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Bio 3A > Chapter 5 - The Structure And Function Of Large Biological Molecules > Flashcards

Chapter 5 - The Structure And Function Of Large Biological Molecules Flashcards

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0
Q

Three classes of macromolecules

A

Proteins
Carbohydrates
Nucleic acids

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1
Q

The most important large molecules in living things

A

Proteins
Lipids
Carbohydrates
Nucleic acids

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2
Q

Polymers

A

Chain-like molecules (macromolecules). Long molecules consisting of many similar or identical building blocks linked by covalent bonds

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3
Q

Monomers

A

The repeating units that serve as the building blocks of polymers

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4
Q

Enzymes

A

Specialized macromolecules that speed up chemical reactions (chemical mechanisms that cells are and break down polymers)

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5
Q

Dehydration reaction

A

Reaction in which two molecules are covalently bonded to each other, with the loss of a water molecule (Monomers connected to these)

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6
Q

How monomers attach to polymers?

A

The polymer and monomer contribute a part of the water molecule lost and attach to each other covalently

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7
Q

Hydrolysis

A

Polymers are disassembled to monomers

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8
Q

How polymers break apart?

A

A water molecule is added making the polymer split and having the hydroxyl group attach to one side and the hydrogen to another

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9
Q

What is the hydroxyl group?

A

The attached part to the OH

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10
Q

Carbohydrates

A

Sugars and polymers of sugars

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11
Q

Monosaccharides

A

Simple carbohydrates ; generally have molecular formulas that are some multiple of the unit CH2O

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12
Q

Carbonyl group

A

Attached to CO

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13
Q

2 classifications of sugar

A

Aldose (aldehyde)

Ketose (ketone)

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14
Q

Which sugar is an aldose and which is a ketose?

A

Aldose - Glucose (CO at end of carbon skeleton)

Ketose - Fructose (CO within carbon skeleton)

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15
Q

Hexoses

A

6-carbon skeleton (Glucose, Fructose)

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16
Q

Pentoses

A

5-carbon skeleton (Ribose, Ribulose)

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17
Q

Trioses

A

3-carbon skeleton (Glyceraldehyde, Dihydroxyacetone)

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18
Q

Source of diversity for simple sugars

A

Spatial arrangement of their parts around asymmetric carbons

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19
Q

Disaccharide

A

Two monosaccharides joined by a glycosidic linkage

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20
Q

Glycosidic linkage

A

Covalent bond formed between two monosaccharides by a dehydration reaction

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21
Q

Polysaccharides

A

Macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages

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22
Q

Storage polysaccharide

A

Stored sugars for later use

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23
Q

Starch

A

Plants storage for glucose

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24
Q

Glycogen

A

Polymer of glucose and branched extensively

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25
Q

Cellulose

A

Major component of the tough walls that enclose plant cells

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26
Q

What configuration is starch glucose monomers in?

A

Alpha configuration (helical)

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27
Q

What configuration is cellulose glucose monomers in?

A

Beta configuration (straight)

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28
Q

What do the differing glycosidic linkages do?

A

Gives the molecules distinct shapes

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29
Q

Chitin

A

Carbohydrate used by anthropoids for their exoskeleton

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30
Q

Only class of large molecules that doesn’t contain true polymers and isn’t considered a macromolecule?

A

Lipids

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31
Q

What kind of molecules are lipids?

A

Hydrophobic

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32
Q

What is fat?

A

Large molecules assembled from smaller molecules by dehydration reactions

33
Q

What two kinds of smaller molecules construct fat?

A

Glycerol and fatty acids

34
Q

Glycerol

A

Is an alcohol, each of its three carbons bears a hydroxyl group

35
Q

Fatty acid

A

Long carbon skeleton, usually 16 to 18 carbon atoms in length. One end is carboxyl and rest is part of a hydrocarbon chain

36
Q

Reason why fats are hydrophobic

A

The nonpolar C-H bonds in the hydrocarbon chains

37
Q

What gives the name fatty acids?

A

The carboxyl group

38
Q

What are required to create a fat?

A

Three fatty acids and a glycerol molecule through ester linkage

39
Q

What is ester linkage

A

A bond formed by a dehydration reaction between a carboxyl group and a hydroxyl group

40
Q

What is the fat called with red fatty acids and a glycerol molecule linked?

A

Triacylglycerol

41
Q

Saturated fats

A

Fats that are solid and have no double bonds with carbon atoms in the chain

42
Q

Unsaturated fats

A

A liquid that consists of one or more carbon atoms double bonded in the chain, causing a kink. (Cis)

43
Q

What causes Trans fat?

A

The addition of hydrogen to make the unsaturated fat to a saturated (solidified) form causes it to be both saturated and unsaturated with a Trans double bond

44
Q

How is fat important to humans and not plants?

