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CfE Advanced Higher Biology > Unit 1 > Flashcards

Unit 1 Flashcards

1
Q

What is a proteome?

A

Entire set of proteins expressed by a genome

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2
Q

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

A
  • Alternative RNA Splicing

- Post Translation Modification

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3
Q

Describe the structure of an amino acid

A
  • Central Carbon Group
  • NH2 Amine Group
  • COOH Carboxylic Group
  • H
  • Variable R group
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4
Q

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

A 
Amine Group(NH2)
Carboxylic Acid Group(COOH)
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5
Q

What are the four classifications of R groups?

A

Acidic
Basic
Polar
Hydrophobic

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6
Q

Describe the features of an Acidic R group

A

Contains a COOH

Negatively charged

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7
Q

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

A

Basic

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8
Q

How are amino acids joined together?

A

Peptide Bonds

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9
Q

What is the primary structure of a protein?

A

Order of amino acids in a peptide chain

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10
Q

What causes secondary structure?

A

Hydrogen Bonds

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11
Q

What are the two main folding motifs?

A

Alpha Helix

Beta Sheet

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12
Q

Describe the Alpha Helix

A

Helical structure with four residues per turn

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13
Q

Describe the Beta Sheet

A

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

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14
Q

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

A
  • Hydrophobic
  • Ionic
  • Hydrogen
  • Van der Waals
  • Disulphide
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15
Q

Where are hydrophobic interactions typically found?

A

Towards the inside of the polypeptide

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16
Q

What two molecules do ionic bonds occur between?

A

COO- and NH3+

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17
Q

What bonds occur between covalent bonds between R groups of Cysteines

A

Disulphide Bridges

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18
Q

What prosthetic group does Myoglobin contain?

A

Haeme

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19
Q

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

A

Glycoprotein

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20
Q

What prosthetic group does Lipoprotein contain?

A

Lipid

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21
Q

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

A

Nucleoprotein

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22
Q

What effect does PH have on a protein?

A
  • 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
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23
Q

Give an example of a protein which contains Quaternary structure

A

Haemoglobin

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24
Q

Describe Quaternary Stucture of a protein

A

Different subunits of polypeptide chains joined together

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25
Q

What is a Cytoplasmic Protein?

A

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

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26
Q

What are the two classifications of proteins at the membrane?

A

Integral

Peripheral

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27
Q

What is the function of Integral Proteins?

A

Found within the membrane, act as channels or transporters

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28
Q

How are integral proteins held in the protein?

A

Strong Hydrophobic Interactions

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29
Q

What is a Ligand?

A

A substance which can bind to a protein

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30
Q

What charge is the DNA sugar phosphate backbone?

A

Negatively Charged

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31
Q

What is the name of proteins that can bind to DNA and stimulate or inhibit the transcription of genes

A

Transcription Factors

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32
Q

What is a Modulator?

A

Substances which can bind to an enzyme at a site remote from the active site

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33
Q

What type of modulators increase the affinity for the substrate?

A

Positive Modulators

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34
Q

Describe Polar R groups

A

Hydrophyllic

Example: C=O, N-H

35
Q

What causes the increase in kinetic energy of a protein molecule?

A

Temperature

36
Q

What effect can increasing the kinetic energy of a protein have?

A

Places stress on the bonds, breaking them, causing the protein to be denatured

37
Q

What part of the protein determines the location in a cell?

A

R groups at the surface of the protein

38
Q

Where are the hydrophobic R groups found in cytoplasmic proteins?

A

Clustered towards the middle

39
Q

How are Peripheral proteins more associated with the heads of the phospholipids?

A

They contain more hydrophyllic R groups

40
Q

Where are the R groups not involved in folding found and what is their purpose?

A

Form areas on the surface

Ligands can bind to them

41
Q

What is the function of positively charged histomes?

A

Bind to DNA to form Nucleosomes, allowing the DNA to be packaged in chromosomes

42
Q

Give an example of how ligand binding can influence the activity of a protein

A

Induced fit in enzymes

43
Q

What is Co-operativity?

A

Co-operativity occurs in proteins with more than one subunit. It is when ligand binding at one subunit alters the conformation of other sub units.

44
Q

Give an example of a protein where co-operativity occurs

A

Haemoglobin

45
Q

Explain the effect of binding of oxygen to one of the sub units in Haemoglobin

A
    • Changes its confirmation
    • In turns changes the conformation of the remaining subunits
  • -Increasing their affinity for oxygen
    • Maximises the O2 uptake in lungs
46
Q

What is the effect of the release of oxygen from Haemoglobin?

