Chapter 2 - Protein Composition and Structure Flashcards

1
Q

Proteins are linear polymers built of monomer units called

A

amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Primary structure of a protein

A

The sequence of amino acids linked end to end.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Secondary structure of a protein

A

The 3d structure formed by hydrogen bonds between amino acids near one another.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Tertiary structure of a protein

A

Formed by long-range interactions between amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Enzymes

A

The proteins that catalyze specific chemical reactions in biological systems.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Zwitterions

A

A molecule or ion having separate positively and negatively charged groups.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

The R group of an amino acid is often referred to as the

A

side chain.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Which isomer of amino acids are constituents of proteins?

A

L amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

For all amino acids, the L isomer has ___ absolute configuration.

A

S

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

In acidic solution the amino group of an amino acid is

A

protonated (-NH3+).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

In acidic solution, the carboxyl group of the amino acid is

A

not dissociated (-COOH).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

As the pH is raised, the first group to give up a proton in an amino acid is the

A

carboxylic acid.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

The protonated amino group in an amino acid loses a proton around pH

A

9

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The only achiral amino acid is

A

glycine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Which amino acids have more than 1 chiral center?

A

Isoleucine and threonine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

How many amino acids have readily ionizable side chains?

A

7

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Peptide bond (or amide bond)

A

Formed by linking the alpha-carboxyl group of one amino acid to the alpha-amino group of another amino-acid.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

The formation of a dipeptide is accompanied by the loss of a

A

water molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

The lifetime of a peptide bond in aqueous solution in the absence of a catalyst approaches ______ years.

A

1000

20
Q

Each amino acid unit in a polypeptide is called a

A

residue.

21
Q

Main chain (or backbone)

A

Regularly repeating part of a polypeptide chain.

22
Q

The polypeptide backbone is rich in ______ bonding potential.

A

Hydrogen

23
Q

The largest known polypeptide is ______ which consists of more than ______ amino acids.

A

Titin; 27000

24
Q

Oligopeptides

A

Peptide chains made of small numbers of amino acids.

25
Q

The most common cross links are

A

disulfide bonds.

26
Q

Disulfide bonds form by

A

the oxidation of a pair of cysteine residues.

27
Q

Cystine

A

The result of two linked cysteines.

28
Q

The amino acid sequences of proteins are determined by

A

the nucleotide sequences of genes.

29
Q

A peptide bond is essentially planar or nonplanar?

A

planar

30
Q

A peptide bond cannot rotate because

A

the bond resonates between a single and double bond with the C=O group.

31
Q

Almost all peptide bonds are (cis or trans)

A

trans.

32
Q

The most common cis peptide bonds are

A

X-Pro linkages

33
Q

phi

A

The angle of rotation about the bond between the nitrogen and the alpha-carbon atoms.

34
Q

psi

A

The angle of rotation about the bond between the alpha-carbon and the carbonyl carbon atoms.

35
Q

The phi and psi angles determine

A

the path of the polypeptide chain.

36
Q

Some diseases resulting from improperly folded proteins.

A
  • Parkinson disease
  • Huntington disease
  • transmissible spongiform encephalopathies (prion disease)
37
Q

Alpha helices, beta strands, and turns are formed by

A

a regular patter of hydrogen bonds between the peptide N-H and C=O groups of amino acids near each other in the linear sequence.

38
Q

The alpha helix is stabilized by

A

hydrogen bonds between the NH and CO groups of the main chain.

39
Q

The CO group of each amino acid forms a hydrogen bond with the NH group of the amino acid that is ______ residues ahead in the sequence.

A

four

40
Q

Number of amino acids residues per turn in an alpha helix.

A

3.6

41
Q

The pitch of the alpha helix is the

A

length of one complete turn along the helix axis.

42
Q

The pitch of the alpha helix is equal to

A

the product of the rise (1.5 A) and the number of residues per turn (3.6), or 5.4 Angstroms.

43
Q

Essentially, all alpha helixes formed in proteins are ______ handed.

A

right

44
Q

Beta sheets are stabilized by

A

hydrogen bonding between polypeptide strands.

45
Q

A beta sheet is formed by

A

linking two or more beta strands lying next to one another through hydrogen bonds.