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Advanced Higher Biology > Unit 1 - Proteins > Flashcards

Unit 1 - Proteins Flashcards

1
Q

What is the Proteome?

A

Entire set of proteins that can be expressed from a genome

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2
Q

What is endoplasmic reticulum?

A

Network of membrane tubules continuous with nuclear membrane

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3
Q

What is Golgi apparatus?

A

Series of flattened membrane discs

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4
Q

What are lysosomes?

A

Membrane bound organelles containing hydrolases that digest proteins, lipids, carbohydrates

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5
Q

What are vesicles?

A

Transports materials between membrane compartments

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6
Q

What is a signal sequence?

A

A short stretch of amino acids at one end of a polypeptide that determines the eventual location of a protein

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7
Q

What is post-translational modification?

A

Changes that occur to polypeptides after they have been synthesised

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8
Q

What is proteolytic cleavage?

A

When Inactive precursors are changed to produce active proteins

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9
Q

What is the R group?

A

Part of an amino acid that varies

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10
Q

What is a prosthetic?

A

A non-protein unit tightly bound to a protein and necessary for its function

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11
Q

What is co-operativity?

A

When changes in binding of a target molecule to one subunit of a polypeptide changes the affinity of the other subunits

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12
Q

What is a ligand?

A

A molecule which binds to a secondary site on an enzyme to alter its confirmation

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13
Q

What is an allosteric enzyme?

A

Enzyme that changes confirmation in response to a modulator

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14
Q

What is a positive modulator?

A

Molecule which increases an enzymes affinity for the substrate

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15
Q

What is a negative modulator?

A

A molecule which reduces an enzymes affinity for the substrate

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16
Q

What is a protein phosphatase?

A

An enzyme that removes a phosphate group from its substrate/catalyses dephosphorylation

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17
Q

What is a protein kinase?

A

A molecule which catalyses the transfer of a phosphate group to other proteins

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18
Q

What is genomics?

A

The study of the genome

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19
Q

What is the genome?

A

The total genetic material in a cell

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20
Q

Why is the proteome larger than the genome?

A

More than one protein can be produced from a single gene as a result of alternative gene splicing

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21
Q

What are genes that don’t code for proteins called?

A

Non-coding RNA genes

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22
Q

Examples of non-coding RNA genes?

A

tRNA, rRNA

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23
Q

Factors that affect the set of proteins expressed

A
  • Metabolic activity
  • Cellular stress
  • Response to signalling molecules
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24
Q

What increases the total area of the membrane?

A

System of internal membranes

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25
Q

What are other structures in eukaryotes that have a membrane?

A
  • Endoplasmic reticulum
  • Golgi Apparatus
  • Lysosomes
  • Vesicles
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26
Q

What are the 2 types of endoplasmic reticulum

A
  1. Rough (ER)
  2. Smooth (ER)
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27
Q

What is the difference between smooth (ER) and rough (ER)?

A

Rough (ER) has ribosomes on its cytosolic face while smooth (ER) lacks ribosomes

28
Q

What are membranes made up of?

A

Lipids and proteins

29
Q

Where are lipids synthesised?

A

Smooth (ER) and inserted into its membrane

30
Q

Where does synthesis of all proteins begin?

A

Cytosolic ribosomes

31
Q

Where is synthesis of cytosolic proteins completed?

A

Cytosolic ribosomes

32
Q

Where do cytosolic proteins go once synthesised?

A

Remain in cytosol

33
Q

How are transmembrane proteins synthesised?

A
  • Carry signal sequence, halts translation at cytosolic ribosome
  • Directs ribosome to dock in ER, forming RER.
  • Translation continues after docking
  • Protein is inserted into membrane of RER
34
Q

What happens after proteins are synthesised at the Rough (ER)?

A

-Transported by vesicles that bud off ER
-Fuse with Golgi apparatus

35
Q

What happens when proteins move through Golgi apparatus?

A

Undergo post-translational modification.

