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bio- biochem Flashcards

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0
Q

Proton

A

Positively charged subatomic particle in an atoms nucleus

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1
Q

8 Characteristics of life

A 
Made of cells
Use energy 
Ability to reproduce 
Respond to stimulus 
Maintain homeostasis 
Grow and develop
Have DNA
Change and evolve over time
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2
Q

Neutron

A

Neutral subatomic particle in an atoms nucleus

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3
Q

Electron

A

Negatively charged subatomic particle in electron shells

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4
Q

Covalent bonds

A

When two atoms share their valence electrons and overlap their electron orbitals in order to complete the outermost orbital shell

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5
Q

Valence electrons

A

Electrons in the outer shells that are used to covalently bond

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6
Q

What makes a molecule organic?

A 
The elements in it are covalently bonded 
Usually big
Associated with living systems
ALWAYS contain carbon
SHNOPSi is commonly found in it
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7
Q

SHNOPSi

A 
Sulfur
Hydrogen
Nitrogen 
Oxygen
Phosphorus 
Silicon
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8
Q

Inorganic

A

Carbon dioxide and other molecules without carbon

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9
Q

Carbon

A

Has 6 total electrons (4 valence)
Can form chains or rings (when it bonds)
Versatile

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10
Q

How many elements can carbon potentially covalently bond with?

A

4 because it has 4 electrons in its outermost shell but can hold up to 8 in that shell– can bond with 4 other atoms to get 8
Can form single, double, or triple bonds, or rings

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11
Q

What are Functional groups?

A

Cluster of atoms that determines the chemical reactivity and other characteristics of a molecule

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12
Q

Name the functional groups

A 
Hydrogen
Hydroxyl
Carboxylic acid
Amino
Phosphate
Methyl
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13
Q

Hydrogen group

A

-H
Polar or nonpolar (depending on which atom it is bonded to)
Involved in dehydration and hydrolysis reactions
Found in: almost all organic molecules

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14
Q

Hydroxyl group

A

-O-H
Polar
Involved in dehydration and hydrolysis reactions
Found in: carbs, nucleic acids, alcohols,some acids, steroids

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15
Q

Carboxylic acid group

A 
=O
-C
              -O-H
Acidic
Involved in peptide bonds
Found in: amino acids, fatty acids
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16
Q

Amino group

A

-H
-N
-H
Basic
May bond an additional H+ to become positively charged
Involved in peptide bonds
Found in: amino acids, nucleic acids

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17
Q

Phosphate group

A 
H
   O
-O-P=O
   O
     H
Acidic
Links nucleotides in nucleic acids
Energy-carrier group in ATP
Found in: nucleic acids, phospholipids
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18
Q

Methyl group

A 
H
   -C-H
H
Nonpolar
Tends to make molecules hydrophobic 
Found in: many organic molecules, especially common in lipids
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19
Q

Polar

A

Has opposite poles (ex: water)

Give away- one side has oxygen

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20
Q

Electronegativity

A

Attracts electrons to its outer shell bc its v close to becoming stable (full electron outer shell)
But shares it evenly, doesn’t steal them
Ex: oxygen has 6 valence electrons, only 2 away

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21
Q

Macromolecules

A

Huge molecules made up of smaller molecules
Macro=giant

Formed thru polymerization reactions

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22
Q

Monomers

A

Subunit

Make up polymers

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23
Q

Polymer

A

Multiple (3+) monomers together

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24
Q

Dimer

A

2 monomers

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25
Q

Polymerization reactions

A

Dehydration synthesis and hydrolysis

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26
Q

Dehydration synthesis/ condensation

A

Anabolic reaction
Monomers join together by removing a water molecule (H2O)
Partial negative end attracted to atrial positive end

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27
Q

Hydrolysis

A

Polymers broken down by breaking a water molecule into -H and -H-O and adding it to break the bond between monomers

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28
Q

4 categories of biological molecules

A

Carbohydrates
Lipids
Proteins
Nucleic acids

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29
Q

Carbohydrate composition

A

C, H and O in ratio of 1:2:1

Ex: glucose is C6H12O6

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30
Q

Monosaccharides

A

Simple or single sugars

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31
Q

Disaccharides

A

Two linked monosaccharides

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32
Q

Polysaccharides

A

Long chains of monosaccharides

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33
Q

Isomer

A

Molecules with the same molecular formula but a diff structure

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34
Q

What’s the only group of biomolecules that’s isometric?

