Proteins Flashcards

(30 cards)

1
Q

Living organisms are

A

Carbon-based

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2
Q

Backbone of biological materials?

A

Hydrocarbons

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3
Q

Four kinds of macromolecules?

A

Proteins, Carbohydrates, Lipids, Nucleic acid

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4
Q

Proteins are

A

Combination of 20 amino acids

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5
Q

Isomers?

A

Same formula, different structure of compounds.
Cis: Same atoms on same side
Trans: Diff atoms on same side

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6
Q

Enantiomers?

A

Molecules that differ in spatial arrangement

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7
Q

Hydrolysis

A

Chemical reaction where water is used to break down chemical bonds

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8
Q

Proteins are held together by what type of bonds?

A

Peptide bonds (covalent)

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9
Q

Are D-amino acids or L-amino acids found in living things?

A

L-amino acids

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10
Q

The “capital letter” is the amino group of the 1st amino acid

A

N-terminus

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11
Q

The “period” is the carboxyl group of the last amino acid

A

C-terminus

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12
Q

Amino acids with positively charged, hydrophilic side chains

A

Arginine (R), Histidine (H), Lysine (K)

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13
Q

Amino acids with negatively charged, hydrophilic side chains

A

Aspartic acid (D), Glutamic acid (E)

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14
Q

Amino acids with polar, uncharged side chains

A

Serine (S), Threonine (T), Asparagine (N), Glutamine (Q), Tyrosine (Y)

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15
Q

Amino acids with non-polar hydrophobic side chains

A

Alanine (A), Isoleucine (I), Leucine (L), Methionine (M), Phenylalanine (F), Tryptophan (W), Valine (V)

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16
Q

Special cases

A

Cysteine (C), Glycine (G), Proline (P)

17
Q

Cysteine may form what type of bond?

A

Disulphide bond b/c it has a SH group

18
Q

Primary structure

A

The linear sequence of amino acids within a protein

19
Q

Secondary Structure

A

Alpha-helix and Beta-pleated sheets

20
Q

Tertiary Structure

A

3-dimensional configuration/ interaction of R-groups and the environment

21
Q

Quaternary Structure

A

Interactions of sub-units

22
Q

Condition that affect protein folding

A

High temperature, pH changes, High concentrations of polar molecules, nonpolar substances

23
Q

Denaturation

A

Folded protein structure is broken down due to extreme conditions

24
Q

Chaperones

A

Proteins that help prevent other proteins from binding to the wrong molecules

25
Heat Shock Proteins
Protect from being denatured and broken down
26
Hemoglobin has 4 polypeptide subunits folded together. This level of protein structure is called
Quaternary
27
Molecules containing an amino acids would be
A weak base
28
Which amino acid can form disulphide bonds?
Cystine (important in protein folding)
29
Importance of Glycine?
It is small and fits into tight corners
30
Why is Proline a special case?
It has a ring structure that limits hydrogen-bonding ability.