Amino acids and Peptides Flashcards

1
Q

Role of proteins

A

Catalysis (glycogen synthase, DNA polymerase)
Transport (hemoglobin, lactose permease)
Structure (collagen, keratin)
Immunity (Antibodies, cytokines, chemokines)
Communication (hormones, neurotransmitters)
Motion (myosin, actin)

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2
Q

Describe the structure of an amino acid

A

-An acidic carboxyl group connected to the alpha carbon
-a basic amino group connected to the alpha carbon
-an alpha hydrogen connected to the alpha carbon
-a R group

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3
Q

Which is the only amino acid that isnt chiral?

A

Glycine

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4
Q

What kind of amino acids do proteins contain?

A

L-amino acids only

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5
Q

What are amino acids classified by?

A

The basis of R - group, nutrition, catabolism

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6
Q

How to tell if an amino acid is hydrophobic (non-polar)?

A

-If the R side chain is only made up of hydrocarbons - side chains don`t lose or gain protons or participate in hydrogen or ionic bonds
-Methionine is exception as contains sulfur
-If side chain is aromatic

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7
Q

Examples of hydrophobic amino acids

A

Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, Glycine, Phenylalanine, Tryptophan, Tyrosine

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8
Q

How to tell if an amino acid is hydrophyllic (polar)?

A

-Side chains are not just hydrocarbons - have charges - reactive with h2o
-Acidic if 2 carboxyl groups and 1 amino group
-Basic if 2 amino groups and 1 carboxyl group

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9
Q

Examples of hydrophyllic amino acids

A

Neutral - Serine, Threonine, Cysteine, Glutamine, Asparagine
Acidic - Glutamic acid, aspartic acid
Basic- Lysine, Histidine, Arginine

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10
Q

What are the 3 special amino acids?

A

Cysteine, Glycine, Proline

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11
Q

Why is Cysteine a special amino acid?

A

Sulfhydryl(thiol) group (-SH) of 2 cysteines can be oxidised to form a covalent cross link called a disulphide bond.

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12
Q

Why is glycine a special amino acid?

A

Simple side chain (R group) - JUST A HYDROGEN

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13
Q

Why is proline a special amino acid?

A

Its side chain and alpha - amino N form a rigid ring structure - contributes to the formation of protein collagen - often nfound at a bend or turn in a protein

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14
Q

At a low pH amino acids exist in a….

A

Positively charged form (cation) - amino group hasn´t been protonated yet so still holds its positive charge

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15
Q

At a high pH amino acids exist in a….

A

Negatively charged form (anion) - carboxyl group hasnt been protonated but amino group has so carboxyl group holds its negative charge

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16
Q

Between the pka for each group, the amino acid exists in a ……….

A

Zwitterion form - has both a pos and neg charge

17
Q

At the amino acid isoelectric point (PI)

A

The net charge is zero - amino acid is lest soluble in water and does not migrate in an electric field

18
Q

Amino acids withz uncharged side chains have how many pka values?

A

2 - the pka of the carboxyl group and the pka of the amino group

19
Q

What do buffers do?

A

Prevent changes in pH close to the pKa

20
Q

What are the 7 amino acids with ionizable side groups?

A

Terminal carboxyl group - aspartic acid/glutamic acid, histidine
Terminal amino group - Cysteine, tyrosine, lysine, arginine

21
Q

How many pkas do amino acids that have ionisable side chains have?

A

3

22
Q

Condensation / Dehydrolysis Rxn with respect to amino acids fusing

A

Carboxyl and amino groups from 2 adjacent amino acids fuse together

23
Q

How are amino acids read?

A

From the amino terminal to the carboxyl terminal

24
Q

What differences can be used to separate proteins?

A

Charge, size, affinity for a ligand, solubility, hydrophobicity, thermal stability