Cells and proteins - 2 Flashcards

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1
Q

what is proteomics?

A

the study of an entire set of proteins expressed by the organism’s genome

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2
Q

what is a proteome?

A

set of proteins in an organism

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3
Q

why is a proteome larger than a genome?

A

since alternative RNA splicing and post translation modification means that one gene = many proteins

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4
Q

what is alternative RNA splicing?

A

different mRNA segments can be treated as introns or axons depending on the protein

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5
Q

name two types of post translation modification

A
  • addition of a phosphate or carbohydrate

- cleavage

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6
Q

what is the structure of an amino acid?

A
  • amide group
  • R group
  • carboxylic group
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7
Q

how do amino acids join together?

A

in a condensation reaction

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8
Q

what type of bonds form when amino acids join together?

A

peptide bonds

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9
Q

what is a chain of amino acids called?

A

a polypeptide

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10
Q

where are the N terminal?

A

where the NH2 group is

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11
Q

where is the C terminal?

A

where the carboxylic group is

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12
Q

what is the primary structure?

A

the order in which the amino acids are synthesised

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13
Q

what are the four classes of amino acids?

A
  • acidic
  • basic
  • polar
  • hydrophobic
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14
Q

describe an acidic amino acid

A
  • negatively charged

- R group = carboxylic group

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15
Q

describe a basic amino acid

A
  • positively charged

- R group = amide group

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16
Q

describe a polar amino acid

A
  • slightly charged

- R group = OH group

17
Q

describe a hydrophobic amino acid

A
  • usually no charge

- R group = hydrocarbon

18
Q

what is the secondary structure?

A

chain which forms either two structures in which hydrogen bonds keep the structure in place

19
Q

what two types of secondary structures can be formed?

A

alpha helix or beta-pleated sheets

20
Q

what are the two types of beta-pleated sheets?

A

anti-parallel sheets or parallel sheets

21
Q

what gives a protein its 3D structure?

A

different types of bonding forming a tertiary structure

22
Q

what types of bonding can form in a tertiary structure?

A
  • hydrogen bonds
  • ionic bonds
  • hydrophobic
  • van der Waals forces
  • disulphide bridges
23
Q

what is a quaternary structure?

A

proteins with many chains of polypeptides subunits connected together

24
Q

what is a prosthetic group?

A

non-protein group which is strongly bound to a polypeptide unit

25
Q

what can cause a protein to denature?

A

temperature and pH

26
Q

what is an R-group?

A

variable group on an amino acid

27
Q

what are the importances of R-groups on a protein?

A
  • determines the structure of protein
  • determines the location within a cell
  • call allow bindings of ligands
28
Q

what are cytoplasmic proteins?

A

soluble proteins that forms a globular structure with hydrophobic core

29
Q

what makes cytoplasmic proteins soluble?

A

surface has a greater proportion of hydrophilic R groups