BIOL 1030H Lecture Notes - Lecture 13: Alpha Helix, Peptide, Hemoglobin

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13 May 2018

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Secondary structure

●Alpha helix: polypeptide chain is twisted tightly in a right-handed coil

●Stabilized by hydrogen bonds between carbonyl group and the amide group four residues

ahead

Beta Sheet

●Adjacent strands can run in the same direction (parallel), or in opposite directions

(antiparallel), as shown here.

●Hydrogen bonds form between carbonyl groups in one polypeptide and amide groups in a

different part of the polypeptide.

●The polypeptide folds back and forth on itself, forming a pleated sheet

Tertiary Structure

●Tertiary structure: three-dimensional shape, usually made of several secondary structure

elements

●Distribution of hydrophilic and hydrophobic R groups and chemical bonds/interactions

that form between the R groups

Quaternary Structure

●This enzyme consists of two identical polypeptide subunits, shown in light green and

dark green.

●Hemoglobin is made up of four subunits: two copies of the polypeptide depicted in

magenta and two copies of the polypeptide depicted in blue

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Document Summary

Alpha helix: polypeptide chain is twisted tightly in a right-handed coil. Stabilized by hydrogen bonds between carbonyl group and the amide group four residues ahead. Adjacent strands can run in the same direction (parallel), or in opposite directions (antiparallel), as shown here. Hydrogen bonds form between carbonyl groups in one polypeptide and amide groups in a different part of the polypeptide. The polypeptide folds back and forth on itself, forming a pleated sheet. Tertiary structure: three-dimensional shape, usually made of several secondary structure elements. Distribution of hydrophilic and hydrophobic r groups and chemical bonds/interactions that form between the r groups. This enzyme consists of two identical polypeptide subunits, shown in light green and dark green.

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

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

violetyellowjacket662

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

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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BIOL 1030H Lecture Notes - Lecture 13: Alpha Helix, Peptide, Hemoglobin

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