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Molecules, Genes And Cells > Proteins > Flashcards

Proteins Flashcards

1
Q

What are enzymes function?

A

Catalyse covalent bond breakage or formation

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2
Q

What are the function of structural proteins

A

Provide mechanical support to cells and tissues

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3
Q

What is the function of motor proteins

A

Generate movement in cells and tissues

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4
Q

What is the function of signal proteins?

A

Carry extra cellular signals from cell to cell

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5
Q

What is the function of transport proteins?

A

Carry small molecules or ions

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6
Q

What is the function of gene regulatory proteins?

A

Bind DNA to switch genes on or off

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7
Q

What is the function of receptor proteins?

A

Detect signals and transmit them to the cells machinery

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8
Q

What is the function of special purpose proteins?

A

Their function is highly variable. For example proteins can act as messengers, antibodies, pumps and channels

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9
Q

How do proteins differ?

A
  • Chemical composition (amino acid sequence)
  • Structure / shape
  • Functions e.g. transport, structural, enzymatic etc
  • Name (haemoglobin, insulin)
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10
Q

What are proteins made of?

A
  • Alpha amino acids
  • Amino acid are linked end to end by covalent bonds in linear chain
  • Amino acid chain known as a polypeptide
  • Polypeptide is folded into specific 3D shape
  • One or more folded polypeptides = protein
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11
Q

What is the primary structure of an amino acid?

A

Linear amino acid sequence

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12
Q

What is the secondary structure of a protein?

A

Polypeptide folding into regular shapes
Different secondary structures packed together = domain

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13
Q

What is the tertiary structure of a protein?

A

Tertiary structure - arrangement of one/ multiple domains
3D structure

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14
Q

What is the quaternary structure of a protein?

A

Arrangement of multiple polypeptides
Protein complex (multi-subunits)

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15
Q

General formula for amino acids?

A

R-CH(NH2)COOH

R = side chain
COOH = carboxyl group
NH2 = amino group
C = alpha carbon
H = alpha proton

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16
Q

What differs between the 20 naturally occuring amino acids in nature?

A

Side chains (R group)

17
Q

What is an amino acids at PH 7?

A

Zwitteron - it has both positive and negative charges

18
Q

Which is the only amino acid that is not chiral? Why?

A

Glycine
The side chain of glycine is H

19
Q

Isomers of amino acids?
Which is found in proteins in nature?

A

L and D
L are found in proteins in nature

20
Q

Which are ‘small and simple’ amino acids?

A

Glycine and alanine

21
Q

Which amino acids have hydrophobic side chains?

A

Valine (Val, V)
Leucine (Leu, L)
Isoleucine (IIe, I)
Methionine (Met, M)

22
Q

What can the amino acids Cystetine do?

A

Thiol group (-SH) can form disulphide bonds (S-S)

23
Q

Which amino acids have aromatic (ring) side chains?

A

Phenylalanine (Phe, F)
Tyrosine (Tyr, Y)
Tryptophan (Trp, W)

24
Q

Which amino acids have polar side chains?

A

Serine (Ser, S)
Threonine (Thr, T)

(Contains -OH group)

25
Q

Which amino acids are positively charged / basic?
What property does this give them?

A

Lysine (Lys, K)
Arginine (Arg, R)
Histidine (His, H)

Hydrophilic

26
Q

Which amino acids are negatively charged / acidic?

A

Aspartate (Asp, D)
Glutamate (Glutamate, E)

27
Q

Which amino acids are charged?

A

Aspartate (Asp, D)
Glutamate (Glu, E)

28
Q

What is different about the amino acid proline?

A
  • Side chain forms a five membered ring by bonding to the nitrogen atom
  • It is an Imino acid NOT amino acid
  • Proline side chain is often rigid and forces a sharp ‘bend’ in the main chain
29
Q

What bond are amino acids joined together with?
Where is the bond?

A

Covalent
Carbonyl group of one amino acids joins together the amino group on the next

30
Q

What type of reaction is polymerisation?
What is the reverse?

A

Condensation reaction
Reverse = hydrolysis

31
Q

What bond is between the C and N of two different amino acids in a polypeptide?

A

Peptide

32
Q

When / where do disulphide bonds occur?

A
  • Between side chains of two cysteine under oxidising condition
  • Tend to be found in proteins that are present extracellularly
  • Disulphide bonds can b cleaved by reduction with a reducing agent such as B-mercaptoethanol
33
Q

What can effect an amino acids properties?

A

Size
Charge
Hydrophobicity
Polar / non-polar

34
Q

What is sickle-cell anaemia caused by?

A

-Mutation that affects single amino acids joins together residue in haemoglobin B
- Glu and Val mutation

35
Q

What is cystic fibrosis caused by?

A

Deletion of single amino acid (Phenylalanine) in te transmembrane conductance regulator (CFTCR)

Molecules, Genes And Cells (1 decks)

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