L8 Flashcards

1
Q

What are all proteins encoded by?

A

Genes

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2
Q

Name 6 functions proteins perform (receptors, hormones etc)

A

Structural proteins = Actin, Micro-tubules, intermediate filaments

Secereted proteins = Hormones

Membrane bound proteins = Receptors

Molecular motors = DNa helicase

Secreted structural proteins = cartialage

Intracellular proteins = cytosolic signalling molecules

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3
Q

How many genes encode proteins?

A

20,000

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4
Q

What are the difference between essential and non-essential amino acids?

A

Non-essential are made by the body from the essential AA or by breakdown of proteins.

Essential AA come from food in our diet..

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5
Q

What bonds are AA held together by and how are they formed?

A

AA held by peptide bonds, formed by condensation reaction to form a covalent bond.

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6
Q

How many AA do proteins contain?

A

Usually from 50-2000

Can be 30-10,000

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7
Q

Name 4 secondary structures of protein

A

a-helices
b-pleated sheets
Loops and turns
Random coils

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8
Q

What is the structure of an a-helix

A

Polypeptide backbone foldied into a spiral formed as H bonds form between carbonyl group and amine group 4aa along the chain
3.6 aa per turn
side chains face outwards

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9
Q

Where are a-helices abundant and why

A

Abundant in membrane proteins
Hydrophobic side chains interact w hydrophobic H-C tails of phospholipids
Hydrophilic backbone shielded from lipid environment and form H bonds

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10
Q

What is the b-sheet structure?

A

Flat structure(sheet)
Laterally packed strands
Each strand w 5-8AA
Shape due to H bonds between carbonyl group and amine group of neighbouring chain
Side chains extend above and below b-sheet

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11
Q

Describe the secondary structure “loops and turns”

A

3-5 AA long, form sharp bend redirecting polypeptide backbone
Hydrophilic residues found on surface of proteins

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12
Q

Describe the secondary structure “random coils”

A

Polypeptide chains w random configuration

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13
Q

How are tertiary structures formed? Name 3 tertiary structures

A

Secondary structure spontaneously fold into 3D conformations
Myoglobin
Tumour necrosis factor alpha
Barrels - 1st/last strand form H bonds forming a barrel

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14
Q

What is a coiled coil?

2 examples

A

2/3 a-helices wound around each other. Hydrophobic AA line up where helices meet.
Keratin
Collagen

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15
Q

What is a post translational modification (PTM)?

A

Covalent processing event from proteolytic cleavage(breaking of peptide bonds between AA) or addition of a modifying group
They modulate function of most eukaryote proteins by altering activity state, localization, turnover and interactions w other proteins.

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16
Q

When is protein denaturation permanent and when is it reversible?

A

Solvent denature proteins disrupting non-covalent interaction losing secondary and tertiary structures. But when solvent is removed the protein will renature

Heat can denature protein but it is irreversible denatured e.g. cooking an egg

17
Q

What is assisted folding?

What are the two classes that assist in folding?

A

Molecular chaperones bind to partially folded polypeptide chains and assist in folding

Two classes are: Heat shock proteins
Chaperonins

18
Q

What is protein charge dependent on>?

A

The AA side chains for example, carboxylic group :glutamic acid and aspartic acid will be negative
Whereas, N group: lysine, arginine, histidine will be positive

19
Q

What is a protein domain?

A

Part of the protein tertiary structure that can exist independently of the rest of the protein chain. The domains can independently fold and be stable.

20
Q

What is the signal sequence?

What happens if a protein does not have 1?

A

Protein leaves ribosome, part of AA sequence will contain the signal sequence to provide info of correct location of protein.

Proteins with none remain in the cytosol

21
Q

What causes cystic fibrosis?

A

DNA mutation that alters protein shape.

The deletion causes mutant CTFR protein to become stuck in ER and abnormal chloride conductance occurs.

22
Q

What causes Creutzfeldt-Jakob disease (CJD)?

A

Misfolding proteins.
Normal protein adopt misfolded prion
This binds to normal protein inducing conversion to abnormal conformation
Abnormal prions form tightly pakced b-sheets that are very stable
Misfolded prions build up in the brain forming amyloid plaques cause progressive slow death of nerves in the brain