Microbiology: Exam 1 review Flashcards


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created 11 years ago by nbogdanoff
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Microbiology
Chapters 1-5
updated 11 years ago by nbogdanoff
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microbiology, science, life sciences, biology
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1

Staphylo

Clustered

2

Cocci

Spherical

3

Aureus

Gold

4

Entero

GI tract

5

Coli

Colon

6

Bacteria

  • Unicellular
  • Prokaryotes
  • No nucleus
  • Peptidoglycan cell wall ( carb+protein)
  • Binary Vision (divid into two)
  • Energy= Organic compounds or photosynthesis

7

Viruses

  • Acellular
  • Core= DNA or RNA, surrounded by protein coat, may have enclosed lipid envelope
  • Only replicated in living host cells

8

Types of Archaea

  • Acidophiles - Acid loving
  • Halophiles - Salt loving
  • Thermophiles - Heat loving
  • Alkaliphiles - Alkali loving
  • Methanogens - Methan loving

9

What is normal microbiota and their function?

  • Microbes normally present on human body
  • Prevent growth of pathogens
  • Produce growth factors ( vitamin k & folic acid)

10

Resistance factors of normal microbiota

Skin, Stomach acid, and antimicrobial chemicals

11

What is an emerging infectious disease (EID), what is an example.

Increasing incidences of a new disease that may have evolved or spread to a new location, Ebola.

12

Three types of bonds

  • Ionic -Middle
  • Covalent -Strongest
  • Hydrogen - Weakest

13

Ionic bond

Attraction between ions of opposite charge. One atom loses electrons and another gains an electron.

14

Covalent bond

Two atoms share one or more pairs of electrons

15

Hydrogen Bond

  • Atom that is covalently bonded to an O or N is attracted to another N or O atom in another molecule.
  • Electromagnetic attraction between polar molecules

16

Types of chemical reactions

  • Synthesis
  • Decomposition
  • Exchange
  • Reversible

17

Synthesis Reaction

Atoms, ions, or molecules combine and form a new larger molecule

18

Glucose + Fructose = Sucrose

Synthesis Reaction

19

Decomposition Reaction

Molecules split into caller molecules, ions, or atoms

20

Sucrose = Glucose + Fructose

Decomposition Reaction

21

NaOH + HCI -----> NaCI = H2O

Exchange Reaction

22

Exchange Reaction

Part synthesis and part decomposition

23

Reversible Reaction

Can go either direction

24

A + B ______ AB

Reversible Reaction

25

Acids

Substances that dissociate into one of more H+

26

HCI ---> H+ + CI-

Acid

27

Bases

Substance that dissociate into one or more OH-

28

NaOH ----> Na++ OH-

Base

29

What is pH

Amount of H+ in a solution

30

pH increased H+

Increased acidity

31

pH increased OH-

Increased alkalinity

32

Optimum pH

7

33

4 organic molecules

  • Carbs
  • Lipids
  • Proteins
  • Nucleic Acids

34

Carbs

  • Cell structure and energy source
  • (CH2O)n
  • Monosaccharides, Disaccharides, Polysaccharides

35

Monosaccarides

Simple sugars with 3 to 7 carbon atoms, glucose, fructose

36

Disaccharides

Formed when 2 monosaccarides are joined in dehydration synthesis

37

Polysaccharides

Tens or hundreds pf monosaccharides joined through dehydration synthesis

38

Lipids

  • Store energy & primary components of cell membranes
  • C,H, and O
  • Fats, oils, waxes, phospholipids, steroids
  • Non polar , insoluble in water

39

Saturated fat

  • Saturated with the max amount of hydrogens.
  • Hydrocarbon are straight and can pack close together = solid at room temp
  • Cannot have anymore Hydrogens

40

Unsaturated fat

  • Double bonds reduce the # of hydrogens
  • Cant pack close together = liquid at room temp
  • Small number of Hydrogens

41

Proteins

  • Cell structure and function
  • Enzymes- speed up chem reactions
  • Trans. Protein- Move chem across membrane
  • Flagella- made of protein
  • some bacteria toxins are protein

42

Amino Acids

building blocks of proteins

43

Peptide Bonds

  • Bond between amino acids
  • Every peptide bond between 2 amino acids, one water molecule is released
  • Formed by hydration synthesis

44

4 levels of protein structure

  • Primary
  • Secondary
  • Tertiary
  • Quaternary

45

Primary Structure

Polypeptide strand (amino acid sequence)

Unique sequence which amino acids are linked together to form a peptide chain

Genetically determined

46

Secondary Structure

Helix and pleated sheet (with 3 polypeptide strands)

Depends on amino acid sequence

Localized, repetitious, twisting or folding of the peptide chain.

