Amino Acids Flashcards

Learning the structure and classification of amino acids.

1
Q

Proline

A

Non-Polar. Proline is the exception in which all other amino acids are α-amino acids. Proline is a secondary amine, therefore it is called an imino acid.

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2
Q

What are the amino acids have side chains which are uncharged rings, linear or branched hydrocarbon chains, with an even distribution of charge?

A

i.e. non-polar (hydrophobic/lypophillic) R- goups.
Glycine, Alanine, Isoleucine, Leucine, Valine, Methionine, Phenylalanine, Tryptophan, Proline.
Exceptions: Met and Trp have a polar atom, but the electronegativity is masked by surrounding hydrocarbons.

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3
Q

Glycine

A

non-polar, R-group = H. This aa is the exception in that is the only aa that is achiral. (not chiral)

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4
Q

Alanine

A

non-polar, R-group = methyl

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5
Q

Isoleucine

A

non-polar, R-group = branched chain hydrocarbon

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6
Q

Leucine

A

non-polar, R-group = branched chain hydrocarbon

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7
Q

Valine

A

non-polar, R-group = branched chain hydrocarbon

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8
Q

Methionine

A

non-polar, R-group contains Sulfur

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9
Q

Phenylalanine

A

non-polar, R-group contains an aromatic ring

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10
Q

Tryptophan

A

non-polar, R-group contains an aromatic ring

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11
Q

What kind of interactions are there between amino acids with non-polar R-groups?

A

Non-polar side chains are hydrophobic and tend to aggregate in water to avoid the polar H2O, forming hydrophobic interactions.

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12
Q

Hydrophobic effect

A

formation of the hydrophobic core in the inside of the proteins. It is a major force behind the folding of globular proteins

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13
Q

What are the amino acids with uncharged, polar R-groups? (one or more electronegative atoms (O, N, S) in the side chain, and electrically neutral at physiological pH)

A

Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine

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14
Q

Which amino acids have an aromatic ring associated with it’s R-group.

A

Tryptophan (non-polar), Phenylalanine (non-polar), Tyrosine (R-group = OH; polar, uncharged)

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15
Q

Which amino acids have a hydroxyl (-OH) group associated with the R-group?

A

Serine, Threonine and Tyrosine. These are polar and uncharged at physiological pH. These can undergo H-bonding interactions with other molecules. These amino acids are sites for post-translational modification, in which phosphates or carbs attach to their -OH group.

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16
Q

Cysteine

A

Polar, uncharged R-group. Contains a sulfhydryl (-SH) group. Undergoes H-Bonding interactions, but cysteine is the only amino acid that can form disulfide bonds. Cysteine is modified into selenocysteine, in which selenium replaces the S of cysteine.

17
Q

Post-translational modification

A

Amino acids provide sites for post-translational modifications, which are essential in some proteins.

1) attachment of phosphates or carbs to the -OH group of serine, threonine or tyrosine.
2) Proline and Lysine are hydroxylated in mature collagen.

18
Q

Disulfide bonds

A

Strong bonds formed upon an oxidation reaction between two cysteines. Cysteine is the only amino acid that can form S-S bonds. The resulting dimer of cysteines is named cystine. As opposed to H-bonds and ionic bonds, which are weak bonds, disulfide bridges are covalent, strong bonds.

19
Q

cystiene

A

the resulting dimer of two cysteines covalently attached to one another via S-S disulfide bond.

20
Q

What are the amino acids with polar and uncharged R-groups?

A

Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine

21
Q

Serine

A

polar, uncharged hydroxyl (-OH) R-group. Can undergo H-bond interactions. Also, can be post-translationally modified by attaching a phosphate or carb to the -OH group.

22
Q

Threonine

A

polar, uncharged hydroxyl (-OH) R-group. Can undergo H-bond interactions. Also, can be post-translationally modified by attaching a phosphate or carb to the -OH group.

23
Q

Tyrosine

A

polar, uncharged hydroxyl (-OH) R-group. Can undergo H-bond interactions. Also, can be post-translationally modified by attaching a phosphate or carb to the -OH group. This amino acid also contains and aromatic ring.

24
Q

What amino acids have polar and charged side chains?

A

Acidic:
Glutamic acid (glutamate), aspartic acid (aspartate)
Basic:
Arginine (positive charg), lysine (positive charge) histidine (charge is between 0 and +1) (ie. HAL)

25
Q

Acidic amino acids

A

(GLAS [GLutamate and Aspartate) Polar and charged; Glutamic acid (a.k.a. glutamate) and aspartic acid (a.k.a. aspartate). These have side chains contain -COOH groups that are dissociated and negatively charged at physiological pH.

26
Q

Basic Amino Acids

A

(HAL) Side chain positively charged at physiological pH, except His.
Arginine (positive charg), lysine (positive charge) histidine (charge is between 0 and +1) (ie. HAL)

27
Q

Which amino acids undergo hydrophobic reactions?

A

Non-polar

28
Q

Which amino acids undergo H-bonds?

A

Any polar amino acid

29
Q

Which amino acids undergo disulfide bonds?

A

cysteine

30
Q

Which amino acids undergo ionic bonds?

A

polar, charged amino acids can do both H-bond and ionic bonds

31
Q

Low pKa means _____ , low pH means _____

A

Low pKa means a stronger acid (more easily let’s go of its H+. Low pH solution means that it is an acidic solution. pKa (1) sauce. pKa near 1 is really strong and pH at 1 is extremely acidic