A

Carbohydrates

Ex: C6H12O6 = fructose and glucose, but they have diff structures

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35
Q

Structure of monosaccharides

A

Back bone of 3-7 carbon atoms
Many -OH And -H functional groups
Ring shaped

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36
Q

Fate of monosaccharides inside a cell

A

Broken down for energy
OR
linked together by dehydration synthesis

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37
Q

Why are most small carbs water soluble

A

They have polar -OH functional groups

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38
Q

Sucrose (table sugar)=

A

Glucose+fructose

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39
Q

Lactose (milk sugar)=

A

Glucose+galactose

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40
Q

Maltose (malt sugar)=

A

Glucose+ glucose

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41
Q

2 types of polysaccharides

A

Storage polysaccharides

Structural polysaccharides

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42
Q

Starch

A

Storage polysaccharide in plants
Polymer of glucose
Formed in roots and seeds as a form of glucose storage

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43
Q

Glycogen

A

Storage polysaccharide in animals
Polymer of glucose
Found in liver and muscles

44
Q

Cellulose

A

Structural polysaccharide in plants
Polymer of glucose – each alternate glucose is inverted
Found in cell walls of plants and some fungi

45
Q

Why are cell walls indigestible for most animals?

A

Made of cellulose
The orientation of the bonds between glucose in cellulose (one is right side up, next is upside down, …) –inverted pattern

46
Q

Chitin

A

Structural polysaccharide in plants and animals
Polymer of modified glucose units
Found in outer coverings of insects, crabs, and spiders
Found in cell wall of some fungi

47
Q

Lipids

A

Large chains of nonpolar hydrocarbons

Hydrophobic and water insoluble

48
Q

Major 4 functions of lipids

A

Long term energy storage
Waterproofing
Membranes in cells (ex: phospholipids)
Hormones (ex: estrogen and testosterone)

49
Q

Fats and oils - structure

A

3 fatty acid subunits + glycerol join by dehydration synthesis to make a triglyceride

50
Q

Fats and oils-purpose

A

Long term energy storage

51
Q

What stores more energy- lipids or carbs? And why

A

Lipids – more energy rich/ energy condensed than carbs

52
Q

Saturated fats

A

Solid at room temperature
Fit as many hydrogens as possible
Mostly SINGLE bonds
fatty acid tails are straight

53
Q

Problem with Saturated fats

A

Can become a plaque and stop your blood flow

54
Q

Unsaturated fats

A

Liquid at room temperature
Less hydrogen atoms
DOUBLE bonds– makes kinks in the tails

55
Q

Problem with unsaturated fats

A

Unsaturated trans fats have been linked to heart disease

56
Q

Waxes

A

Long hydrocarbon chains
Strongly hydrophobic
Highly saturated

57
Q

Waxes-purpose

A

Form waterproof coatings and build honeycomb structures

58
Q

Examples of where waxes are used

A

Waterproofing:
Leaves and stems of plants
Fur in mammals(especially marine)
Insect exoskeletons

59
Q

Phospholipids

A

Form plasma membranes around all cells

60
Q

Phospholipid structure

A

2 fatty acids + glycerol + short polar functional group

61
Q

What is special about phospholipids (in terms of water solubility)?

A

It has polar heads (functional group) which are hydrophilic

And nonpolar fatty acid tails which are hydrophobic

62
Q

Steroid structure

A

Four carbon rings fused together

63
Q

Steroids examples

A

Cholesterol (found in membranes of animal cells)

Male and female sex hormones

64
Q

Most important biomolecules

A

Proteins

65
Q

Protein function

A 
Structure 
Movement
Defense
Storage 
signaling 
Catalyze reactions (most important)
66
Q

Examples of structural proteins

A

Collagen in skin

Keratin in hair, nails, and horns

67
Q

Examples of movement proteins

A

Actin and myosin in muscles

68
Q

Examples of defense proteins

A

Antibodies in bloodstream

69
Q

Examples of storage proteins

A

Albumin in egg white

70
Q

Example of signaling protein

A

Growth hormone in bloodstream

71
Q

Example of catalyzing proteins

A

Enzymes

72
Q

Protein composition

A

Chains of amino acids joined by dehydration synthesis

73
Q

Amino acid structure

A

R group
Amino group-O-carboxylic acid group
H

74
Q

R Group in amino acids

A

Variable group, differs in every amino acid

Some are hydrophobic some are hydrophilic

75
Q

If the R group is a cysteine..

