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Dat Bootcamp > Bio1 Molecules/ Fundamentals > Flashcards

Bio1 Molecules/ Fundamentals Flashcards

1
Q

Any substance that takes up space and has mass

A

Matter

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2
Q

What matter is composed of?

A

Elements

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3
Q

Substance that has specific chemical/physical properties

A

Element

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4
Q

Smallest unit of matter/retains all chemical properties of element

A

Atom

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5
Q

Combining 2 or more atoms creates a

A

Molecule

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6
Q

Atoms carbon tends to bond with in an organic molecule

A

Hydrogen,oxygen,nitrogen

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7
Q

Molecules that contain more than one element

A

Compounds

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8
Q

Strong attractive forces that hold atoms WITHIN a molecule

A

Intramolecular forces

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9
Q

Force that exists BETWEEN molecules

A

Intermolecular forces

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10
Q

Is intra or intermolecular forces stronger?

A

Intramolecular forces are stronger

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11
Q

Type of force that determines physical properties

A

Intermolecular forces

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12
Q

Molecules that have potential of bonding to other identical molecules through chemical reactions

A

Monomers

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13
Q

The process which polymers are formed by monomers bonding is called

A

Polymerization

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14
Q

3 varieties of carbohydrates

A

Monosaccharides,disaccharides,polysaccharides

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15
Q

Monosaccharides have a ratio of precisely

A

1 carbon per water molecule

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16
Q

Monosaccharide empirical formula

A

(CH2O)n

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17
Q

5 carbon monosaccharides

A

Pentodes

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18
Q

6 carbon monosaccharides

A

Hexoses

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19
Q

Sugar molecule is ALPHA if hydroxyl Group on first carbon

A

Points down

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20
Q

Sugar molecule is BETA if hydroxyl group on first carbon

A

Points up

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21
Q

An example of pentose (5carbon sugar)

A

Ribose

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22
Q

____ and _____ are examples of hexoses (6carbon sugars)

A

Glucose , Fructose

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23
Q

Glucose and fructose are

A

Isomers

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24
Q

Type of carbohydrate that forms when 2 monosaccharides bond

A

Disaccharide

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25
Q

Monosaccharides monomers bond via which reaction

A

Dehydration/condensation reactions

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26
Q

Functional group and atom that combine in dehydration/condensation reaction

A

Hydroxyl (OH) and Hydrogen

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27
Q

Type of bond in dehydration/condensation reaction

A

Covalent

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28
Q

What is released in a dehydration/condensation reaction?

A

H2O

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29
Q

Opposite of dehydration/condensation reaction

A

Hydrolysis; adds H2O to covalent bond splits monomers apart

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30
Q

Bond that forms when carbohydrate attaches to another molecule

A

Glycosidic

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31
Q

Carbohydrates linked to lipids are called

A

Glycolipids

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32
Q

Carbohydrates linked to proteins

A

Glycoproteins

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33
Q

1glucose + 1 fructose =

A

Sucrose

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34
Q

1 galactose + 1 glucose=

A

Lactose

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35
Q

1 glucose + 1 glucose=

A

Maltose

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36
Q

Polysaccharides are long polymers of

A

Monosaccharides

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37
Q

2 polysaccharide purposes

A

Storage, structure

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38
Q

Crucial storage polysaccharide in plants

A

Starch

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39
Q

Starch contains many glucose monomers in____ and ____ forms

A

Linear, branched

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40
Q

Linear plant starch

A

Amylose

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41
Q

Type of glycosidic bonds in amylose

A

Alpha-1,4- glycosidic bonds

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42
Q

Branched form of plant starch

A

Amylopectin

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43
Q

Type of bonds in amylopectin

A
  • Alpha1,4 glycosidic (linear)

- Alpha1,6 glycosidic (branched)

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44
Q

Storage polysaccharide found in humans

A

Glycogen

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45
Q

Glycogen contains many

A

Glucose monomers

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46
Q

Which is more branched amylopectin or glycogen?

A

Glycogen more branched

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47
Q

Types of bonds glycogen

A
  • alpha 1,4 glycosidic

- MANY alpha 1,6 glycosidic

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48
Q

Glycogen primarily stored in what type of human cells?

A

Liver cells(mostly) ; also muscle cells

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49
Q

Name 2 alpha glucose polysaccharides

A

Starch(amylose or amylopectin) and glycogen

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50
Q

Structural polysaccharide found in plant cell walls, wood and paper

A

Cellulose

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51
Q

Cellulose is a ___

A

Glucose polymer

52
Q

Type of bonds in cellulose

A

Beta 1,4 glycosidic bonds

53
Q

What beta 1,4 glycosidic bonds in cellulose do?

A

Allow cellulose to form linear strands that pack together parallel

54
Q

Intermolecular force that holds adjacent cellulose strands together in parallel

A

Hydrogen bonds

55
Q

Due to its structure cellulose has

A

High rigidity

56
Q

Can humans digest cellulose?

