Proteins Flashcards

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
Q

Heat Shock Proteins

A

Protect from being denatured and broken down

26
Q

Hemoglobin has 4 polypeptide subunits folded together. This level of protein structure is called

A

Quaternary

27
Q

Molecules containing an amino acids would be

A

A weak base

28
Q

Which amino acid can form disulphide bonds?

A

Cystine (important in protein folding)

29
Q

Importance of Glycine?

A

It is small and fits into tight corners

30
Q

Why is Proline a special case?

A

It has a ring structure that limits hydrogen-bonding ability.