A

Plants are immobile and use starch as it’s energy storage. Although 1 gram of fat stores twice as much energy as a polysaccharide, plants don’t need it like mobile mammals do such as humans

45
Q

Phospholipid

A

Essential for cells because they are major constituents of cell mem- branes. Two fatty acids attached to glycerol

46
Q

What differences do the head and tails of the phospholipids have?

A

The head is hydrophilic and has an affinity for water while the tails are hydrophobic

47
Q

Difference between hydrophobic and hydrophilic?

A

Hydrophobic - nonpolar

Hydrophilic - polar

48
Q

What is steroids

A

A lipid characterized by a carbon skeleton consisting of four fused rings

49
Q

What is cholesterol?

A

Type of steroid crucial to animals (cell membrane and sex hormones)

50
Q

Importance of proteins

A

Account for more than 50% of the cell’s dry mass

Instrumental in almost everything organisms do

51
Q

Catalysts

A

Chemical agents that selectively speed up chemical reactions without being consumed by the reaction

52
Q

The similarity between all proteins?

A

They all come from the same set of 20 amino acids, linked in unbranched polymers

53
Q

What is a polypeptide?

A

Polymer of amino acids (bond between amino acids is peptide bond)

54
Q

What is a protein?

A

Biologically functional molecule made up of one or more polypeptides, each shaped to a three dimensional figure

55
Q

What is a carboxyl group?

A

CO double bond and also COH bond (C attaching to both)

56
Q

What is an amino acid?

A

Organic molecule with an amino group and a carboxyl group

57
Q

Functions of proteins

A

Enzymatic - acceleration of chemical reactions
Storage - store amino acids
Hormonal - coordination of organisms activities
Motor - movement
Defensive - protection against disease
Transport - transport of substances
Receptor - response of a cell to chemical stimuli
Structural - support

58
Q

How does an amino acid become a polypeptide?

A

An amino acid is a monomer. This monomer connects to another amino acid through a peptide bond. This peptide bond is when the carboxyl group of one amino acid is bonded with the amino group of the acid and undergoing dehydration reaction to become linked, thus creating polypeptides with multiple amino acids

59
Q

Where do the amino acids chain start?

A

Amino group side (N-terminus)

60
Q

What is so important about protein shape?

A

It is important for so many things because it is like a puzzle piece fitting to other cells and parts by having that specific shape. This is all achieved by the specific side chain and number of polypeptides a protein has

61
Q

Four levels of protein structure

A

Primary
Secondary
Tertiary
Quaternary

62
Q

Primary structure

A

Sequence of amino acids

63
Q

Secondary structure

A

Coiled or folded in patterns that contribute to the protein’s overall shape

64
Q

How are secondary structures formed?

A

Through the hydrogen bonds in the polypeptide backbone (not side chain)

65
Q

Alpha helix

A

Delicate coil held together by hydrogen bonding every fourth amino acid

66
Q

Beta pleated sheet

A

Two or more segments of the polypeptide chain lying side by side (called β strands) are connected by hydrogen bonds between parts of the two parallel segments of the polypeptide backbone

67
Q

Tertiary structure

A

Overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids

68
Q

Hydrophobic interaction

A

Amino acids with hydrophobic (nonpolar) side chains usually end up in clusters at the core of the protein, out of contact with water. Thus, a “hydrophobic interaction” is actually caused by the exclusion of nonpolar substances by water molecules. Once nonpolar amino acid side chains are close together, van der Waals interactions help hold them together. Meanwhile, hydrogen bonds between polar side chains and ionic bonds between positively and negatively charged side chains also help stabilize tertiary structure

69
Q

Disulfide bridges

A

Covalent bonds further reinforcing the shape of a protein

70
Q

Quaternary structure

A

Overall protein structure that results from the aggregation of these polypeptide subunits

71
Q

Denaturation

A

Proteins break their shape due to environmental changes around them

72
Q

Chaperonins

A

Protein molecules that assist in the proper folding of other proteins

73
Q

Ways to see shapes of protein

A

X-Ray crystallography
NMR spectroscopy
Bioinformatics

74
Q

Nucleic acids

A

Polymers made of monomers called nucleotides

75
Q

DNA

A

Genetic material that organisms inherit from their parents

76
Q

RNA

A

Interacts with the cell’s protein-synthesizing machinery to direct production of a polypeptide, which
folds into all or part of a protein

77
Q

What composes a nucleotide?

A

Five-carbon sugar (pentose)
Nitrogenous base
One or more phosphate groups

78
Q

Two families of nitrogenous bases

A

Pyrimidine

Purines

79
Q

Pyrimidine?

A

One six-membered ring of carbon and nitrogen atoms

80
Q

Members of pyrimidine

A

cytosine (C)
thymine (T)
uracil (U)

81
Q

Members of purines

A

adenine (A)

guanine (G)

Bio 3A (5 decks)

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