Amino Acid to polypeptides to protein. Flashcards

1
Q

Amino acids are joined during translation by peptidyl transferase (main function of ribosome). what brings amino acids to ribosome?

A

tRNA bring AA to ribosome, which reacts to other tRNA. Carboxyl group reacts with amino group on new amino acid, there is a condensation reaction -OH- lost from carboxyl & -H+ lost from amino.

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2
Q

What is the smallest & largest proteins?

A

TAL in fruit flies, 11aa.
Titin in humans 34,350 aa.

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3
Q

Explain secondary structure.

A

hydrogen bonds between N-H & C=O, there is a a-helix (coiled strand), & a Beta-sheet, parallel or anti depending on alignment of strands, anti-parallel is more stable.

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4
Q

Explain tertiary structure.

A

most stable, lowest energy. held by interactions between R-groups ; disulphide bridges, ionic bonds, hydrogen bonds, van Der Waals interactions.

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5
Q

What is incorrect folding or misfiling of proteins often related to?

A

Protein aggregation & fibrillogenesis which is connected to diseases such as; BSE, Huntingtons and Alzheimers disease.

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6
Q

How do you figure out how proteins fold?

A

You find out how they denature. An unfolding process and not a disruption of the peptide bonds.

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7
Q

what is it called when hydrophobic groups come together to avoid water?

A

Hydrophobic collapse.

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8
Q

what are oligomeric proteins made up of?

A

Multiple proteins held together by non-covalent bonds.oligomeric proteins are easier to repair.

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9
Q

alanine to pyruvate.

A

alanine loses its amino group by transamination to form pyruvate catalysed by alanine aminotransferase.

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10
Q

asparagine to oxaloacetate.

A

asparagine to hydrolysed by asparaginase liberating ammonia and aspartate. aspartate loses its amino group by transamination via the enzyme aspartate aminotransferase to form oxaloacetate.

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11
Q

amonitransferases catalyse the reversible transamination between an amino acid and a ketone acid, giving rise to 1 of 3 non essential amino acids…

A

a-ketoglutarate-glutamate.
pyruvate - alanine.
oxaloacetate - aspartate.

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12
Q

what is the prosthetic group?

A

Compounds bound to enzymes and their change from 1 form to another and back takes place in a single catalytic cycle.

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13
Q

pyridoxal phosphate is the active form of what?

A

pyridoxine (vitamin b6)

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14
Q

glutamine is converted to glutamate and ammonia by enzyme glutaminase…

A

glutamate is converted to a-ketoglutarate by oxidative deamination by glutamate dehydrogenase.

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15
Q

threonine and serine can have amino group directly converted to ammonium. (NH4+)

A

Serine to pyruvate by serine dehydratase & threonine to a-ketaglutarate by threonine dehydratase.

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16
Q

Describe dehydratase enzymes.

A

H2O is lost in these reactions, serine loses H+ & -OH group from a- and b- carbons respectively, forming unstable intermediate aminocrylate. H2O is then added back, producing the products. PLP is cofactor.

17
Q

Urea cycle, what’s steps in mitochondria ?

A

1) Carbamoyl phosphate synthase & 2) ornithine transcarbamylase.

18
Q

Urea cycle ; what’s the in cytosol?

A

3) arginosuccinate synthase
4) arginosuccinate lyase
5) arginase

19
Q

The urea cycle and Krebs cycle are interlinked through…

A

argininosuccinate.

20
Q

The c3 family are converted to pyruvate, name the three groups.

A

serine, alanine, cysteine.

21
Q

The c5 family, enter the citric acid cycle as a-ketoglutarate through glutamate.

A

Proline, histidine, glutamine, arginine.

22
Q

What are non-polar amino acids forming succinylcholine CoA?

A

Leucine, isoleucine, valine.

23
Q

isoleucine & valine

A

Propionyl-CoA to succinyl-CoA

24
Q

Leucine

A

Acetoacetate and acetyl-CoA for ketone body production.

25
Q

The first step to forming succinyl-coa is a transaminase reaction producing the appropriate a-keto acid. Creating a branched chain a-keto acid dehydrogenase complex.

A

Followed by a series of oxidation/reduction reactions similar to TCA cycle.