sidechain - ANSWER-polar,
uncharged
these two amino acids can go under modification of phosphorylation of their hydroxyl
groups on their side chains - ANSWER-serine and threonine
if glutamine has one more carbon in length than asparagine who has the larger
molecular weight between the two. - ANSWER-glutamine
what are the two amino acids that have a sulfur group - ANSWER-methinine and
cystine
, what is the difference between cystine and methinine - ANSWER-cystine's sulfer
group is exposed and methinine's sufler group is not. This allows cystine to create
covalently linked disulfide bonds from 2 cystines.
why are disulfide bonds important - ANSWER-Protein stabilization and inter and intra
molecular bonding
what does adding heat do to covalent peptide bonds - ANSWER-the covalent
peptide bonds are easy to disrupt when you add heat. Thats why proteins unfold like
when you cook an egg
have people tried to fold back proteins - ANSWER-yes the ALS they used an egg
model to try and treat critical diesease.
extremophiles it is possible to? - ANSWER-stable protein structure
what can two cysteines form only when what happens - ANSWER-can form covalent
disulfide bonds only if their side chains are close together
what is an exmaple where we need a disulfide bond - ANSWER-keratin (hair nails.)
Rhinosasours has really strong disulfide bonds for their horns
what has 2 polypeptides linked covalently with disulfide bonds - ANSWER-insulin
how do disulfide bonds form - ANSWER-By the oxidation of sulfhydryl groups (two
cysteines)
can disulfide be intra or intermolecular - ANSWER-it can be both inter or intra
what amino acids have long side chains - ANSWER-lysine and arginine
why is the two amino acids positively charge - ANSWER-they end in a quindido and
methyl group which both carry a positive charge as a side chain
what amino group has the potential to be in the postively charged group and what is
the pka? - ANSWER-histidine, it ends in the enizadol group (ring structure). Pka is
around 6
with histidine what does pH>pKa mean and why - ANSWER-the ph of the cell is 7
and the emidazol pka is 6 so yeah. because hisitide has more unportanated
histodenes
what is a special ability of histidine - ANSWER-it has the ability to change
protonation
what is the difference between the two negatively charged aspartic and glutamic acid
- ANSWER-glutamate is one carbon longer longer on the side chain
