Things I forget Flashcards

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1
Q

What is the definition of risk?

A

the likelihood of harm arising from exposure to hazard

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2
Q

give 2 examples of a control measure

A
  • using appropriate handling technique
  • protective clothing and equipment
  • aseptic technique
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3
Q

What is a linear dilution series?

A

they differ by an equal interval
ex:
0.1, 0.2, 0.3 and so on

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4
Q

What is a log dilution series?

A

they differ by s constant proportion
ex:
10^-1, 10^-2, 10^-3 and so on

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5
Q

How does affinity chromatography work?

A
  • a solid matrix or gel column is created with specific molecules bound to the matrix or gel
  • soluble, target proteins in a mixture, with a high affinity for these molecules become attached to them as the mixture washes down the column
  • other non-target molecules with a weaker affinity are washed out
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6
Q

What happens during electrophoresis?

A

charged macromolecules move through an electric field applied to a gel matrix

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7
Q

How are proteins separated during electrophoresis?

A

native gels separate proteins by their shape, size and charge
native gels do not denature the molecule so that the separation is by shape, size and charge

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8
Q

What is the isoelectric point?

A

the pH at which a soluble protein has no net charge and will precipitate out of solution

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9
Q

Explain how proteins are separated using their isoelectric points in electrophoresis

A
  • soluble proteins can be separated using an electric field and a pH gradient
  • a protein stops migrating through the gel at its isoelectric point in the pH gradient because it has not net charge
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10
Q

What are immunoassay techniques used for?

A

used to detect and identify specific proteins

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11
Q

How do immunoassays work?

A
  • use stocks of antibodies with the same specificity, known as monoclonal antibodies
  • an antibody specific to the protein antigen is inked to a chemical ‘label’
  • the ‘label’ is often a reporter enzyme producing a colour change, but chemiluminescence, fluorescence and other reporters can be used
  • in some cases the asset uses a specific antigen ti detect the presence of antibodies
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12
Q

What is western blotting?

A
  • used after SDS-PAGE electrophoresis
  • the separated proteins from the gel are transferred (blotted) onto a solid medium
  • the proteins can be identified using specific antibodies that have reporter enzymes attached
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13
Q

What do culture media do?

A

promote the growth of specific types of cells and microbes

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14
Q

What are animal cells grown in?

A

medium containing growth factors from serum

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15
Q

What is the proteome?

A

the proteome is the entire set of proteins expressed by a genome

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16
Q

What are genes that do not code for proteins called?

A

non-coding RNA genes

17
Q

What are the receptors for hydrophobic signalling molecules?

A

Transcription factors

18
Q

What are transcription factors?

A

proteins that when bound to DNA can either stimulate or inhibit initiation of transcription

19
Q

What does the hormone receptor complex do?

A

Moves to the nucleus where it binds to specific sites on DNA and affects gene expression

20
Q

What DNA sites does the hormone receptor complex bind to and what effect does this have?

A
  • Binds to specific DNA sequences called hormone response elements (HREs)

-Binding at these sites influences the rate of transcription, with each steroid hormone affecting the gene expression of many different genes

21
Q

How do transmembrane receptors act as signal transducers?

A

By converting the extracellular ligand-binding event into intracellular signals, which alters the behavior of the cell

22
Q

Describe what happens once insulin binds to its receptor

A
  • Binding of insulin to its receptor causes a
    conformational change that triggers
    phosphorylation of the receptor.
  • This starts a
    phosphorylation cascade inside the cell,
  • Which eventually leads to GLUT4-containing
    vesicles being transported to the cell
    membrane.
23
Q

How is the resting membrane potential restored?

A

inactivation of the sodium channels and the opening of potassium channels

24
Q

Explain the steps of the travel of the action potential

A

1) Binding of a neurotransmitter triggers the opening of ligand-gated ion channels at the synapse

2) Ion movement occurs and there is depolarisation of the plasma membrane.

3) If sufficient ion movement occurs, and the membrane is depolarised beyond a threshold value, the opening of voltage-gated sodium channels is triggered and sodium ions enter the cell down their electrochemical gradient

4) this leads to a rapid and large change in the membrane potential

5) a short time after opening the sodium channels become inactivated

6) voltage-gated potassium channels then open to allow potassium ions to move out of the cell to restore the resting membrane potential

25
Q

What does restoration of the resting membrane potential allow?

A
  • the inactive voltage-gated sodium channels to return to a conformation that allows them to open again in response to depolarisation of the membrane
  • ion concentration gradients are re-established by the sodium potassium pump, which actively transports excess ions in and out of the cell
26
Q

What is the function of retinal?

A

absorbs a photon of light and rhodopsin changes conformation to photoexcited rhodopsin

27
Q

What is the role of photoexcited rhodopsin?

A
  • Activates a G-proteins called transducin which activates the enzyme phosphodiesterase (PDE)
  • One photo excited rhodopsin activates hundreds of molecules of G-protein.
  • Each activated G-protein activates one molecule of PDE
28
Q

What does PDE do?

A
  • It catalyses the hydrolysis of a molecule called cyclic GMP (cGMP)
  • Each active PDE molecule breaks down thousands of cGMP molecules per second
  • The reduction in cGMP concentration as a result of its hydrolysis affects the function of ion channels in the membrane of rod cells
29
Q

What does the reduction in cGMP concentration result in?

A

The closure of ion channels in the membrane of rod cells, which triggers nerve impulses in neurone in the retina

30
Q

What do cyclin proteins do and where do they come from?

A
  • they are proteins that accumulate during cell growth
  • involved in regulating the cell cycle
31
Q

How do cyclin proteins regulate the cell cycle?

A
  • Cyclins combine with active cyclin-depndant kinases (CDKs)
  • Active cyclin-CDK complexes phosphorylate proteins that regulate progression through the cycle
  • If sufficient phosphorylation is reached. progression occurs
32
Q

What happens at the G1 checkpoint?

A
  • Retinoblastoma protein (Rb) acts as a tumour supressor by inhibiting the transcription of genes that code for proteins needed for DNA replication
  • Phosphorylation by G1 cyclin-CDK inhibits the retinoblastoma protein (Rb)
  • this allows transcription of the genes that code for proteins needed for DNA replication. Cells progress from G1 to S phase
33
Q

What happens at the G2 checkpoint?

A
  • The success of DNA replication and and damage to DNA is assessed
  • DNA damage triggers the activation of several proteins including p53 that can stimulate DNA repair, arrest the cell cycle or cause cell death
34
Q

What is an example of an external death signal?

A

The production of death signal molecules from lymphocytes

35
Q

What is an example of an internal death signal?

A

DNA damage

36
Q

How do external death signals work?

A

External death signal molecules bind to a surface receptor protein and trigger a protein cascade within the cytoplasm

37
Q

What causes activation of p53 tumour-suppressor protein?

A

An internal death signal resulting from DNA damage

38
Q

What do both types of death signal result in?

A

activation of caspases (types of protease enzyme) that cause the destruction of the cell

39
Q

What is the role of apoptosis in development of an organsim?

A

to remove cells no longer required as development progresses or during metamorphosis