Unit 1 Flashcards

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1
Q

what is the proteome

A

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

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2
Q

what factors affect the set of proteins expressed by a given cell type

A

metabolic activity of the cell, cellular stress, response to signalling molecules and healthy vs diseased cells

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3
Q

what is the difference between the two ERs

A

Rough endoplasmic reticulum has ribosomes on its cytosolic face whereas smooth endoplasmic reticulum lacks ribosomes

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4
Q

what is the Golgi apparatus

A

the Golgi apparatus is a series of connected flattened membrane discs to allow molecules to move within the apparatus. the Golgi apparatus is adjacent to the endoplasmic reticulum.

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5
Q

what are lysosomes

A

membrane bound organelles containing a variety of hydrolyses that digests proteins lipids, nucleic acids and carbohydrates. they are acid allowing optical function of its enzymes.

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6
Q

what is the site of lipid synthesis

A

smooth endoplasmic reticulum

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7
Q

where is the site of protein synthesis

A

the synthesis of all proteins start and end in the cytosolic ribosome then the proteins remain in the cytosol.

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8
Q

what are examples of post translational modification

A

proteolytic cleavage, phosphorylation and adding functional groups

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9
Q

what is the basic structure of amino acids

A

central carbon, amine (NH2), carboxylic acid (COOH), a hydrogen and a variable R group.

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10
Q

what are the features of an acidic amino acid

A

carboxylic acid (COOH) group, hydrophilic

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11
Q

what are the features of a basic amino acid

A

Amine group, hydrophilic

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12
Q

what are the features of a polar amino acid

A

C=O, OH or NH group, hydrophilic

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13
Q

what are the features of an hydrophobic amino acid

A

hydrocarbon group, hydrophobic

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14
Q

what causes the range of functions of amino acids

A

the R groups which vary in size, shape, charge, hydrogen bonding capacity and chemical reactivity.

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15
Q

what is the primary structure of a protein

A

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

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16
Q

what are the three types of tertiary structure

A

alpha helix, beta sheet and turns

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17
Q

which amino acid is the main driving force of protein folding

A

hydrophobic as hydrophilic predominate at the surface of a soluble protein

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18
Q

what bonds are found in proteins

A

hydrogen bond and disulphide bonds.

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19
Q

what is quaternary structure of proteins

A

protein with two or more connected polypeptide subunits.

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20
Q

what are the non protein binding units necessary for proteins function

A

prosthetic groups

21
Q

what are allosteric proteins

A

allosteric proteins have quaternary structure and multiple binding sites, when a substrate binds to one of these sites the affinity of the others alters. this means activity of enzymes can vary greatly with small changes of substrate concentration

22
Q

how does pH and temperature affect affinity

A

as temperature increases affinity decreases and as pH increases affinity increases

23
Q

what do modulators do

A

modulators change the conformation of allosteric proteins. positive modulators increase affinity, negative modulators decrease affinity

24
Q

what enzyme os responsible for the phosphorylation of proteins

A

kinase

25
Q

what enzyme os responsible for the dephospho-rylation of proteins

A

phosphatase

26
Q

what are the two membrane protein types

A

integral and peripheral

27
Q

What are the specific sites on DNA that hormone response complexes bind to

A

hormone response elements, which directs influence the rate of transcription

28
Q

what is the cytoskeleton

A

the network of proteins extending throughout the cytoplasm is known as the cytoskeleton

29
Q

what protein are microtubules composed of?

A

tubulin radiations from the centrosome

30
Q

what does the cell cycle compose of

A

G1 phase DNA synthesis, S phase DNA Replication, M phase and G2 phase further DNA growth

31
Q

what are the stages of mitosis

A

interphase, prophase, metaphase, anaphase, telophase

32
Q

what protein is involved in regulating the cell cycle

A

cyclin with combine to cyclin dependent kinases to phosphorylate proteins that regulate progression through the cycle

33
Q

what is the result of uncontrolled reduction in the rate of the cell cycle

A

degenerative disease

34
Q

what is the result of an uncontrolled increase in the rate of the cell cycle

A

tumour formation

35
Q

what is apoptosis and how is it brought upon

A

triggered by internal or external death signals such as DNA damage from lymphocytes.
death signals bring upon activation of caspases that cause destruction of the cell

36
Q

what does an internal death signal resulting from DNA damage do

A

activates p53 tumour suppressor protein

37
Q

Name the class of enzyme found within lysosomes.

A

hydrolase

38
Q

Describe the role of vesicles.

A

Transport materials between membrane compartments.

39
Q

Define the term facilitated diffusion.

A

The passive transport of substances across the membrane through specific transmembrane proteins.

40
Q

Describe the relationship between the sodium-potassium pump and glucose symport in the small intestine.

A

The sodium gradient created by the sodium-potassium pump drives the active transport of glucose.

41
Q

What type of protein are the receptors for steroid hormones?

A

Transcription factors

42
Q

What is an action potential?

A

A wave of electrical excitation along a neuron’s plasma membrane.

43
Q

Describe the role of CDKs.

A

They phosphorylate proteins that regulate progression through the cycle.

44
Q

Describe one role of p53 protein.

A

stimulate DNA repair;
stop/arrest the cell cycle;
cause cell death/apoptosis

45
Q

Give an example of an internal death signal.

A

DNA damage

46
Q

Give an example of an external death signal.

A

lymphocytes

47
Q

What term described the pH at which a soluble protein had no net charge and will precipitate out of solution

A

Isoelectric point

48
Q

What is a haemocytometer used for

A

To estimate cell numbers in a liquid culture

49
Q

Describe the cause of type 2 diabetes

A

Loss of insulin receptor function