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Biology 100 > Structure and Function of Large Biological Molecules > Flashcards

Structure and Function of Large Biological Molecules Flashcards

1
Q

Macromolecules are…

A

large biological molecules that can generate polymers

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2
Q

A polymer is…

A

longer structure made up of many repeating subunits

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3
Q

A monomer is…

A

a single subunit

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4
Q

Examples of macromolecules are…

A

carbohydrates, proteins, nucleic acids

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5
Q

Lipids are ____ macromolecules but are______

A

not; large biological molecules

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6
Q

The process of building a polymer….

A

dehydration synthesis

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7
Q

The process of breaking down a polymer…

A

hydrolysis

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8
Q

2 monomers is a…

A

dimer

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9
Q

Dehydration reaction is…

A

when monomers bond together through the loss of a water molecules

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10
Q

Dehydration reaction results in a ______ bond + the removal of a ______ and ______

A

covalent; hydroxyl group + H atom;

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11
Q

We use _____ to facilitate this process

A

enzymes

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12
Q

Hydrolysis is…

A

used to generate monomers or smaller components of a polymer

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13
Q

In Dehydration _____ is _____ the cell and in Hydrolysis _____ is ______ the cell

A

water; leaving; water; entering

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14
Q

Carbohydrate are..

A

molecules that contain carbon, hydrogen, and oxygen in a ratio of 1:2:1

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15
Q

The simplest carbohydrate are ….

A

monnosaccharides

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16
Q

Monosaccharides have….

A

molecular formulas that are usually multiples of CH2O

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17
Q

Carbohydrates have an abundance of _______ which make it ideal for _______

A

carbo-hydrogen bonds; energy storage

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18
Q

The carbohydrate sugars can be classified by their _____ group-> _____ and ____

A

carbonyl group; aldoses; ketoss

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19
Q

Most common example of a monosaccharide is …

A

glucose

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20
Q

glucose can exists in a _____ form and a _____ form

A

linear; ring

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21
Q

glucose has a lot of _______ due to ____ bonds

A

energy storage; carbo-hydrogen

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22
Q

What position is the carbonyl group in and what property does it give glucose

A

position- alpha, allows glucose to switch between linear and ring formation

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23
Q

disaccharide

A

2 monosaccharides

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24
Q

oligosccharide

A

more then 3 less then many

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25
Q

The formation of a disaccharide results in the release of _____ and the formation of a _______

A

water; glycosidic linkage

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26
Q

Glycosidic bond

A

covalent bond between two monosccharides

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27
Q

Glycosidic bonds will occur in the presence of an …

A

enzyme

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28
Q

For sucrose + maltose the glycosidic linkage will occur at the _____ group

A

hydroxyl

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29
Q

Example of polysaccharides are …

A

strach, glycogen, cellulose

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30
Q

______ is an example of a polysaccharide that utilizes ____ as its monomeric subunit

A

Starch; glucose

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31
Q

Starch has ____ glycosidic linkage in position ____ and _____

A

alpha; 1-4; 1-6

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32
Q

Starch is used to….

A

store energy in plant

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33
Q

Starch readily reacts with _____ which allows for ______, which causes the release of _____ in a plant

A

water; hydrolysis reactions; energy

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34
Q

Glycogen is used for ________ in ______ cells

A

storage; animal

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35
Q

Glycogen has ….

A

extensive branching

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36
Q

Explain how Glycogen is used in liver cells

A

source of glucose to help maintain blood sugar levels

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37
Q

Explain how Glycogen is used in muscle cells

A

source of fuel to generate ATP; needed by muscles for contraction

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38
Q

Glycogen + Starch can be easily ____ to extract ______

A

hydrolyzed; energy

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39
Q

Cellulose has _____ glycosidic linkages which results in _______, making it more suitable for _______ rather then ______

A

beta; parallel branching; structure; ennergy storage

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40
Q

Cellulose forms _____ which______ to cause____

A

rigid linear rods; aggregate laterally; microfibril

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41
Q

The alpha o beta position of glucose will depend on the

A

position of the hydroxyl group

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42
Q

Whether the hydroxyl group is alpha or beta can effect

A

1) the spacing of the glycosidic linkages

2) The ability for certain enzymes to hyrodolize the glycosidic linkages

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43
Q

Humans cannot digest cellulose because

A

we do not contain the enzymes that can hydrolyze the beta linkages found in glucose

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44
Q

Animals can digest cellulose because

A

have different microbiles that are capable of hydrolyzing the beta linkages

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45
Q

Lipids are ___ macromolecules

A

NOT

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46
Q

Lipids are…

A
  • largely non-polar
  • insoluble in water
  • consist of primarily hydro-carbon regions
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47
Q

Lipids are used for

A

1) energy storage

2) thermal insulation

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48
Q

Examples of Lipids are

A

1) phospholipids
2) chlorofil
3) steroids

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49
Q

The components of fats are

A

1) Glycerol backbone

2) 3 fatty acid tails

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50
Q

The ____ group if the glycerol is attached to the long ____

A

carboxyl; carbon skeleton

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51
Q

The dehydration synthesis of the glycerol + fatty acid tails results in a

A

ester linkage

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52
Q

The fatty acids tails within a fat can differ in

A

1) size

2) double bonds

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53
Q

Fats are for long term storage because of the

A

hydro-carbons

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54
Q

Fats can be stored in ____ cells and serve to ______ the internal oragns

A

adipose; cushion

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55
Q

Saturated fats have the _____ # of possible ____

A

maximum; H bonds

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56
Q

Saturated fats can _____ because….

