Access Millions of academic & study documents

Cell Bio

Content type
User Generated
Subject
Biology
School
Benedictine College
Type
Homework
Showing Page:
1/3
1. The hydrophobic amino acids Leu, Phe, Val, Ile, and Met are more likely to be in the
interior of a protein than the polar amino acids Ser, Ser-p, Lys, Gln, His, and Glu. The
polar amino acids are likely to be present on the outer surface of the protein exposed
to the outside environment.
2. A. This statement is true. The active site is made up of only a few amino acid side
chains. The rest of the protein is needed to keep the polypeptide chain in place, offer
additional binding sites for regulatory functions, and help the protein find its way
about the cell.
B. This statement is false. The electromagnetic interactions between molecules were
distributed in non-covalent interactions. These bonds are distinct from covalent bonds
in that they do not share electrons. The stability of macromolecules is dependent on
interactions like this. Electrostatic interactions, tiny pi effects, Vander Waal's forces,
and hydrophobic effects are all types of interactions.
c. This statement is true. Because substrate must fit in the active site of an enzyme and
allow for proper positioning of the substrate to form an enzyme-substrate complex,
the active site of an enzyme occupies a small portion of the enzyme.
d. This statement is true. Because catalysis includes the creation of covalent bonds,
This increases the number of covalent intermediates in the reaction and lowers the
energy of later transition states.
E. There may be more than two allosteric sites where effectors bind and trigger an
enzyme conformational shift, hence there may be more than two binding sites. Thus,
this statement is true.
F. This statement is false. Only a few amino acid side chains make up the active site.
The remainder of the protein is required to retain the polypeptide chain in place,

Sign up to view the full document!

lock_open Sign Up
Showing Page:
2/3
provide additional binding sites for regulatory functions, and aid in the protein's
movement around the cell.
3. A. If the product inhibits Enzyme B, even then the reaction will stop and the end
product will cease its formation. However, I don’t think this is energetically
favorable, because the product binds with the enzyme A, and changes its
conformation such that the starting substrate can’t bind to the enzyme hence, stopping
the reaction. This can’t be the same for enzyme B as it does not interact with the
starting substrate.
b. This would increase the production of the end product as it will increase the
attraction between the enzyme and the starting substrate. This will also deplete the
starting substrate. This reaction can be energetically favorable as the end product acts
as a catalyst.
c. This condition will lead to equilibrium, The positive effector will enhance the
activity of the enzyme and the end product will inhibit its action. Thus, the enzyme
will reach equilibrium. Hence, I think this reaction is energetically favorable.
4. A. The molecular weight of the highest activity is 50kDa
B. The enzyme is a multi-subunit complex that requires all subunits to function; you
may have damaged the complex during purification (i.e. separated the subunits).
Alternatively, under your purification circumstances, the protein may have
precipitated/denatured.
c. An inhibitor may inhibit the enzyme's activity in the crude lysate.
You may have separated the two during purification, allowing the enzyme to function
at full capacity.

Sign up to view the full document!

lock_open Sign Up
Showing Page:
3/3

Sign up to view the full document!

lock_open Sign Up
Unformatted Attachment Preview
1. The hydrophobic amino acids Leu, Phe, Val, Ile, and Met are more likely to be in the interior of a protein than the polar amino acids Ser, Ser-p, Lys, Gln, His, and Glu. The polar amino acids are likely to be present on the outer surface of the protein exposed to the outside environment. 2. A. This statement is true. The active site is made up of only a few amino acid side chains. The rest of the protein is needed to keep the polypeptide chain in place, offer additional binding sites for regulatory functions, and help the protein find its way about the cell. B. This statement is false. The electromagnetic interactions between molecules were distributed in non-covalent interactions. These bonds are distinct from covalent bonds in that they do not share electrons. The stability of macromolecules is dependent on interactions like this. Electrostatic interactions, tiny pi effects, Vander ...
Purchase document to see full attachment
User generated content is uploaded by users for the purposes of learning and should be used following Studypool's honor code & terms of service.
Studypool
4.7
Indeed
4.5
Sitejabber
4.4