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

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

Flashcards in Ch 2, 3, and 4: Molecules and Life Deck (61):
1

Digestive system

Where food is process in a long canal
Secretion occurs along the way to break down the food

2

Food

Specific types of molecules that can make ATP for us
Carbohydrates + lipids + proteins

3

Nitrogenous acid

Proteins and nucleic acids

4

Hierarchy of organization

Atoms
Macromolecules
Cells
Tissues
Organs
Organ Systems
Organism

5

Hydrophilic

Water soluble molecules
Polar or ionic

6

Hydrophobic

Water insoluble molecules

7

Amphipathic

Molecules that have both hydrophilic and hydrophobic properties

8

Biological molecules

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

9

What makes up proteins?

Amino acids

10

What makes up carbohydrates?

Glucose, fructose, and galactose

11

What makes up nucleic acids?

Nucleotides

12

What makes up lipids?

Fatty acids and glycerols

13

Roles of macromolecules

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

14

Proteins

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

15

Amino acid structure

Central carbon that forms 4 bonds
H group
Hydroxyl group
Amino group
R group

16

Argine

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

17

Histidine

Hydrophilic side chain
Positively charged
Essential amino acid

18

Lysine

Hydrophilic side chain
Positively charged
Essential amino acid

19

Aspartic acid

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

20

Glutamic acid

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

21

Serine

Hydrophilic side chain
Can be made from essential amino acids

22

Threonine

Hydrophilic side chain
Essential amino acid

23

Asparagine

Hydrophilic side chain
Can be made from essential amino acids

24

Glutamine

Hydrophilic side chain
Can be made from essential amino acids

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