36
Q

What happens after post-translational modification?

A

Vesicles that leave the Golgi apparatus take proteins to the plasma membrane and lysosomes.

37
Q

What are examples of secreted substances?

A
  • Peptide hormones (insulin)
  • Digestive enzymes (trypsin)
38
Q

What is the pathway of secreted substances?

A
  • Translated in ribosomes on RER, enter its lumen
  • Bud off RER in a vesicle and go to Golgi Apparatus
  • Packaged into secretory vesicles
  • These vesicles move to and fuse with plasma membrane, releasing them out of the cell
39
Q

What are many secreted proteins synthesised as?

A

Inactive precursors ( require proteolytic cleavage to become active )

40
Q

What functional groups do all amino acids contain?

A
  • Amine group
  • Acid group
41
Q

Categories of R-groups

A
  • Polar
  • Hydrophobic
  • Acidic
  • Basic
42
Q

What is the acidic R group?

A

Contains a carboxylic acid side chain (-COOH)

43
Q

What is the basic R group?

A

Contains an amino side chain (-NH2)

44
Q

What is a polar R group?

A

They are hydrophilic, meaning they seek contact with aqueous solutions

45
Q

What are hydrophobic R groups?

A

Also known as non-polar, they avoid contact with liquids

46
Q

What are amino acids linked by?

A

Peptide bonds

47
Q

What is the primary structure?

A

The sequence in which the amino acids are synthesised into the polypeptide

48
Q

How is secondary structure formed?

A

Hydrogen bonding along the backbone of the protein

49
Q

What are the 3 types of secondary structure?

A
  • Alpha helix
  • Beta sheets
  • Turns
50
Q

What is an alpha helix?

A

Spiral with R groups sticking out

51
Q

What are Beta sheets?

A

Parts of polypeptide chain which run along side each other to form corrugated sheet with R above and below ( can be antiparallel and parallel )

52
Q

What are turns?

A

They reverse the direction of the polypeptide chain and the chain folds back on itself

53
Q

What is the tertiary structure?

A

The final folded shape of the polypeptide.

54
Q

How is the tertiary structure stabilised?

A

Interactions of amino acids

55
Q

Examples of R group interactions

A
  • Hydrophobic interactions
  • Ionic bonds
  • London dispersion forces (LDFs)
  • Hydrogen bonds
  • Disulphide bridges
56
Q

When does quaternary structure exist?

A

Proteins with two or more connected polypeptide subunits which are linked by bonds between 2 or more polypeptide chains

57
Q

What does the quaternary structure describe?

A

The spatial arrangement of the subunits

58
Q

What effect does increasing temperature have on R groups and structure of protein?

A
  • Disrupts the interactions that hold proteins in shape
  • Protein unfolds and becomes denatured
59
Q

What effect does increasing PH have on R groups and structure of protein?

A
  • Interactions are lost
  • Changes conformation of protein until it becomes denatured
60
Q

What happens when a ligand binds to a protein?

A

Changes the conformation of the protein which causes a functional change in the protein

61
Q

What do modulators do?

A

Regulate the activity of the enzyme when they bind to the allosteric site

62
Q

What effect does decreasing pH/increasing temperature have on haemoglobin and oxygen?

A

Lowers the affinity of haemoglobin for oxygen, so binding of oxygen is reduced. (in actively respiring tissue, this will promote increased oxygen delivery to tissues).

63
Q

What is phosphorylation?

A

When a phosphate group is added to the protein

64
Q

What can phosphorylation do to a protein?

A

Can cause reversible conformational changes in proteins

65
Q

The ___________________ of ATP is transferred to specific R groups (Protein Kinases)

A

Terminal phosphate

66
Q

What is phosphorylation a method of in many cellular proteins?

A

Regulation

67
Q

What does adding a phosphate group do to the charge and bonds?

A

Adds a negative charge, Ionic interactions can be disrupted and new ones created

Advanced Higher Biology (8 decks)

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