BIOL 151 Lecture 4: Bio 151 - Chapter 4

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7 Feb 2017

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4. 1 molecular structure of proteins: amino acids contain a central carbon atom called the (alpha) carbon, connected by covalent bonds to four different chemical groups: Amino acids differ in their side chains. The side chain differs from one amino acid to the next. Basic amino acids tend to be positively charged at intracellular ph, and acidic amino acids tend to be negatively charged. The small size of the amino acid also makes it flexible, allowing more flexibility of the polypeptide backbone, which is important in the folding of the protein. It is more rigid compared to glycine, therefore allowing it to maintain protein structures. It makes a special contribution through it"s -sh group. The -sh group can help form a s-s disulfide bond, which can form cross bridges that can connect different parts of the same protein or even different protein. Successive amino acids in proteins are connected by peptide bonds: peptide bond: the bond formed between two amino acids.

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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

Unit 2 Organic Chemistry

Organic compounds vs. Inorganic compounds

What makes a compound organic? Inorganic?

Functional groups (phosphate groups, amino groups, carboxyl groups)

Know the structure of each of these groups, and which organic compounds they are found in. You can draw them for your own use.

Hydrolysis

What is it? What is it used for?

Dehydration synthesis

What is it? What is it used for?

Carbohydrates (Monosaccharides, Disaccharides, Polysaccharides and examples)

Know the process of joining two monosaccharides together to create a disaccharide.

Be able to give examples of several monosaccharides, disaccharides and polysaccharides.

Monosaccharide examples (3)	Disaccharide examples (2)	Complex carbohydrates (3)

Lipids (Saturated vs. Unsaturated; Phospholipids, Steroids)

Define a saturated fatty acid.

Define an unsaturated fatty acid. Draw if it helps.

What process is used to put the fatty acid chain on a glycerol molecule?

Hydrophilic vs. hydrophobic

Define hydrophilic.

What part of the phospholipid is hydrophilic?

Define hydrophobic.

What part of the phospholipid is hydrophobic?

Proteins, types and functions

What is a protein composed of, and what does it do?

Amino acids

Name the three parts of the amino acid that come off the common Carbon.

Identify each of the three parts. (Amino Acid ID game)

Peptide Bonds

How are they formed?

What two parts of each amino acid do they join together?

Enzymes - define.

Levels of Protein structure

Complete the chart below.

Protein structure level	definition
Primary
Secondary
Tertiary
Quarternary

Protein Denaturation

What is it and how does it happen?

Define what a Solute is.

Define what a solvent is

Nucleic acids (DNA, RNA, ATP)

Nucleotide

Name its three parts and be able to identify each of them on a diagram. (Nucleotide ID game)

What are the two possible sugars used in a nucleotide?

Complete the Table below.

	DNA	RNA	ATP
What sugar does it have?
What nitrogen bases does it have?
Provide the pairings of the nitrogen bases of each nucleic acid			N/A
What is its structure?

1. What is an organic molecule?

2.Name three hydrocarbons and be able to draw their structural formulas.

3. What is an isomer? List and describe the three types (structural, geometric, and enantiomers).

4. Be able to recognize and describe the properties of these functional groups: aldehyde, ketone, hydroxyl, sulfhydryl, carboxyl, amino, and phosphate groups.

5. What is a monosaccharide? Give two examples of these molecules and their functions.

6. Describe these chemical reactions: dehydration synthesis (condensation reaction) and hydrolysis (rehydration).

7. What is a disaccharide? List two and give their functions.

8. What is a polysaccharide? List two storage forms and two structural forms. How are they formed and what is their specific function?

9. How do the pancreatic hormones insulin and glucagon regulate blood sugar levels?

10. What is molting and why is it necessary in certain animals?

11. What four molecules are bonded together to form a triglyceride or fat? Why are fats nonpolar? What are some functions of fats as well as other lipids such as oils and waxes?

12. How do saturated and unsaturated fats differ? Discuss bonding patterns and possible sources of these fats. Which type is healthier for you? Why?

13. Why do animals store most of their excess glucose as fats or oils rather than as glycogen or protein? Give two reasons.

14. What are phospholipids? Identify parts of the phospholipid bilayer that are hydrophobic or hydrophilic? What important cell structure do these molecules help create?

15. Describe the structure of a steroid. How is cholesterol used in beneficial ways in your body?

16. What are LDLs and HDLs? Which is considered good or bad cholesterol? What condition could result from high blood pressure?

17. What are four ways to either reduce high blood cholesterol or maintain a safe level?

18. What is the composition of an amino acid? Why would they be considered nonpolar, polar, acidic, or basic?

19. Define dipeptides and polypeptides.

20. Describe the primary structure of a protein. What type of bonding creates it?

21. What is the secondary structure of a protein? Name two types of secondary structure and indicate what type of bonding holds them together. List three fibrous proteins.

22. What is the tertiary structure of a protein? What types of bonds or chemical interactions allow a protein to maintain this structure? List three globular proteins.

23. What is the quaternary structure of a protein? Describe a hemoglobin molecule.

24. What are the subunits of nucleic acids and what is their composition? How are these subunits bonded together? What is DNS's basic shape?

25. List three differences between DNA and RNA.

BIOL 151 Lecture 4: Bio 151 - Chapter 4

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