Unit 1 Flashcards Preview

CfE Advanced Higher Biology > Unit 1 > Flashcards

Flashcards in Unit 1 Deck (83)
Loading flashcards...
1

What is a proteome?

Entire set of proteins expressed by a genome

2

Give two reasons why the proteome is larger than the genome?

- Alternative RNA Splicing
- Post Translation Modification

3

Describe the structure of an amino acid

- Central Carbon Group
- NH2 Amine Group
- COOH Carboxylic Group
- H
- Variable R group

4

What are the two main groups present in all amino acids?

Amine Group(NH2)
Carboxylic Acid Group(COOH)

5

What are the four classifications of R groups?

Acidic
Basic
Polar
Hydrophobic

6

Describe the features of an Acidic R group

Contains a COOH
Negatively charged

7

What classification of R groups contains an amide group and is positively charged?

Basic

8

How are amino acids joined together?

Peptide Bonds

9

What is the primary structure of a protein?

Order of amino acids in a peptide chain

10

What causes secondary structure?

Hydrogen Bonds

11

What are the two main folding motifs?

Alpha Helix
Beta Sheet

12

Describe the Alpha Helix

Helical structure with four residues per turn

13

Describe the Beta Sheet

Polypeptide chain linked together side by side, can be parallel or antiparallel

14

Name some of the possible interactions that can cause tertiary structure of the protein

-Hydrophobic
-Ionic
-Hydrogen
-Van der Waals
-Disulphide

15

Where are hydrophobic interactions typically found?

Towards the inside of the polypeptide

16

What two molecules do ionic bonds occur between?

COO- and NH3+

17

What bonds occur between covalent bonds between R groups of Cysteines

Disulphide Bridges

18

What prosthetic group does Myoglobin contain?

Haeme

19

Give an example of a protein that contains a carbohydrate prosthetic group?

Glycoprotein

20

What prosthetic group does Lipoprotein contain?

Lipid

21

Give an example of a protein that contains a nucleic acid prosthetic group?

Nucleoprotein

22

What effect does PH have on a protein?

-Affects the concentration of H+ and OH- Ions in solution
-Changes charge of protein
-Places stress on polar interactions such as hydrogen and ionic bonding
-Denature the protein

23

Give an example of a protein which contains Quaternary structure

Haemoglobin

24

Describe Quaternary Stucture of a protein

Different subunits of polypeptide chains joined together

25

What is a Cytoplasmic Protein?

Proteins found in the cytoplasm
Hydrophyllic R groups on the surface
Globular proteins
Example: Enzymes and Hormones

26

What are the two classifications of proteins at the membrane?

Integral
Peripheral

27

What is the function of Integral Proteins?

Found within the membrane, act as channels or transporters

28

How are integral proteins held in the protein?

Strong Hydrophobic Interactions

29

What is a Ligand?

A substance which can bind to a protein

30

What charge is the DNA sugar phosphate backbone?

Negatively Charged