BIOLOGY 151 Lecture Notes - Lecture 7: Van Der Waals Force, Heat Shock Protein, Disulfide

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21 Feb 2016

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The n terminus is the amino group of the first amino acid and the period is the carboxyl group of the last amino acid. Secondary structure- chemical and physical interactions cause folding. Characterized by a-helices and b-pleated sheets with random coiled regions. Tertiary structure- folding gives that complex 3d structure. Five factors promote protein folding and stability- h bonds, ionic bonds, hydrophobic effects, van der waals forces, disulfide bridges. When a protein is heated, it gets denatured. When cooled, it returns to normal tertiary structure, demonstrating that the info to specify protein shape is contained in its primary structure. High temp, ph changes, high concentration of polar molecules and nonpolar substances all affect the secondary and tertiary structure. Heat shock proteins are the general class of stress-induced chaperone proteins. Quarternary structure- mad of two or more polypeptides. Nucleic acids- storage, expression, and transmission of genetic info. Dna- stores genetic info coded in the sequence of their monomer building blocks.

Related Questions

Is DNA a protein if so what makes up proteins, if not what it is and what are its monomers called? Describe the primary, secondary, tertiary, and quaternary structure of DNA (this sub-question is independent of the answer to the first question).

Describe electrostatic bonds, covalent bonds, van der Waals interactions, and hydrogen bonds and give an example of each.

Which of the four classes of amino acids has side chains with the greatest hydrogen-bond-forming potential?

Which has the greatest potential to form electrostatic interactions?

Which class has the greatest potential for hydrophobic interactions?

Of the following amino acids, (K), (Y), and (F), which side-chains would you expect to be the most soluble in a polar aqueous solution? Which the least?

Would you agree with the statement that many different amino acid sequences can fold into the same basic tertiary structure? What data can you cite as evidence for your position?

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 level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

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BIOLOGY 151 Lecture Notes - Lecture 7: Van Der Waals Force, Heat Shock Protein, Disulfide

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