1.) Fill In The Blank. In three separate site-directed mutagenesis experiments,
ID: 205429 • Letter: 1
Question
1.) Fill In The Blank. In three separate site-directed mutagenesis experiments, scientists altered a Lys residue in corn PEP carboxylase to an Asn, Glu, or Arg. The substitution that you would expect to have the least effect on enzymatic activity would be ______ because it, like Lys, is ______ charged at physiological pH. The substitution that you would expect to have the most effect on enzymatic activity would be ______ because it is _____ charged at physiological pH. (Use structure tables if you need to.)
2.) Mutations in the genes for a hemoglobin or chain
a.) May cause anemia
b.) May decrease O2 binding
c.) May increase O2 binding
d.) All of the above
3.) Myoglobin, globin, and globin have similar structures because
a.) They all bind oxygen
b.) They have almost identical amino acid sequences
c.) They are cooperative proteins
d.) They evolved from a common ancestor
4.) The aggregation of a misfolded protein may lead to
a.) The accumulation of starch
b.) Nerve cell regeneration
c.) A neurodegenerative disease
d.) A bacterial infection
5.) The amino acid shown here has a _____ side chain.
a.) Polar
b.) Charged
c.) Hydrophobic
d.) Cannot be determined with the information provided
OH HCCH3Explanation / Answer
1.) The substitution that you would expect to have the least effect on enzymatic activity would be __Arg____ because it, like Lys, is ___positively ___ charged at physiological pH. The substitution that you would expect to have the most effect on enzymatic activity would be ___Glu___ because it is __Negatively___ charged at physiological pH.
2) may cause a decrease in binding of oxygen
3) They have almost identical amino acids which makes them similar in structure.
4) The aggregation of a misfolded protein may lead to A neurodegenerative disease
5) Polar uncharged amino acid because it is Threonine amino acid structure.
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