BIOL1006 Lecture Notes - Lecture 2: Insulin, Globular Protein, Ionic Bonding

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9 Aug 2016

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In -pleated sheets, stretches of amino acids are held in an almost fully-extended conformation that pleats or zig-zags due to the non-linear nature of single c-c and. The r groups of the amino acids in a -pleated sheet point out perpendicular to the hydrogen bonds holding the -pleated sheets together, and are not involved in maintaining the -pleated sheet structure. The tertiary structure of a polypeptide chain is its overall three-dimensional shape, once all the secondary structure elements have folded together among each other. Interactions between polar, nonpolar, acidic, and basic r group within the polypeptide chain create the complex three-dimensional tertiary structure of a protein. When protein folding takes place in the aqueous environment of the body, the hydrophobic r groups of nonpolar amino acids mostly lie in the interior of the protein, while the hydrophilic r groups lie mostly on the outside.

Related Questions

The sequence of amino acids is considered to be the ________ structure of a protein.

Select one:

a. secondary

b. tertiary

c. quaternary

d. primary

The pattern the backbone folds, for example alpha-helix or beta pleated sheet, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

Which type of forces stabilizes the primary structure of a protein?

Select one:

a. Salt bridges

b. Hydrogen bonding between the carbonyl group and amino group

c. Dipole-dipole

d. Peptide bonds

The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

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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

1. The side chain of tyrosine is considered to be polar because even though it is reminiscent of phenylalanine it also has two types of atoms that have large differences in electronegativity with asymmetry at the terminus.

a.) True

b.) False

2. Which of these changes in primary structure will be certain to cause a loss of protein activity?

a.) Asp to Glu

b.) His to Lys

c.) Trp to Ser

d.) Gly to Pro

e.) Not enough information is given since any one of these changes could be severe depending on the context of the situation

3.The difference between fetal and adult hemoglobin with regard to oxygen binding occurs because fetal hemoglobin has an amino acid substitution in one of its chains that results in a histidine (adult version) being replaced by a serine (fetal version).

a.) True

b.) False

4. What will likely happen if the side chains of aspartate and histidine at pH 5 are next to each other in a polypeptide chain?

a.) The side chains of these amino acids will be uncharged and there will be no electrostatic effect.

b.) The side chains of these amino acids will be charged and they will attract each other.

c.) The side chains of these amino acids will be charged and they will repel each other.

d.) Not enough information is given to determine the effect.

5. A beta pleated sheet:

a.) can occur between two different polypeptide chains
b.) can be formed by either intramolecular or intermolecular hydrogen bonds
c.) can only form when cysteines form disulfide bridges within this structure
d.) forms when side chains of D and E attract each other
e.) both a and b

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BIOL1006 Lecture Notes - Lecture 2: Insulin, Globular Protein, Ionic Bonding

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