If a Primary Structure of a protein contained charged areas and hypdrophobic areas, describe how that protein would fold. What would happen if the DNA was damaged and a hydrophic amino acid was substituted for a charged amino acid?

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Related questions

Look at your table of amino acid R-group structures. Which category amino acids are likely to change physical and/or chemical properties if the pH of the surrounding medium changes?

Polar, non charged amino acids.

Basic amino acids.

Non-polar amino acids.

Look at your amino acid structure tables. What category of amino acid is histidine?

basic

non-polar

polar, non-charged

How would Bronsted-Lowry describe histidine?

proton acceptor

proton donor

1. Amino acid changes in the primary structure of the protein arenot capable of causing changes in the
overall shape of a protein.
a.) True
b.) False

2. An alpha helix:
a.) is destabilized by the amino acid alanine
b.) can only form by hydrogen bonding between different polypeptidechains
c.) can only form when cysteines form disulfide bridges within thisstructure
d.) all of the above
e.) none of the above

3. What will likely happen if two aspartates at pH 5 are next toeach other in a polypeptide chain?
a.) The side chains of these amino acids will be uncharged andthere will be no effect.
b.) The side chains of these amino acids will be charged and theywill attract each other.
c.) The side chains of these amino acids will be charged and theywill repel each other.
d.) Not enough information is given to determine the effect.

4. Consider the amino acid phenylalanine. Which of the followingbest describes where you predict this
amino acid would be found?
a.) This amino acid is hydrophobic and would be on the surface of aprotein that is in the middle
of a membrane.
b.) This amino acid is hydrophilic and would be on the surface of aprotein that is in the middle
of a membrane.
c.) This amino acid is hydrophobic and would be in the interior ofa protein that is in the middle
of a membrane.
d.) This amino acid is hydrophilic and would be in the interior ofa protein that is in the middle of
a membrane.
e.) Not enough information is given to determine.

5. The difference between fetal and adult hemoglobin with regard tooxygen binding occurs because fetal
hemoglobin has an amino acid substitution in one of its chains thatresults in a histidine being replaced by a
serine.
a.) True
b.) False

Assuming that the mutations are adaptive, how would that affect the stability of a protein at low and high temperatures?

Given:

1) Glutamine to lysine in a warm adapted species.Glutamine is uncharged while lysine is positively charged, therefore there would likely be a change as an uncharged amino acid is being replaced with positively charged amino acid.

2) Threonine to Alanine in a warm adapted species. Threonine is polar uncharged while Alanine is hydrophobictherefore there would likely be a change, as a polar charged amino acid is being replaced with a hydrophobic amino acid.

3) Glutamic acid to aspartic acid in a cold adapted species. Both Aspartic acid to Glutamic acid are negatively charged, therefore, there would likely be no effect with this change as both are negatively charged amino acids.

4) Glycine to alanine in a warm adapted species. Both Glycine to Alanine are non polar amino acids, therefore the change would likely have no effect as both are non polar and hydrophobic.