Proteins Flashcards

1
Q

Identify at least 4 different roles of proteins.

A

Catalysis, structure, transport, binding, signaling.

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2
Q

What are the different groups of amino acids?

A

Non-polar, polar, non-ionizable, basic, acidic.

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3
Q

Cysteine is a polar, non-ionizable amino acid. T/F

A

False. It is ionizable and uncharged.

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4
Q

Leucine is a basic amino acid. T/F

A

False. Leucine is neutral.

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5
Q

Phenylalanine is a non-polar amino acid. T/F

A

False. It is negative.

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6
Q

Aspartate is an acidic amino acid. T/F

A

True.

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7
Q

Threonine is a polar, non-ionizable amino acid. T/F

A

True.

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8
Q

List at least 2 different types of post translational modification.

A

Phosphorylation, acetylation, hydroxylation, methylation.

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9
Q

The amine on one amino acid can react with the carboxylate on another one.

A

True. That is how peptides form.

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10
Q

One amino acid can react with another to form a peptide bond between them. T/F

A

True.

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11
Q

If the two amino acids are cysteines, they can react to form a disulfide bridge. T/F

A

True.

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12
Q

An amide bond can form due to the reaction of one amino acid with another. T/F

A

True.

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13
Q

Rank from the smallest to the largest the following: protein, peptides, polypeptide.

A

Protein, peptide, polypeptide.

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14
Q

Primary structure is held together by peptide bonds. T/F

A

True.

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15
Q

Secondary structure is held together by hydrophobic interactions. T/F

A

(False?) hydrogen bonds

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16
Q

Tertiary structure is held together by hydrophobic interactions. T/F

A

True. Depending on the environment.

17
Q

Quaternary structure is held together by hydrogen bonds (and other interactions). T/F

A

True. Non-covalent bonds, which are hbonds

18
Q

“Glycine-isoluecine-valine-glutamate-glutamine…” begins to spell out which part of the structure. Of the protein insulin? Its _____ structure.

A

N terminus

19
Q

What are the differences between primary structure, secondary structure, tertiary structure and quaternary structure of a protein?

A

Primary: peptide chain, peptide bonds
Secondary: Alpha helix, beta sheet, hydrogen bonds.
Tertiary: Increased folding, non-polar core. Hydrogen bonds.
Quaternary structure: Subunit complexes.

20
Q

You can’t rotate around the peptide bond, because of the double bond character. T/F

A

True

21
Q

All of the rotatable bonds in the backbone can achieve any bond angle. T/F

A

False. Rotation is limited by the peptide bond.

22
Q

The bonds before and after the alpha carbon are the rotatable bonds in a protein. T/F

A

True.

23
Q

Some of the bond angles are prohibited due to steric conflict. T/F

A

True

24
Q

What are the similarities and differences between alpha helices and beta sheets?

A

Alpha helix: non-adjacent amino acids interact with Hbon.
Beta sheet: hbond between adjacent amino acids. Antiparrallel.

25
Q

There are no regions between the secondary structures within a tertiary structure. T/F

A

False, turns and loops

26
Q

The regions between secondary structures are usually called random coil regions. T/F

A

False. Random coils pertain to primary structure.

27
Q

How many tertiary structures come together to form quaternary structure?

A

2+

28
Q

Fibrous proteins are not very abundant or important in humans. T/F

A

False. Collagen is one of the most abundant

29
Q

Protein folding is faily well understood now that crystalography is worked out.T/F

A

True

30
Q

Hydrophobic collapse is involved in some proteins but probably not the majority. T/F

A

Hydrophobic side chains will connect in a non-aqueous environment.

31
Q

The information that directs the process of the folding of a protein comes from ____.

A

DNA

32
Q

Proteins all have failry rigid structures. T/F

A

Depends on the protein.

33
Q

Proteins have greatly varying amounts of flexibility. T/F

A

True.

34
Q

Some proteins are quite rigid while others “breathe” a lot more. T/F

A

True

35
Q

A few proteins are so flexible that their entire structure can alter. T/F

A

True. Lactoferrin, glycine