Important Molecules Flashcards

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1
Q

How are peptide bonds formed?

A

peptide bonds are formed by linking a carboxyl group of one amino acid with a a-amino group of another amino acid

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2
Q

What is a residue?

A

an individual amino acid part of a polypeptide chain

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3
Q

What is the “backbone” of a polypeptide chain?

A

N-C-C-N-C-C

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4
Q

What is an amino terminus?

A

the first end made during polypeptide synthesis

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5
Q

What is a carboxyl terminus?

A

the last end made during polypeptide synthesis

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6
Q

In the oligopeptide Phe-Glu-Gly-Ser-Ala, which residue has a free a-amino group, and which residue has a free a-carboxyl group?

A

Phe - amino group

Ala - carboxyl group

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7
Q

What is a protease?

A

a proteolytic enzyme that cleaves peptide bonds

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8
Q

What is cystine?

A

dimer of cysteine, residue that results from one cysteine residue besoms disulfide-bonded to another cysteine residue

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9
Q

What is a denatured protein?

A

non-functional protein that is improperly folded. the protein’s shape is disrupted without breaking peptide bonds.

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10
Q

How does urea affect protein?

A

urea disrupts hydrogen bonding by extremes of pH, extremes of temperature, and changes in salt concentration

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11
Q

Primary Structure

A

simplest level of protein structure, the same as sequence

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12
Q

Secondary Structure

A

initial folding of a polypeptide chain into shapes stabilized by hydrogen bonds between backbone NH and CO groups

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13
Q

Parallel B-pleated sheets vs anti-parallel B-pleated sheets?

A

parallel sheets have polypeptide chains running in the same direction, anti-parallel have sheets running in the opposite direction

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14
Q

If a single polypeptide folds once and forms a B-pleated sheet with itself, would this be a parallel or anti-parallel B-pleated sheet?

A

Anti-parallel

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15
Q

Tertiary Structure

A

protein folding that concerns interaction between amino acid residues located more distantly from eachother

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16
Q

Which of the following may be considered an example of tertiary protein structures?
I. van der Waals interactions between two Phe R-groups located far apart on a polypeptide
II. Hydrogen bonds between backbone amino acids
III. Covalent disulfide bonds between cysteine residues located far apart on a polypeptide

A

I and III

17
Q

What is a polypeptide subunit?

A

a single polypeptide chain that is part of a large complex containing many subunits

18
Q

Quaternary Structure

A

highest level of protein structure, the arrangement of subunits in a multisubunit complex

19
Q

What is the difference between a disulfide bridge involved in a quaternary structure and one involved in tertiary structure?

A

quaternary disulfides are bonds that form between chains that aren’t linked by peptide bonds. tertiary disulfides are bonds that form between residues in the same polypeptide.

20
Q

Why do fatty acids end in a carboxylic acid?

A

the chains are synthesized two carbons at a time for acetate

21
Q

How does the shape of an unsaturated fatty acid differ from that of a saturated fatty acid?

A

an unsaturated fatty acid is bent or kinked the double bond

22
Q

If fatty acids are mixed into water, how are they likely to associate with each other?

A

the long hydrophobic chains will interact with each other to minimize contact with water, exposing the charged carboxyl group the aqueous environment

23
Q

Would a saturated or an unsaturated fatty acid residue have more van Der Waals interaction with a neighboring alkyl chain in a bilayer membrane?

A

a saturated fatty acid would have more van Der Waals interactions. the bent shape of the unsaturated fatty acid means that it doesn’t fit in as well and has less contacted with neighboring groups

24
Q

What are the structural determinants of membrane fluidity?

A

degree of saturation, tail length, and amount of cholesterol

25
Q

How do double bonds affect membrane fluidity?

A

double bonds tend to increase membrane fluidity

26
Q

How does length affect membrane fluidity?

A

decreasing the length of a fatty acid tails increase fluidity

27
Q

How does cholesterol affect membrane fluidity?

A

increases fluidity at low temps, decreases fluidity at high temps; keeps fluidity at an optimum level

28
Q

How are linked phosphates able to provide so much energy?

A

linked phosphates act as a compressed spring waiting to fly open and provide energy