Biology 1002B Lecture Notes - Lecture 3: Actin, Rhodopsin, Hemoglobin

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3 Feb 2013

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All proteins are polymers of amino acids (residues) There are 20 different side groups represented by r: eg. Single hydrogen atom: this side group give them individual properties. Polypeptide: chains of covalently peptide bonded amino acids. Protein: polypeptide folded into a specific 3d shape. Formed by dehydration synthesis: amino group of amino acid (n terminal) + carboxyl group of another amino acid (c terminal, amino acids are added only to the carboxyl end, the four levels of protein structure. Primary structure: unique sequence of amino acids, forms a polypeptide, determined by nucleotide sequence coding region. H bonds between top and bottom coil: beta pleated sheet. H bonds between atoms of each strand: less regular: random coil or loop, hydrogen bonds between hydrogen (attached to n) and oxygen (attached to c) Tertiary structure: folding of secondary structure into 3d shape, four major interaction between r groups. Ionic bonds (+ amino acid with oxygen)

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

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

lilacmammoth542

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.

Biology 1002B Lecture Notes - Lecture 3: Actin, Rhodopsin, Hemoglobin

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