A

tightly pack; no presence of double bonds

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57
Q

Saturated fats help ______ fats and are ______ at room temp

A

stabilize; solid

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58
Q

Unsaturated fats have ______ which results in

A

one or more double bounds; kink

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59
Q

Most unsaturated fats have a _____ double bond

A

cis

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60
Q

A cis double bond has

A

hydrogens located on the same side of the double bond

61
Q

Characteristics of unsaturated fats

A

1) cant pack together

2) liquid at room temp

62
Q

Trans fats have a _____ double bond

A

trans

63
Q

A trans bond has

A

the hydrogens on opposite sides

64
Q

Trans fats have the same characteristics as

A

Saturated Fats

65
Q

Explain how trans fats can cause diseases in humans

A

because they can pack together we can consume more which creates plaque deposits, making it more difficult for blood to move in the body

66
Q

Phospholipids have a ______ head and ______ tails

A

hydrophilic; hydrophobic

67
Q

For phospholipids the _____ hydroxyl group in _____ will be attached to a ____

A

3rd; glycerol; phosphate group

68
Q

One phospholipid tail is ___ and the ____

A

saturated; unstaurated

69
Q

Phospholipids will form themselves into a

A

bilayer

70
Q

In the bilayer the ____ will face the exterior and the ____ will face the interioor

A

polar heads; non-polar tails

71
Q

Steroids are derived from

A

4-ring hydro-carbon skeletons

72
Q

Steroids will have a …

A

polar Hydroxyl group

73
Q

A common steroid is…

A

Cholesterol

74
Q

Role of enzymes

A

help increase the rate of a chemical reaction

75
Q

Role of Defensive Proteins

A

amplify +. use to fight diseases or protect against disease

76
Q

Role of Storage Proteins

A

resivour for amino acids -> subunits of proteins

77
Q

Role of Transport Proteins

A

transport substances into, out of, or within a cell

78
Q

Role of Hormones

A

mediate a response between an organism and the cells found within there

79
Q

Role of Receptor proteins

A

receive signals from outside cell -> illicit response

80
Q

Role of Motor proteins

A

movement or motility

81
Q

Role of Structural Proteins

A

provide physical support + shape to cell + organelles

82
Q

Amino acid monomers are the

A

building block for proteins

83
Q

Describe the amino acid backbone

A

amino group + carboxyl group attached to a alpha carbon with a H attached

84
Q

in the amino backbone the two functional groups are

A

ionized

85
Q

The properties of an amino acid are determined by the

A

side chain

86
Q

Hydrophobic side chains have

A

hydrocarbon bonds

87
Q

Hydrophobic side chains will _______ in the interior of a protein

A

cluster

88
Q

Proteins apart of the cellular membrane will have a

A

significant amount of hydrophobic amino acid regions

89
Q

Polar side chains will

A

face aqueous solutions to maximize water interactions or with other polar molecules

90
Q

charged amino acids have a _____ at _____ values that are characteristic of a cell

A

charge; ph

91
Q

Polypeptides are ______ and built from

A

unbranched; amino acids

92
Q

The process of connecting amino acids together

A

dehydration synthesis

93
Q

Describe the formation of a polypeptide bond

A

carboxyl group interacts with amino group of incoming acid

94
Q

A polypeptide bond is _____ and _____ from _____ terminus to ______ tterminus

A

covalent; directional; N; C

95
Q

Ways to depict proteins

A

1) Space-filling model
2) Ribbon model
3) Simplified Diagrams
4) Lock +Key Diagrams
5) Wire Frame Model

96
Q

Space-filling model

A

info on atoms in the structure

97
Q

Ribbon model

A

info on polypeptide backbone + folding patterns

98
Q

Simplified Diagrams

A

transparent so allows for shape + backbone to be seen

99
Q

Lock + Key

A

shows binding sites

100
Q

Wire Frame Model

A

shows relationship between antibody protein + flu virus protein

101
Q

The protein primary structure is based on the ________+ determines ______

A

sequence of amino acids; 3-D architecture

102
Q

The protein secondary structure can consist of _____ and ____ which result from ______ that happens between _______ components of the _____

