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cell bio Flashcards

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1
Q

what is cell biology

A

the study of cells at microscopic and molecular levels

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2
Q

describe phospholipid structure

A
  • hydrophilic heads (love water, interact with water)
  • hydrophobic tails (hate water, do not interact with water)
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3
Q

molecules that speed up a chemical reaction without changing

A

catalysts

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4
Q

what are the two types of prokaryotes

A

bacteria (eubacteria) and archaea (archaebacteria)

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5
Q

what element are biomolecules centred around

A

carbon

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6
Q

______ are not present in plant cells

A

cholesterol, type of lipid steroid

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7
Q

what are the two organelles that plants have that animals lack

A

chloroplasts and vacuoles

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8
Q

name the organelle:
contents of the whole cell that are within the plasma membrane but outside the nucleus

A

cytoplasm

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9
Q

portion of cytoplasm that is outside membrane enclosed organelles

A

cytosol

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10
Q

generation of ATP happens where

A

mitochondra/chloroplasts

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11
Q

most membrane protein and soluble organelle protein synthesis happens where

A

endoplasmic reticulum ER

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12
Q

sorting of proteins and lipids from ER happens where

A

Golgi apparatus

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13
Q

which organelle contains genome, DNA and RNA synthesis

A

nucleus

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14
Q

what organelle move most material between organelles and up-taken extracellular molecules

A

endosomes

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15
Q

organelle that degrades unneeded intracellular organelles and extracellular molecules that get brought into the cell

A

lysosomes

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16
Q

aggregate of molecules based on weak, multivalent interactions between scaffolds and client molecules which keep them in the area, lack surrounding membranes

A

biomolecular condensates

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17
Q

transport of proteins from one compartment to another by membrane-bound intermediates (vesicles)

A

vesicular transport

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18
Q

a membrane enclosed dynamic cellular organelle that is involved in the selective transport of proteins/material to other compartments

A

vesicle

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19
Q

process of a protein moving across a membrane

A

protein translocation

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20
Q

dense core of enzymes involved in many processes and also the site of synthesis and destruction of hydrogen peroxide

A

peroxisomes

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21
Q

where do peroxisome proteins come from

A
  • peroxisomal membrane proteins come from the ER with peroxisome precursors
  • proteins from cytosol
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22
Q

in the mitochondria there are how many membranes and how many aqueous spaces?

A

2 membranes: outer member and inner membrane

2 aqueous spaces: matrix and intermembrane space

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23
Q

where are proteins that are made in the ER translated?

A

on ribosomes attached to rough ER

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24
Q

where are proteins that are made in the cytosol translated

A

on free ribosomes in cytosol

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25
Q

what happens in the smooth ER

A
  1. synthesis of steroid hormones
  2. storage of calcium ions
  3. detoxification of alcohol and liver cells (barbiturates)
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26
Q

Term for the portion of each amino acid that gives the amino acid its unique properties

A

side chain

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27
Q

protein folding is mediated by what kind of interactions

A

non-covalent (ionic, van der waals, etc)

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28
Q

when folding of protein begins right away what is it called

A

co-translational

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29
Q

what helps proteins fold into shape

A

chaperons

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30
Q

what are the two folding patterns of secondary protein structure

A
  1. alpha helix
  2. beta pleated sheets
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31
Q

two alpha helices wrap around each other, made by interacting hydrophobic regions on proteins

A

coiled-coil

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32
Q

in beta pleated sheets where do the arrows point to start and end

A

start: N
end: C

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33
Q

protein secondary structure is characterized by what bond

A

H bonds

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34
Q

what are the two types of tertiary structured proteins

A

FG: fibrous and globular proteins

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35
Q

what tertiary protein is usually structural materials outside of cells ex. Keratin, collagen

A

fibrous proteins

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36
Q

what kind of protein is a prion protein

A

a plasma membrane protein

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37
Q

normal prions are folded with what

A

alpha helices

38
Q

prion disease leads to neuronal death which does what to the brain?

A

makes the brain spongey which is fatal!

39
Q

group of proteins that share origin (related function or similar sequence/structure)

A

Protein families

40
Q

what must fit precisely into a binding site of a protein

A

a ligand

41
Q

positive regulation of an allosteric enzyme by

A

an activator molecule

42
Q

end product of metabolic pathway inhibits earlier enzymes that help make it.

