Module 1 - Unit 2 Flashcards Preview

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Flashcards in Module 1 - Unit 2 Deck (72)
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1

Identify the Monomer for Proteins

Amino Acids

2

Identify the Monomer for DNA

Prosphate
deoxyribose and
4 bases ( Adenine, Guanine, Thymine, Cytosine)

3

Identify the Monomer for RNA

RNA: Nucleotide containing, adenine, cytosine, guanine and uracile

4

What is the monomer of a lipid?

Glycerol and 3 fatty acids is the monomer of a lipid.This is also the basic structure of a lipid.

5

What are the monomers of sucrose?

glucose and fructose

6

what are the monomers of lactose?

glucose and galactose

7

What are the monomers of maltose?

2 glucose molecules

8

Describe the primary structure of a protein

• Primary:
○ Refers to the amino acid sequence or polypeptide backbone
○ Determines the 3 dimensional shape
○ 2-Dimensional

9

Describe the secondary structure of proteins

• Secondary:
○ 3-dimensional
○ Takes shape when the string is raised off the table and the side chains interact causing the string to fold
○ Refers to the folding of the polypeptide backbone in the protein

10

Describe the tertiary structure of a protein

Tertiary
○ Most proteins fold into shapes that are classified as globular and some form long fibers.
○ This structure is stabilized by mostly non-covalent forces
§ Hydrophbic interactions
§ Ionic bonds
§ Hydrogen bonds

11

Describe the quaternary structure of proteins

• Quarternary
○ Interaction of 2 or more polypeptide chains that associate to form a larger protein is the next conformational level

12

What type of bonds hold primary structured proteins together?

Peptide Bonds

13

What type of bonds hold secondary structured proteins together?

Hydrogen Bonds

14

What type of bonds hold tertiary structured proteins together?

Hydrophobic interactions
Ionic bonds
Hydrogen bonds

15

Briefly describe how proteins can be denatured and explain the biological impact.

Denaturation is the term used for any change in the three-dimensional structure of a protein that renders it incapable of performing its assigned function. A denatured protein cannot do its job. (Sometimes denaturation is equated with the precipitation or coagulation of a protein; our definition is a bit broader.) A wide variety of reagents and conditions, such as heat, organic compounds, pH changes, and heavy metal ions can cause protein denaturation

16

What are some differences between DNA and RNA?

DNA, or deoxyribonucleic acid, is like a blueprint of biological guidelines that a living organism must follow to exist and remain functional. RNA, or ribonucleic acid, helps carry out this blueprint's guidelines. Of the two, RNA is more versatile than DNA, capable of performing numerous, diverse tasks in an organism, but DNA is more stable and holds more complex information for longer periods of time.

17

What are the two major stages in protein synthesis?

- Transcription
- Translation
- inititiation
- elongation
- termination

p.49-50**

18

What are the different types of chromosomal mutations?

○ Deletion of a gene: Gene becomes unattached to the centrometre and is lost.

○ Duplication of genes: The mutant genes are displayed twice on the same chromosome. This can prove to be advantageous as no genetic material is lost or altered and new genes are gained. The new chromosome posseses all its initial genes plus a duplicated one, which is usually harmless.

○ Inversion of genes: The order of particlular genes are reversed. The new sequence may not be viable but may also be advantageous.

○ Translocation of genes: Information from one of two homologous chromosomes breaks and binds to the other. This usually is lethal.

19

Name the mutations caused by alternation of the genes

○ Deletion: Loss of one nucleotide uridine in the example below leads to different sequence of amino acids.

○ Insertion: A nucleotide is inserted into a sequence. This alters the chain as in the above example and is called a frameshift alteration.

○ Inversion: This is where a particular nucleotide sequence is reversed. This may or may not be serious depending on the final amino acid that is inserted.

○ Substitution: This is where a certain nucleotide is replaced with another. An example of this type of alteration is discussed in the Case History on Sickle Cell Anemia. In this condition, the 6th amino acid on the hemoglobin beta-chain calls for glutamate but in sickle cell anemia the amino acid coded for this position calls for valine. This change has physiological consequnces as discussed in the case history. NOTE: A change in base pairs results in an amino acid change but if the new amino acid has the same chemical properties as the old one then it is unlikely to have a deleterious clinical outcome.

20

In what form is glucose stored in muscle?

Glycogen

21

Which of the following carbohydrates is a polysaccharide?
a) starch
b) sucrose
c) lactose
d) glucose

Starch

22

One of the following is not consistent with the structure of a phospolipid ?
a) glycerol
b) 3 free fatty acids
c) 2 free fatty acids
d) phosphate

3 free fatty acids ( it's only 2 fatty acids)

23

8. What substance is a precursor to all steroid hormones?
a) fatty acids
b) cholesterol
c) triglycerides
d) phospholipids

Cholesterol

24

In serum electrophoresis when a buffer solution of pH 8.6 is used, which of the following characterizes the proteins?
a) net negative charge
b) net positive charge
c) net zero charge
d) migrate to the cathode

A net negative charge

25

Which of the following bases are not associated to DNA?
a) adenine
b) guanine
c) uracil
d) cytosine

Uracil

26

What distinguishes 1 amino acid from another?

R-group

27

How many different amino acids exist?

20

28

The charge of an amino acid can be positive, negative or neutral. What can the nature of the charge affect?

1- Net charge of a protein
2- Effect on the ion distribution
3- Buffers
4- Structural effects

* see p. 6 for further detail)

29

How many of the 20 amino acids are synthesized by the human cells?

10
the remainder or essential amino acids must be obtained by our diets.

30

True or False
Proteins are polymers of amino acids linked together via peptide bond?

TRUE