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

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
Q

Tyrosine

A

Hydrophilic side chain

Can be made from essential amino acids

26
Q

Cysteine

A

Polar

Can be made from essential amino acids

27
Q

Glycine

A

R group - H

Can be made from essential amino acids

28
Q

Proline

A

R group is covalently linked to the amino group

Can be made from essential amino acids

29
Q

Alanine

A

Hydrophobic side chain

Can be made from essential amino acids

30
Q

Isoleucine

A

Hydrophobic side chain

Essential amino acid

31
Q

Methionine

A

Hydrophobic side chain

Essential amino acid

32
Q

Phenylalanine

A

Hydrophobic side chain

Essential amino acid

33
Q

Tryptophan

A

Hydrophobic side chain

Essential amino acid

34
Q

Valine

A

Hydrophobic side chain

Essential amino acid

35
Q

Leucine

A

Hydrophobic side chain

Essential amino acid

36
Q

Amino acid polymerization

A

Primary
Secondary
Tertiary
Quaternary

37
Q

Primary structure

A

Covalent bonds form between amino acids
Condensation reaction
Sequence of amino acids determines the structure

38
Q

Secondary structure

A

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
Q

Tertiary structure

A

R group interactions
Not one specific bond type - depends on the R groups
The protein starts to take its shape

40
Q

Quaternary structure

A

Tertiary proteins interact with each other to form a complex protein
Ex. hemoglobin

41
Q

Crucial functions of proteins

A

Can be chemical facilitators - enzymes

Can be surface membrane substances

42
Q

What ensures that proteins form the right shape?

A

The cell environment:
pH (level of acidity)
temperature
salt function

43
Q

Denatured protein

A

A non-functional protein

44
Q

Protein structure…

A

determines its function

45
Q

Carbohydrates function

A

Energy storage
Structural components
Surface receptors - give the cell an identity

46
Q

Types of carbohydrates

A

Monosaccharides
Disaccharides
Oligosaccharides
Plysaccharides

47
Q

Glycosidic linkage

A

When an oxygen covalently connects two glucose monomers

48
Q

Glycogen

A

Stored forms of carbs in out body

Stored in liver or muscles

49
Q

Nucleic acids

A

Specialized polymers that store and transmit information
Two types - DNA and RNA
Phosphate group + sugar + base

50
Q

Purines

A

Double ring structure
Adenine
Guanine

51
Q

Pyrimidines

A

Single ring structure
Cytosine
Thymine
Uracil

52
Q

RNA

A

Smaller than DNA
A disposable copy of a particular gene in DNA
Single helix
Thymine isn’t found

53
Q

DNA

A 
Encodes hereditary info 
Transfers info to RNA molecules
Double helix
Uracil isn't found
Hydrogen bonds stabilize the two strands together
54
Q

ATP

A

Energy currency inside the cell

Molecules that possess a high amount of energy in covalent bonds

55
Q

cAMP

A

A specialized ribonucleotide
A chemical messenger
Essential for hormone action and the transfer of info by the nervous system

56
Q

Lipids

A

Not soluble in water

57
Q

Lipid functions

A 
Energy storage
Cell membranes
Capture of light energy
Hormones and vitamins
Thermal insulation
Electrical insulation of nerves
58
Q

Triglyceride

A

Glycerol + 3 fatty acids

Involved in energy storage

59
Q

Ester linkage

A

Covalent bond between glycerol and a fatty acid

60
Q

Saturated lipid

A

Lipid that has a full set of hydrogens

61
Q

Unsaturated lipids

A

Lipids that have at least one double bond

Happens frequently at cold temps

LS 2 (14 decks)

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