A

Reduces the affinity of the other subunits

47
Q

What is a benefit of reducing the affinity of other subunits when oxygen is released from Haemoglobin?

A

Helps to release oxygen in oxygen depleted environments

48
Q

Give an example of an oxygen depleted environment

A

Respiring Tissue

49
Q

What two conditions can further reduce affinity of haemoglobin subunits for oxygen

A 
Low pH (caused by presence of CO2)
High Temperature
50
Q

What can be added or removed from particular R groups to cause reversible conformational change in proteins?

51
Q

What type of modification is Phosphorylation an example of?

A

Covalent modification and post translation modification

52
Q

What can Phosphorylation help to regulate?

A

The activity of many cellular proteins

53
Q

What is the function of a Kinase?

A

Catalyse Phosphorylation, by transferring phosphate from ATP to the protein

54
Q

What is the name for the enzymes that catalyse de-phosphorylation?

A

Phosphatase

55
Q

Where are ATPases found?

A

Membrane, as are membrane bound

56
Q

What and how do ATPases use phosphate for?

A

ATPases use phosphate to phosphorylate themselves, and they use it to change their confirmation and alter their activity

57
Q

What is a use of transmembrane ATPases?

A

Active transport of ions and the sodium potassium pump

58
Q

What triggers the movement of Myosin?

A

Conformational changes due to ligand binding

59
Q

What does movement of Myosin cause?

A

The movement of finer actin filaments

60
Q

Describe the process of Muscle Contraction

A
  1. Myosin heads are bound to the actin, forming cross bridges
  2. Binding of ATP occurs, causes a conformational change, myosin heads detach from the actin and swing forward
  3. ATP is broken into ADP + Pi. They remain bound to the myosin and cause a second conformational change. The myosin acts as an ATPase
  4. Myosin rebinds to the actin but at a further position along the filament. A third conformational change occurs.
  5. ADP + Pi are released. Myosin head returns to original confirmation, dragging the actin filament along
61
Q

What type of substances are able to diffuse directly through the bilayer in a membrane?

A

Hydrophobic

62
Q

Give an example of a molecule that can diffuse directly through the membrane bilayer

A

Oxygen, Carbon Dioxide, Water, Steroid Hormones

63
Q

Give an example of a molecule that requires a membrane protein to move it across the membrane

A

Glucose, Charged Molecules such as Na+, K+ and Ca2+

64
Q

Can membrane proteins create/maintain concentration gradients?

65
Q

What are the two types of membrane proteins?

A

Channels, Transporters

66
Q

Describe Channel Proteins

A

Transmembrane proteins, passage is always passive through them
They can be gated or ungated

67
Q

Give an example of an ungated protein

68
Q

What are the two ways gated channels can be controlled?

A

Ligand Gated

Voltage Gated

69
Q

Describe Ligand Gated Channel Proteins

A

Binding of a ligand triggers conformational change
Example: Neurotransmitters act as ligands when binding to receptors in post synaptic neurons, which open to allow sodium ions in

70
Q

How are voltage gated channels opened and closed?

A

Changes in Ion Concentration across the membrane

71
Q

Explain the difference between transporters and channels

A

Channels - molecule binds to channel to allow other molecules to move through
Transporters - molecule binds to transporter so it can move through

72
Q

Are transporters specific?

73
Q

If a transporter moves molecules passively what is this known as?

A

Facilitated Diffusion

74
Q

Give an example of a transporter and where it can be found

A

GLUT 4 transporter

Found in Fat and Muscle Cells

75
Q

Define ‘Coupled Transport’

A

The movement of two molecules together across a membrane

76
Q

What is the difference between a symport and an antiport?

A

A symport moves both molecules in the same direction, and antiport moves them in opposite directions

77
Q

Give an example of coupled transport and state the two molecules, the name of the transporter and whether the transporter is an antiport or a symport

A

Glucose Symport

  • Transfers Na+ and Glucose
  • Symport
  • Found in cells lining small intestine
78
Q

In the glucose symport, does sodium move up or down its concentration gradient?

79
Q

What happens when Na+ binds to the Glucose Symport?

A

causes a conformational change which pushes both sodium and glucose across the membrane

80
Q

How do cells maintain the gradient of sodium required for the glucose symport?

A

Using an active transport protein, known as the sodium potassium pump(Na+/K+ ATPase)

81
Q

Where does the Sodium Potassium ATPase get its energy from?

A

The hydrolysis of ATP

82
Q

Describe the direction of the Sodium Potassium Pump

A

Sodium out, Potassium In

83
Q

Link to my free higher biology flashcards

A

https://www.brainscape.com/p/1L84J-LH-5FXJ1

CfE Advanced Higher Biology (2 decks)

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