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27. Which of the following statements is not true concerning protein folding? a. Proteins fold around a hydrophobic core b. The interior of proteins is held together exclusively by hydrophobic interactions c. The amino acid sequence of a protein is responsible for determining the shape of a protein d. The active conformation of a protein is it most thermodynamically favorable state e. none of the above

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Lelia Lubowitz
Lelia LubowitzLv2
28 Sep 2019
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Related questions

Protein Structure

a.Different function of proteins and examples:

b. Protein building blocks:

1. atomic composition of building block:

2. "parts" or "functional groups" of the building block:

c. Importance of side chain (R group):

d. Hydrophobic amino acids characteristics:

e. Hydrophilic amino acids characteristics:

f. Charged amino acids characteristics

Copy and complete the table below regarding the characteristics and which groups in the polypeptide interact together at each structural level of the protein.

characteristics

groups interacting

Primary structure

Secondary structure

Tertiary structure

Quartenary structure

Value: 2

Choose the correct statement(s). You may choose more than one answer.

[mark all correct answers]
a. Proteins are the building blocks of amino acids.

b. Enzymes are a type of protein.

c. Quartenary structure consists of two or more polypeptide chains interacting.

d. Amino acids are made of carbon, hydrogen, nitrogen and phosphorus.

e. The primary structure of a protein is formed due to the interaction of side groups.

Value: 3

Put the following statements regarding the structural levels of a protein formation in the correct order.

Below is a sequence of events. Place them in the order they should occur, number 1 being the first item. Select the step number from the drop down next to each item.

Items to order:

1. Individual amino acids are bonded together via peptide bonds.

2. Two or more polypeptide chains interact via bonds.

3. Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

4. Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

Value:4

Put the following statements regarding the structural levels of a protein formation in the correct order

Individual amino acids are bonded together via peptide bonds.

 1 2 3 4

Two or more polypeptide chains interact via bonds.

 1 2 3 4

Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

 1 2 3 4

Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

 1 2 3 4

Value: 5

Hydrophobic amino acids will be found _______________.

a. In the interior (inner core) of a protein, away from the watery environment.

b. in the interior of a plasma membrane.

c. Both A and B

d. Neither

Value: 6

A protein's function is defined by ____________.

a. enzymatic reactions

b. it's shape.

c. chain of nucleotides.

d. the presence of carbon and hydrogen.

Value: 7

Which of the following is NOT considered a protein function?

a. transport of substances across membrane

b. enzymatic reactions

c. provides structural support

d. carries genetic information

16.Globular proteins fold up into compact, spherical structures that have uneven surfaces. They tend to form

multisubunit complexes, which also have a rounded shape. Fibrous proteins, in contrast, span relatively large

distances within the cell and in the extracellular space. Which protein is not classified as a fibrous protein?

(a)elastase (b)collagen (c)keratin (d)elastin

17.You have two purified samples of protein Y: the wild-type (nonmutated) protein and a mutant version with a

single amino acid substitution. When washed through the same gel-filtration column, mutant protein Y runs through

the column more slowly than the normal protein. Which of the following changes in the mutant protein is most likely

to explain this result?

(a)the loss of a binding site on the mutant protein surface through which protein Y normally forms dimers

(b)a change that results in the mutant protein’s acquiring an overall positive instead of a negative charge

(c)a change that results in the mutant protein’s being larger than the wild-type protein

(d)a change that results in the mutant protein’s having a slightly different shape from the wild-type protein

18.Which of the following statements is true?

(a)Disulfide bonds are formed by the cross-linking of methionine residues.

(b)Disulfide bonds are formed mainly in proteins that are retained within the cytosol.

(c)Disulfide bonds stabilize but do not change a protein’s final conformation.

(d)Agents such as mercaptoethanol can break disulfide bonds through oxidation.

19.Proteins bind selectively to small molecule targets called ligands. The selection of one ligand out of a mixture of

possible ligands depends on the number of weak, noncovalent interactions in the protein’s ligand-binding site. Where

is the binding site typically located in the protein structure?

(a)on the surface of the protein (b)inside a cavity on the protein surface

(c)buried in the interior of the protein (d)forms on the surface of the protein in the presence of ligand

thanks

1. A sequence of amino acids in a certain protein is found to be – Ser – Gly – Pro – Gly –

The sequence is most probably part of a(n):

a. beta turn

b. antiparallel beta sheet

c. alpha-helix

d. parallel beta-sheet

e. alapha-sheet

2. Which statement about peptides bonds is NOT TRUE?

There is perfectly free rotation about the peptide bond.

The peptide bond has partial double-bond character.

The peptide bond is shorter than a normal carbon-nitrogen single bond.

The peptide bond usually has a trans configuration with respect to the alpha-carbons of the two amino acids involved in the peptide bond.

Peptide bonds are made via condensation of an amine and a carboxylic acid with loss of water.

3. Which of the following statements about proteins is FALSE?

Active proteins are generally very loosely structured.

In water-soluble proteins, hydrophobic amino acid residues are generally buried and not exposed to water.

Primary structure determines tertiary structure.

Secondary structure is regular, recurring arrangements in space of nearby amino acid residues in a polypeptide.

Quaternary structure involves the interaction of subunits in a protein with more than one polypeptide chain.

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