Proteins and Quality Control Flashcards

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1
Q

What Are Molecular Chaperones?

A

proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures

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2
Q

What are Chaperonins?

A

Proteins that facilitate folding of mis folded proteins

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3
Q

Acetylation

A

process where an acetyl functional group is transferred from one molecule (in this case, Acetyl-Coenzyme A) to another

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4
Q

Phosphorylation

A

post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group

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5
Q

Glycosylation

A

reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule

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6
Q

Hydroxylation

A

chemical process that introduces a hydroxyl group (-OH) into an organic compound

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7
Q

Methylation

A

a process by which methyl groups are added to the DNA molecule. Methylation can change the activity of a DNA segment without changing the sequence

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8
Q

Carboxylation

A

a chemical reaction in which a carboxylic acid group is introduced in a substrate

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9
Q

What are some forms of protein Modifications?

A

Acetylation, Phosphorylation, Glycosylation, Hydroxylation, Methylation, Carboxylation

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10
Q

What are 3 ways Proteins are Degradated?

A
  1. Within lysosomes
  2. Degestive proteases
  3. Ubiquitin-mediated protein degradation
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11
Q

What is Ubiquitin?

A

is a small regulatory protein that has been found in almost all tissues. The addition of ubiquitin to a substrate protein is called ubiquitination or ubiquitylation

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12
Q

How can Ubiquitin effect proteins?

A

Ubiquitination can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions

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13
Q

Sepcificity

A

ability of one protein to bind one molecule in preference to another

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14
Q

Affinity

A

strength of binding

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15
Q

What is an example of an Enzyme working as a catalyst?

A

Kinases

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16
Q

Kinases

A
  1. Contain an ATP-binding site which is highly conserved

2. Transfer phosphate groups to proteins to induce changes in protein structure

17
Q

What is need for High affinity interactions to take place?

A

The binding site of the protein must be complementary to the ligand molecule

18
Q

CDRs

A

Complementarity-determining Regions of antibodies that are highly variable

19
Q

Epitope

A

portion of a protein bound by an antibody

20
Q

Protein Scaffolds

A

known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes

21
Q

What are some examples of molecular motors?

A

Ribosomes, Myosin, Kinesins, Dynein, RNA polymerase and DNA polymerase

22
Q

How does the Kinase/Phosphatase Switch Work?

A

Protein Kinase Phosphorylates the switch proteins using ATP causing it to go inactive. Protein Phosphatase dephosphorylates the switch proteins using H20 causing it to become active