A

No; it passes through digestive tract as fiber

57
Q

Chitin is a __

A

Structural polysaccharide

58
Q

Chitin is found in ____ and ____

A

Fungi cell walls, insect exoskeleton

59
Q

Chitin is a structural polysaccharide of ____

A

N-acetylglucosamine monomers

60
Q

Types of bonds in chitin

A

Beta 1,4 glycosidic bonds

61
Q

Two beta glucose polysaccharides

A

Chitin and cellulose

62
Q

Proteins contain polymers called

A

Polypeptides

63
Q

Polypeptides contain monomeric subunits called

A

Amino acids

64
Q

4 things central carbon in amino acid bonded to

A
  • amino group(NH2)
  • Hydrogen atom
  • carboxyl group(COOH)
  • R group
65
Q

Total number of amino acids

A

20

66
Q

Amino acids are linked via covalent bond called

A

Peptide bond

67
Q

Amino acids form peptide bonds via

A

Dehydration/condensation reactions

68
Q

Reactions that separate amino acids of polypeptide

A

Hydrolysis

69
Q

Enzyme that catalyzes peptide bond formation

A

Peptidyl transferase

70
Q

Peptidyl transferases are ___

A

Aminoacyl transferases

71
Q

Polypeptides have a ___ terminus and a ____ terminus

A

Amino(N-) ; carboxyl(C-)

72
Q

Primary structure of a protein

A

It’s amino acid sequence

73
Q

All proteins have

A

Primary structure

74
Q

Secondary structure of protein

A

Folds due to intermolecular forces between atoms of polypeptide backbone

75
Q

All the amino acid structural features EXCLUDING R group

A

Polypeptide backbone

76
Q

Secondary structure does not include

A

Interactions between R group atoms

77
Q

Which level protein structure includes alpha helices and beta pleated sheets?

A

Secondary

78
Q

Most common intermolecular force for secondary structure? And where do they occur?

A

Hydrogen bonding; occurs between carboxyl(COOH)and amino groups(NH2

79
Q

The common interactions between R groups in tertiary structure

A
  • Ionic bonding
  • Hydrogen bonding
  • Dipole-dipole interactions
  • Van see Waal( London dispersion forces)
  • Hydrophobic interactions
  • Disulfide bonding
80
Q

Tertiary structures usually involve

A

Non-covalent interactions

81
Q

Bond in tertiary structures that involve covalent interactions

A

Disulfide bond

82
Q

Which amino acids allow disulfide bond formation?

A

Cysteine

83
Q

Structure that refers to large proteins that have multiple subunits(multiple polypeptide chains)

A

Quaternary

84
Q

Multiple polypeptide chains in a quaternary structure, entire structure is

A

Protein

85
Q

Causes proteins to lose secondary,tertiary,quaternary structures

A

Protein denaturation

86
Q

Denatured proteins retain

A

Primary structure

87
Q

Loss of shape leads to

A

Loss of protein function

88
Q

Causes of protein denaturation

A
  • excess temp
  • chemicals
  • pH changes
  • Radiation
89
Q

3 structural classifications of proteins

A
  • fibrous
  • globular
  • intermediate
90
Q

Intermediate and globular structural proteins are

A

Soluble

91
Q

Fibrous structural proteins are

A

Insoluble

92
Q

Protein that forms structural component of cells

A

Fibrous structural protein

93
Q

Example of fibrous protein

A

Collagen

94
Q

Proteins that are folded tightly and perform many functions

A

Globular

95
Q

Example of globular structural protein

A

Albumin

96
Q

Fiber shaped proteins that perform many functions

A

Intermediate

97
Q

Example of intermediate structural protein

A

Fibrinogen

98
Q

The 2 compositional protein classifications are

A

Simple, conjugated

99
Q

Simple protein compositions contain only

A

Amino acids(ex: albumin)

100
Q

Conjugated protein compositions contain

A

Amino acids+ non protein components

101
Q

Examples of conjugated proteins

A

Glycoproteins (mucin)
Metalloproteins(hemoglobin)
Lipoproteins(LDL/HDL)

102
Q

Molecules that increase reaction rates

A

Catalyst

103
Q

What part of reaction do catalysts not affect?

A

Spontaneity

104
Q

Catalysts are not

A

Used up in reaction; they manipulate meaning reaction does not change them

105
Q

Catalysts lower this to speed up reaction

A

Activation energy/transition state energy

106
Q

Catalysts cannot change

A

Energy absorbing(endothermic) reactions to ——-> energy releasing(exothermic) reactions and vice versa

107
Q

Catalysts do not affect energy of

A

Reactants or products

108
Q

Biological, globular protein catalysts are

A

Enzymes

109
Q

Substrates bind to enzymes at the

A

Active site

110
Q

Active sites have unique properties and

A

Substrate specificity

111
Q

Measures how efficient enzyme is converting substrate to product

A

Scecificity constant

112
Q

Enzymes bind at active site via

A

Induced fit model

113
Q

Example of RNA enzyme

A

Ribozyme

114
Q

Non protein molecules that assist enzymes

A

Cofactors

115
Q

Cofactors usually help enzymes by donating/accepting a component such as

A

Electrons

116
Q

Organic cofactors (ex vitamins)

A

Coenzymes

117
Q

Inorganic cofactors are

A

Metal ions ( iron, magnesium)

118
Q

Enzymes that are bound to their cofactor

A

Holoenzymes

119
Q

Enzymes not bound to cofactor

A

Apoenzyme

120
Q

Cofactors that tightly/covalently bind to their enzyme in holoenzyne

A

Prosthetic groups

121
Q

Proteins have highest enzymatic activity when ____ and____ are in optimal ranges

A

pH and temp

122
Q

Enzyme regulation where inhibitors compete with substrate for active sites

A

Competitive inhibition

123
Q

Can outcompete competitive inhibitor by

A

Adding more substrate

124
Q

What is enzyme saturation

A

When all the active sites are occupied

125
Q

Inhibitor binds to allosteric site of enzyme

A

Non competitive inhibition

126
Q

Different location then active site of enzyme catalysis

A

Allosteric site

127
Q

Non competitive inhibitor binds to allosteric site modifies the

A

Active Site ;so substrate has reduced/inability to bind

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