Shape results from hydrogen bonds joining the atoms of peptide bonds at diffrent locations along polypeptide chain

47

Tertiary Structure

When helix folds irregularly, forming disulfide bridges, hydrogens bonds, and ionic bonds between amino acids in the chain.

Determines what protein looks like

48

Conjugated Proteins

  • Glycoproteins
  • Lipoproteins

49

Glycoproteins

contain oligosaccharides covalently attached to proteins

50

Lipoproteins

Contain both proteins and lipids, bound to the proteins, which allow fats to move through the water

51

Prokaryote

  • One circular chromosome, not a membrane
  • Bacteria: peptidoglycan cell walls
  • Archaea: Pseudomurein cell walls

52

Eukaryote

  • Paired chromosome, in nuclear membrane
  • Polysaccharide cell wakks

53

Prokaryotic cell shapes

  • Coccus- Sherical
  • Bacillus- rod shaped
  • Spiral
    • Spirillum
    • Vibrio
    • Spirochete

54

Prokaryotic Arrangements

  • Pairs
  • Clusters
  • Chains
  • Terads
  • Sarcinae

55

Pairs

Diplococci and Diplobacilli

56

Clusters

Staphylococci

57

Chains

Streptococci and Streptobacilli

58

Tetrads

Divide in two planes

59

Sarcinae

divide in four planes

60

Gram Positive

  • Stack of peptidoglycan
  • One membrane
  • Stains purple

61

Gram Negative

  • Single layer
  • Seconds membrane
  • Periplasmic space

62

Simple Diffusion

Movement from high to low concentration

63

Facilitated Diffusion

Movement from hight to low concentration, but involves a transporter protein

64

Facilitated Diffusion: Non- Specific

Any molecule can move thought transporter protein

65

Facilitated Diffusion: Specific

Only certain molecules can move through transporter protein

66

Active Transport

Movement against concentration gradient, allows bacteria to accumulate high concentrations , needs ATP

67

Osmosis

Movement of water across a selectively permeable membrane, allows free movement

68

Isotonic

Equal on both sides, allows free movement

69

Hypotonic

Solution lower that osmotic pressure, less salute & more water

70

Hypertonic

Higher concentration of salutes inside the cell, water flows out to maintain balance.

71

Metabolism

Sum of chemical reactions in an organism

72

Catabolism

Provides energy and building blocks fro anabolism

73

Anabolism

Uses energy and building blocks to build large molecules

74

Enzymes

Facilitate and catalyze proteins

Some are highly specific based on conformation (prime,sec,&tertiary)

They are reusable

75

Apoenzyme

An enzyme without its cofactor, inactive

76

Holoenzyme

Apoenzyme plus cofactor, active

77

Factors that influence enzyme

  • Temperature- best at 37 C
  • pH- Optimum 7.2-7.4
  • Substrate concentration- W/ increase the rate of increasing active site till all enzymes are at maximum
  • Inhibitors - Feedback inhibition binds to molecule decreases its activity

78

Oxidation and reduction reactions

Both are used in catabolism to extract energy and store it in ATP

79

Oxidation

Removal of electrons produces energy

80

Reduction

Gain of electrons

81

Difference between resperation and fermentation

Respiration uses all 3 steps and fermentation only uses glycolysis

82

Three parts of respiration

Glycolysis, Krebs Cycle, and Electron transport chain

83

Phototrophs

Use light as primary energy source

84

Chemotrophs

Use energy from chemicals (oxidation reduction)

85

Autotrophs

use carbon dioxide as carbon source

86

Heterotrophs

Use organic carbon source