Ch 2, 3, and 4: Molecules and Life Flashcards

1
Q

Digestive system

A

Where food is process in a long canal

Secretion occurs along the way to break down the food

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2
Q

Food

A

Specific types of molecules that can make ATP for us

Carbohydrates + lipids + proteins

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3
Q

Nitrogenous acid

A

Proteins and nucleic acids

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4
Q

Hierarchy of organization

A
Atoms
Macromolecules
Cells
Tissues
Organs
Organ Systems
Organism
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5
Q

Hydrophilic

A

Water soluble molecules

Polar or ionic

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6
Q

Hydrophobic

A

Water insoluble molecules

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7
Q

Amphipathic

A

Molecules that have both hydrophilic and hydrophobic properties

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8
Q

Biological molecules

A
Molecules of life that allow cells to survive
Proteins
Carbohydrates
Nucleic acids
Lipids
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9
Q

What makes up proteins?

A

Amino acids

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10
Q

What makes up carbohydrates?

A

Glucose, fructose, and galactose

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11
Q

What makes up nucleic acids?

A

Nucleotides

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12
Q

What makes up lipids?

A

Fatty acids and glycerols

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13
Q

Roles of macromolecules

A
Energy storage
Structural support
Transport
Protection and defense
Regulation of metabolic activities
Means for movement, growth, and development
Heredity
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14
Q

Proteins

A

Most abundant macromolecule
Vary in function and size
Folding is crucial to the function
Influenced largely by amino acid sequence

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15
Q

Amino acid structure

A
Central carbon that forms 4 bonds
H group
Hydroxyl group
Amino group
R group
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16
Q

Argine

A

Hydrophilic side chain
Positively charged
Can be made from essential amino acids

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17
Q

Histidine

A

Hydrophilic side chain
Positively charged
Essential amino acid

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18
Q

Lysine

A

Hydrophilic side chain
Positively charged
Essential amino acid

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19
Q

Aspartic acid

A

Hydrophilic side chain
Negatively charged
Can be made from essential amino acids

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20
Q

Glutamic acid

A

Hydrophilic side chain
Negatively charged
Can be made from essential amino acids

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21
Q

Serine

A

Hydrophilic side chain

Can be made from essential amino acids

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22
Q

Threonine

A

Hydrophilic side chain

Essential amino acid

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23
Q

Asparagine

A

Hydrophilic side chain

Can be made from essential amino acids

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24
Q

Glutamine

A

Hydrophilic side chain

Can be made from essential amino acids

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25
Tyrosine
Hydrophilic side chain | Can be made from essential amino acids
26
Cysteine
Polar | Can be made from essential amino acids
27
Glycine
R group - H | Can be made from essential amino acids
28
Proline
R group is covalently linked to the amino group | Can be made from essential amino acids
29
Alanine
Hydrophobic side chain | Can be made from essential amino acids
30
Isoleucine
Hydrophobic side chain | Essential amino acid
31
Methionine
Hydrophobic side chain | Essential amino acid
32
Phenylalanine
Hydrophobic side chain | Essential amino acid
33
Tryptophan
Hydrophobic side chain | Essential amino acid
34
Valine
Hydrophobic side chain | Essential amino acid
35
Leucine
Hydrophobic side chain | Essential amino acid
36
Amino acid polymerization
Primary Secondary Tertiary Quaternary
37
Primary structure
Covalent bonds form between amino acids Condensation reaction Sequence of amino acids determines the structure
38
Secondary structure
Carboxyl and amino groups form hydrogen bonds with each other R-group extends outward Protein starts to change shape - alpha helix or beta pleated sheet
39
Tertiary structure
R group interactions Not one specific bond type - depends on the R groups The protein starts to take its shape
40
Quaternary structure
Tertiary proteins interact with each other to form a complex protein Ex. hemoglobin
41
Crucial functions of proteins
Can be chemical facilitators - enzymes | Can be surface membrane substances
42
What ensures that proteins form the right shape?
The cell environment: pH (level of acidity) temperature salt function
43
Denatured protein
A non-functional protein
44
Protein structure...
determines its function
45
Carbohydrates function
Energy storage Structural components Surface receptors - give the cell an identity
46
Types of carbohydrates
Monosaccharides Disaccharides Oligosaccharides Plysaccharides
47
Glycosidic linkage
When an oxygen covalently connects two glucose monomers
48
Glycogen
Stored forms of carbs in out body | Stored in liver or muscles
49
Nucleic acids
Specialized polymers that store and transmit information Two types - DNA and RNA Phosphate group + sugar + base
50
Purines
Double ring structure Adenine Guanine
51
Pyrimidines
Single ring structure Cytosine Thymine Uracil
52
RNA
Smaller than DNA A disposable copy of a particular gene in DNA Single helix Thymine isn't found
53
DNA
``` Encodes hereditary info Transfers info to RNA molecules Double helix Uracil isn't found Hydrogen bonds stabilize the two strands together ```
54
ATP
Energy currency inside the cell | Molecules that possess a high amount of energy in covalent bonds
55
cAMP
A specialized ribonucleotide A chemical messenger Essential for hormone action and the transfer of info by the nervous system
56
Lipids
Not soluble in water
57
Lipid functions
``` Energy storage Cell membranes Capture of light energy Hormones and vitamins Thermal insulation Electrical insulation of nerves ```
58
Triglyceride
Glycerol + 3 fatty acids | Involved in energy storage
59
Ester linkage
Covalent bond between glycerol and a fatty acid
60
Saturated lipid
Lipid that has a full set of hydrogens
61
Unsaturated lipids
Lipids that have at least one double bond | Happens frequently at cold temps