A

Can form disulfide bridges

76
Q

How are amino acids joined together to create a protein?

A

Dehydration synthesis creates a peptide bond between the carbon (from carboxylic acid group) and the nitrogen (amino group) of adjacent amino acids

O-H from carboxylic acid group and H from amino group are taken out as water

77
Q

Importance of amino acids

A

The sequence, type, position, and number of amino acids determines the proteins structure and function

78
Q

What happens if the positioning of R groups is disrupted?

A

Certain bonds will not be made which will lead to denaturing the protein (loss of function)

79
Q

4 levels of protein structure

A

Primary
Secondary
Tertiary
Quaternary

80
Q

Primary structure

A

Sequence of amino acids linked together in a protein

81
Q

Secondary structure

A

Helices and pleated sheets

82
Q

Tertiary structure

A

Complex folding of the protein chain held together by disulfide bridges, hydrophilic/hydrophobic interactions, and other bonds

83
Q

Quaternary

A

Multiple protein chains are linked together

84
Q

Nucleotides

A

Make up nucleic acids

85
Q

Nucleotide structure

A

Phosphate group-5 carbon sugar-nitrogen containing base

86
Q

Two types of nucleotides

A

Ribonucleotides (A,G, C, U) found in RNA

Deoxyribonucleotides (A,G,C,T) found in DNA

87
Q

Two types of nucleic acid polymers

A

DNA found in chromosomes (carries genetic info needed for protein construction )
RNA (copies of DNA used directly in protein construction)

88
Q

Other nucleotides (diff purposes )

A

Nucleotides as intracellular messengers
…as energy carriers
…as enzyme assistants

89
Q

Nucleotides as intracellular messengers

A

Cyclic nucleotides carry chemical signals between molecules

90
Q

Nucleotides as energy carriers

A

ATP carries energy stored in bonds between phosphate groups

NAD+ and FAD carry electrons

91
Q

Nucleotides as enzyme assistants

A

Coenzymes help enzymes promote and guide chemical reactions

92
Q

Anabolic reactions

A

Building up reaction

Reactant + reactant -> product

93
Q

Catabolic reactions

A

Breaking down reaction

Reactant -> product + product

94
Q

Activation energy

A

The amount of energy needed to start a reaction

95
Q

What happens when chemical bonds form or break?

A

Energy is either released if absorbed

96
Q

Do anabolic reactions absorb or release energy ?

A

Absorbs - needs a constant energy source (endothermic)

Look at graph in ppt

97
Q

Do catabolic reactions absorb or release energy?

A

Release- spontaneous reactions (but will need a spark or something to start it)
Exothermic
Look at graph in ppt

98
Q

Where do we get energy needed for absorbing (anabolic) reactions?

A

Humans- food

Plants- sunlight

99
Q

Catalyst

A

Speeds up rate of chemical reaction

Lowers activation energy

100
Q

Enzymes

A

Proteins that speed up chemical reactions ( by providing a substance for it to occur on)

101
Q

How are enzymes specific?

A

Enzymes and substrates (reactants) are made for each other like lock (enzyme) and key (substrate)

102
Q

How are enzymes named?

A

Named after their function + “ase”

Ex: DNA polymerase

103
Q

Substrate

A

Reactant

What the enzyme will change

104
Q

Active site

A

Place on enzymes where substrates bind

105
Q

Enzyme-substrate complex

A

When enzyme and substrate binds together

106
Q

Denaturing an enzyme

A

Changing and enzymes shape

107
Q 
Anything that influences  a chemical reaction:
pH
Temperature 
Regulatory proteins
Inhibitors
A

What affects enzymes?

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