Aminoacids and Proteins Flashcards

1
Q

What is a Ketogenic amino acid?

A

Ketogenic amino acids are those amino acids that are converted to acetyl CoA or Acetoacetate which are precursors to ketone bodies

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2
Q

What are Glucogenic amino acids?

A

Are those amino acids which are converted to precursors for glucose synthesis like alpha-ketoglutarate, succinyl CoA, Fumarate

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3
Q

What is the general structure of all amino acids except for Glycine

A

The alpha carbon is a chiral center.

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4
Q

Name all amino acids in the Non-polar, aliphatic group

A
  1. Glycine 2. Alanine 3. Proline 4. Valine 5. Leucine 6. Isoleucine 7. Methionine
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5
Q

Name all amino acids in the Aromatic group

A
  1. Phenylalanine 2. Tyrosine 3. Tryptophan
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6
Q

Name all amino acids in the Polar, uncharged group

A
  1. Serine 2. Threonine 3. Cysteine 4. Asparagine 5. Glutamine
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7
Q

Name all amino acids in the Positively charged group

A
  1. Lystine 2. Histidine 3. Arginine
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8
Q

Name all amino acids in the Negatively charged group

A
  1. Asparate 2. Glutamate
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9
Q

Stereoisomerism in Alpha aminoacids

A
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10
Q

The amino acids are all chiral except for ______?

A

Glycine

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11
Q

All naturally occurring proteins from all living organisms conist of (L or D) Amino acids?

A

L amino acids

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12
Q

What is a zwitterion?

A

A zwitterion is neutral molocule with a positive AND a negative electrial charge, though multiple positive and negative charges can be present

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13
Q

Define a Protein

A

Proteins are polymers built from amino acids joined by PEPTIDE BONDS

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14
Q

Explain the different structures of Proteins (ie) Primary, secondary ect….

A
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15
Q

Give an example of how a single amino acid can alter the function of a protein

A

Normal red blood cells to sickle cell blood cells…. just one amino acid is changed and completely changes the function of the cell.

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16
Q

Define Proteostasis

A

Refers to the process by which cells control the abundance and folding of the proteome, and consists of a highly interconnected network that integrates the regulation of gene expression, signaling pathways, molecular chaperones and protein degredation systems.

17
Q

What CANT a protein lose even when it is denatured?

A

A protein can never lose its PRIMARY structure even when denatured. When a protein is in its Unfolded state, it becomes inactive.

18
Q

What famous disease is related to Collagen

A

Scurvy (Vitamin C defiency)

Osteogenesis Imperfecta: a person has too little type I collagen or a poor quality of type I collagen due to a mutation in one of the type I collagen genes

19
Q

Explain the steps of Collagen Synthesis

A