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BIOL340 > BIOL340 Proteostasis (3.1) > Flashcards

BIOL340 Proteostasis (3.1) Flashcards

1
Q

What is a protein?

A

Linear chain of amino acids encoded by a DNA blueprint

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2
Q

What is the proteome?

A

Genomes encode all proteins that form the proteome

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3
Q

What state are proteins functional in?

A

Folded, Native Scape

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4
Q

What are the levels of protein structure?

A

Primary, Secondary, Tertiary, Quaternary

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5
Q

What is a domain?

A

Spatially-disctinct modules of a protein, functioning in semi-independence

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6
Q

How are domains grouped?

A

Into families based on structural similarities

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7
Q

What level of structure determines 3D structure?

A

Primary Structure

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8
Q

What is Levinthal’s Paradox?

A

Proteins have an infinite number of conformations, but folding only takes seconds/minutes

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9
Q

What state are folded proteins in?

A

The most thermodynamically favourable, having the lowest energy.

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10
Q

What are the two main folding pathways?

A

Hydrophobic Collapse and Nucleation of Folded Domains

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11
Q

Describe hydrophobic collapse

A

Hydrophobic residues find each other in the protein, causing collapse

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12
Q

Describe nucleation of folded domains

A

Local interactions form secondary structure, with one domain folding leading to further folding

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13
Q

Where are the hydrophobic residues?

A

Internalised

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14
Q

What is the major concept of proteostasis?

A

Turn over of proteins, and the maintenance of proteins

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15
Q

When does protein misfolding occur?

A

In the disordered state

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16
Q

What forms an amporphous precipitate?

A

Amorphous aggregation pathway; Fast, disordered aggregates

17
Q

What forms a fibril

A

amyloid fibril pathway; slow and highly ordered

18
Q

Are aggregates visible in solution?

A

Yes

19
Q

What is needed for a diagnosis of Alzheimers?

A

Protein aggregate formation in the brain

20
Q

What are some common aggregation related diseases?

A

Alzheimers, parkinsons, systemic amyloidosis,

21
Q

What are the areas of protoestasis control?

A

Extracellular proteostasis, synthesis and folding, aggregation, HSPs, UPS, ERAD, Autophagy

22
Q

What are the fates for non-native proteins

A

Rescue by chaperones
Degradation by proteases
Aggregation

23
Q

Describe the general features of chaperones

A

recognise and bind non-native proteins, assiting in folding and assembly, as well as prevenitng protein aggregation

24
Q

Describe general fetarues of holdases

A

Bind hydrophobic regions, protecting from inappropriate interactions; Hold but do not refold; ATP independent

25
Q

Describe general features of foldases

A

Faciliatate correct folding by regulated binding and release; ATP-dependent; prevent inappropriate interactions

26
Q

Describe foldase chaperone (Hsp70) action

A

Polypeptide emerges from ribosome; Hsp70 chaperones bind to elongating polypeptide; Hsp70 shields from inappropriate interactions; Release of polypeptide for proper folding

27
Q

Describe foldase chaperone Hsp60 action

A

non-native protein binds to hydrophobic region inside GroEL; GroES attaches; GroEL cavity increases, protein refolding occurs; ATP hydrolysis and GroES is released; Folded protein released

28
Q

What are the 2 ways of protein degradation?

A

proteasome and lysosome

29
Q

What does the proteasome do

A

Chops protein into singular amino acids

30
Q

How does the proteasome work

A

non-native protein recognised by ubiquitin ligases; poly-ubiquitinated protein binds to cap of proteasome; ubiquitin is removed and protein is fed into chamber; amino acids cut and released

31
Q

What motif is recognised in chaperone mediated autophagy?

A

KFERQ, recognised under stress

32
Q

What does recognition of KFERQ do

A

direction to lysosomes

33
Q

What is the purpose of the aggregosome

A

Moves aggregated proteins to one point to have a central point for machinery to act

34
Q

What occurs in uncontrolled aggregation

A

Formation of an inclusion body

BIOL340 (5 decks)

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