A

coils; folds; H bonds; repeated; polypeptide backbone

103
Q

Folds + coils result from

A

H bonding at repeated constituents in the polypeptide backbone

104
Q

Coils are…

A

alpha helices

105
Q

Folds are

A

beta pleated sheets

106
Q

Form + Function of Coils

A
  • Spiral shape
  • assist in the formation of H bonds between amino groups and carboxyl groups of an adjacent peptide
  • INTRAMOLECULAR BONDING
107
Q

Form + Function of Folds

A
  • run from neighboring segments of polypeptide backbone or polypeptide backbones that have folded upon themselves
  • rigid structure
  • can participate in both INTER + INTRA MOLECUlAR BONDING
108
Q

Fold + Coil formation is dependent on

A

amino acids

109
Q

The protein tertiary structure results from

A

interactions that are seen within the R groups

110
Q

Examples of tertiary structure interactions are …

A

H bonds, ionic bonds, hydrophobic interactions, van der walls, covalent bonds -> disulfide bridges

111
Q

Explain the importance of H bonds in protein tertiary structure

A
  • allow for interactions that were perviously to far apart to interact through polypeptide folding
112
Q

Explain the importance of ionic bonds in protein tertiary structure

A
  • occur with charged side chains
  • repel same charge
  • attract opposite charge
  • if PH IS DISRUPTED = AFFECT IN CHARGE = DISRUPT INTERACTION
113
Q

Explain the importance of Hydrophobic interactions in protein tertiary structure

A
  • lead protein to fold to minimize interaction with hydrophilic environment and maximize interaction with hydrophobic groups
114
Q

Explain the importance of Van der Waals in protein tertiary structure

A
  • perminent dipole leads to hydrogen bonding

- depend on close proximity

115
Q

Explain the importance of disulfide bridges in protein tertiary structure

A
  • contribute to stability of a protein through covalent bonding
  • can be INTER of INTRA
  • Strongest type of bonding
  • Example- insulin
116
Q

The protein quaternary structure is

A

when 2 or more polypeptide chains form one or more macromolecule

117
Q

Do all proteins reach quaternary level ?

A

No

118
Q

Things that determine protein structure

A
  • level of pH
  • salinity
  • temp
119
Q

Denaturation is

A

loss of proteins native structure

- still has the amino acids

120
Q

Explain the structural difference of a protein + its effect on the cells form and function during sickle cell

A
  • change in the 6th amino acid in the primary structure
  • affects beta subunits shape + makes them clump together
  • causes cell to not efficiently transport oxygen
121
Q

X ray crystallography is

A

used to figure out protein structure + where atoms are positioned in respect to the protein

122
Q

Nucelic acids

A

store, transmit, and express genetic information

123
Q

The monomer of nucleic acids are

A

nucleotides

124
Q

The two major types of nucleic acids are

A

DNA + RNA

125
Q

DNA provides ____ that allows for transition between _____ to _____

A

directions; nucleic acid; polypepide

126
Q

DNA -> mRNA process is called

A

Transcription

127
Q

mRNA -> Polypeptide process is called

A

Translation

128
Q

The 3 main components of nucleotides

A

1) Nitrogenous base
2) Pentose (5-carbon sugar)
3) Phosphate group 1 or more

129
Q

The backbone of a nucleotide is the ______ and is linked together by ______

A

sugar-phosphate backbone; phosphor diesther linkages

130
Q

Nucleoside =

A

nitrogenous base + sugar

131
Q

The 2 families of nitrogenous basses are

A

1) Pyrimidines

2) Purines

132
Q

Pyrimidines are + contain

A
  • are a 6 member ring structure

- Cytosine C, Thymine T, and Uracil U ( RNA)

133
Q

Purines are + contain

A
  • 2 fused ring structure - 1 is 6 member other is 5 member

- contains Adenine A, and Guanine G

134
Q

DNA has a _____ at _____ position

A

Hydrogen; 2 prime

135
Q

RNA has a _____ at _____ position

A

hydroxide; 2 prime

136
Q

Nucleic acids result from _____ being linked together through a _______

A

nucleotides; phosphodiester bridge

137
Q

phosphodiester bond is the

A

phosphate group with a 5 prime carbon of one nucleotide that joins 3 prime carbon of the next nucleotide

138
Q

Phosphodiester bonds have intrinsic ______ and go from ____ to ___

A

directionality; 5 prime; 3 prime

139
Q

DNA occurs as a ______ that can _______

A

double strand; interact with each other

140
Q

Complimentary base pairing occurs between

A

nitrogenous bases

141
Q

The complimentary base pairing occurs due to

A

H bonds

142
Q

A goes with

A

T

143
Q

C goes with

A

G

144
Q

A to T will always create

A

2 bonds

145
Q

C to G will always create

A

3 bonds

146
Q

The strands will run

A

anti-parallel

147
Q

RNA exists as a _______ but can form _____

A

single strand; double strand structures

148
Q

In RNA we use ____ instead of ______

A

U; T

149
Q

Transfer RNA strand runs

A

anti-parallel to itself

Biology 100 (5 decks)

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