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Microbiology > Ch. 7: Microbial Biochemistry > Flashcards

Ch. 7: Microbial Biochemistry Flashcards

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Biology 101 flashcards
1
Q

biochemistry

A
  • the discipline that studies the chemistry of life
  • its objective is to explain form & function based on chemical principles
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2
Q

organic chemistry

A

the discipline devoted to the study of carbon-based chemistry, which is the foundation for the study of biomolecules & the discipline of biochemistry

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3
Q

macronutrients

A

most abundant elements in cells
- hydrogen (H), oxygen (O), nitrogen (N), phosphorous (P), sulfur (S)
- CHONPS
- account for 99% weight of cell

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4
Q

the four most abundant elements

A
  • hydrogen
  • carbon
  • oxygen
  • nitrogen
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5
Q

micronutrients

A
  • trace elements
  • required by some cells; essential to many biochemical reactions
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6
Q

examples of trace elements

A
  • sodium (Na)
  • potassium (K)
  • zinc (Zc)
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7
Q

organic molecules

A

typically contain chains of carbon & hydrogen atoms

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8
Q

inorganic compounds

A
  • don’t contain carbon
  • make up 1-1.5% of cell weight
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9
Q

biomolecules

A

part of living matter & contain carbon

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10
Q

carbon skeleton

A

carbon atoms bind together in large #s producing this chain
- can be branched, straight, or ring shaped

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11
Q

isomers

A

molecules w/the same atomic makeup but different structural arrangement of atoms

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12
Q

structural formulas

A

serve as graphic representation of molecular structure, showing how the atom is arranged

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13
Q

structural isomers

A

compounds that have identical molecular formulas but differ in bonding sequence of the atoms

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14
Q

example of structural isomers

A

glucose, galactose, fructose

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15
Q

functional groups

A

groups of atoms w/in molecules that are categorized by their specific chemical composition & chemical reactions they perofmr

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16
Q

symbol R

A

stands for residue or remainder in chemical formula

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17
Q

hydrogen bonds

A

involving a hydrogen atom located between a pair of other atoms having a high affinity for electrons; such a bond is weaker than an ionic bond or covalent bond

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18
Q

hydroxyl functional group

A

-OH

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19
Q

methyl functional group

A

C-CH3

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20
Q

carboxyl functional group

A
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21
Q

Carbonyl

A
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22
Q

amino

A
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23
Q

phosphatw

A
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24
Q

sulfhydryl

A
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25
Q

macromolecules

A

large molecules formed by linking together a great # of identical, or very similar, smaller organic molecules

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26
Q

monomers

A

smaller molecules that act as building blocks

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27
Q

polymers

A

macromolecules that result from linking monomers together

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28
Q

what are the main groups of carbon containing molecules

A
  • proteins
  • carbohydrates
  • lipids
  • nucleic acids
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29
Q

carbohydrates

A

energy storage, receptors, food, structural role in plants, fungal cell walls, exoskeleton of insects

30
Q

lipids

A

energy storage, membrane structure, insulation, hormones, pigments
- composed of hydrogen & carbon

31
Q

nucleic acids

A

storage & transfer of genetic information

32
Q

proteins

A

enzymes, structure, receptors, transport, structural role in cytoskeleton of a cell & extracellular matrix
- when # of amino acids becomes very large or when multiple polypeptides are used as building subunits these result

33
Q

dehydration synthesis

A

monomer molecules bind end to end in process that results in formation of water molecules as byproduct

34
Q

covalent bond

A

a water molecule is removed as 2 monosaccharides are linked

35
Q

monosaccharides

A
  • simple sugars
  • simplest carbohydrate
  • 4 or more are stable in cyclic or ring structure
36
Q

disaccharide

A

2 monosaccharides chemically bonded

37
Q

glycosidic bond

A

name given to covalent bond between 2 monosaccharides

38
Q

polysaccharide (glycans)

A

large polymers composed of hundreds of monosaccharide monomers

39
Q

what are the most important polysaccharides

A

starch, glycogen, cellulose
- cellulose = linear, structural component
- glycogen = branched, energy storage in animals & bacteria
- starch = branched; energy storage in plants

40
Q

peptidoglycan composed of what

A

alternating NAG & NAM units

41
Q

NAG stands for

A

N-acetylglucosamine

42
Q

NAM stands for

A

N-acetylmuramic acid

43
Q

chitin composed of what

A

polymers of NAG

44
Q

fatty acids

A

lipids that contain long-chain hydrocarbons terminated w/carboxylic acid functional group

45
Q

hydrophobic

A

water fearing; water repelling

46
Q

hydrophilic

A

water loving

47
Q

saturated fatty acids

A
  • fatty acids w/ hydrocarbon chains that contain single bonds
  • have greatest # of hydrogen atoms possible & are therefor saturated
  • solid at room temp
  • example: stearic acid
48
Q

unsaturated fatty acids

A
  • fatty acids w/hydrocarbon chains containing at least one double bond
  • liquid at room temp
  • example: oleic acid
49
Q

unsaturated fatty acids

A
  • trfatty acids w/hydrocarbon chains containing at least one double bond
  • liquid at room temp
  • example: oleic acid
50
Q

triglyceride (triacylglycerol)

A

formed when 3 fatty acids are chemically linked to a glycerol molecule
- primary components of adipose & sebum

51
Q

ester linkage (bond)

A

a compound derived from an acid in which at least one acidic hydrogen atom of that acid is replaced by an organyl group.

52
Q

complex lipids

A

contain at least 1 additional component, such as phosphate group (phospholipid) or carbohydrate moiety (glycolipid)

53
Q

phospholipid

A
54
Q

glycolipid

A
55
Q

amphipathic

A

molecule presenting w/a hydrophobic portion & a hydrophilic portion

56
Q

steroids

A

complex ring structures found in cell membranes

57
Q

most common type of steroid

A

cholesterol

58
Q

amino acid

A

organic molecule that has a central carbon atom referred to as a alpha carbon bonded to H atom side chain, -COOH, NH3; 4th group bonded to carbon varies and is called side chain and is represented by R

59
Q

oligopeptide

A

formed by joining up to approx. 20 amino acids

60
Q

polypeptide

A

formed from up to 50 amino acids

61
Q

4 levels of protein structure

A
  • primary
  • secondary
  • tertiary
  • quaternary
62
Q

primary protein structure

A

simply the sequence of amino acids that make up the polypeptide chain

63
Q

secondary protein structure

A
  • long chains where hydrogen bonding may occur between amino & carbonyl groups w/in peptide backbone
  • results in localized folding of polypeptide chain into helices and sheets
64
Q

tertiary

A

large scale 3D shape of a single polypeptide chain
- these interactions can result in this: disulfide bridges, hydrogen bonds, ionic bonds, hydrophobic reactions

65
Q

disulfide bridges

A

bond between SH functional groups

66
Q

quaternary structure

A

interactions that hold together protein subunits

67
Q

native structure

A

folded proteins that are fully functional in their normal biological role

68
Q

denature

A

when proteins lose 3D shape & are longer functioning

69
Q

conjugated proteins

A

have a nonprotein portion

70
Q

glycoprotein

A

carbohydrate w/protein

71
Q

lipoprotein

A

carbohydrate w/lipid

Microbiology (30 decks)

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