A

feedback inhibition

43
Q

enzymes that adds the phosphate

A

kinase

44
Q

enzymes that removes the phosphate

A

phosphatase

45
Q

reactions that occur in response to stimulus

A

signalling cascades

46
Q

addition of methyl group, typically represses gene expression

A

methylation

47
Q

addition of acetyl group, typically enhances gene expression

A

acetylation

48
Q

small molecule bound to enzyme and participates in catalysis reaction

A

coenzyme

49
Q

oxygen carrying protein that requires iron atom to function

A

heme

50
Q

bind multiple proteins to improve the probability of their interaction and confine proteins to certain regions/compartments of the cell

A

scaffolds

51
Q

separation of cell components by size and density mediated by high speed centrifugation.

A

cell fractionation

52
Q

donor and acceptor fluorescent molecules allow us to visualise protein interactions

A

FRET

53
Q

allows us to study protein movement

A

FRAP

54
Q

forces that are several times that of gravity are applied on solutions to increase the rate and which different components settle in the tube based on size.

A

centrifugation

55
Q

chromatography where separation is based on size

A

gel filtration chromatography

56
Q

chromatography where separation is based on charge

A

ion exchange chromatography

57
Q

chromatography where separation is based on ability to bind a protein

A

affinity chromatography

58
Q

addition of sugars (carbohydrates) onto proteins

A

glycosylation

59
Q

Two types of proteins are involved in targeting vesicles to specific compartments

A

Rab and SNAREs proteins

60
Q

on which terminal of ER proteins is the retrieval signal located

A

C terminal

61
Q

process by which the contents of secretory vesicles are released into the extracellular environment

A

exocytosis

62
Q

eukaryotic cells that lack surrounding membranes but concentrate biomolecules proteins and nucleic acids

A

biomolecular condensates

63
Q

random movement of particles

A

brownian motion

64
Q

cells harness what for movement?

A

brownian motion (random movement of particles)

65
Q

archaea is structurally similar to __________but genome is closer to ___________

A

bactera, eukaryotes

66
Q

what do eukaryotes have but prokaryotes dont

A

organelles and nucleus

67
Q

eukaryotes consist of what four groups of organisms

A

animals, plants, fungi and protists

68
Q

combination of 2 cells living in symbiotic relationship - one cells lives inside the other

A

endosymbiont theory

69
Q

simplified controlled environment

A

culture

70
Q

homogenous cells that have undergone modifications to grow continuously in culture, once placed in culture, these cells keep growing and replicating

A

cell line

71
Q

culture obtained directly from the organism

A

primary culture

72
Q

extent to which the detail of a specimen is retained in the image

  • dependent on the wavelength of light
A

resolution

73
Q

produces higher resolution images by excluding out of focus light

A

confocal microscopy

74
Q

can produce higher resolution images by overcoming diffraction limit

A

superresolution microscopy

75
Q

a protein that exhibits green fluorescence when exposed to light

A

green fluorescent protein (GFP)

76
Q

uses electrons as a light source, the image is formed when electrons pass through a specimen

A

electron microscopy

76
Q

best used for viewing detailed structures within cells and tissues, specimens are stained with heavy metal solutions

A

TEM

77
Q

best used for viewing extensions or processes that cells use to interact with the environment, specimens are dried, coated with C and metals and shot at with electrons

A

SEM

78
Q

particular atom grouping that behave as a unit

A

functional groups

79
Q

what reaction forms polymers by joining monomers

A

condensation, water is removed

80
Q

what reaction breaks down polymers into monomers

A

hydrolysis, water is added

81
Q

use an energetically favourable reaction to drive an energetically unfavourable reaction

A

reaction coupling

82
Q

what type of bonds link fatty acids to glycerol

A

ester bonds

83
Q

what are monosaccharides linked by

A

COC linkages

84
Q

energy stored in easy to convert form

A

carrier molecules

85
Q

an electrophoresis method that allows protein separation by mass.

A

SDS PAGE

86
Q

enzymes that add sugars onto proteins are called

A

glycotransferases

87
Q

addition of sugars (carbohydrates) onto proteins

A

glycosylation

88
Q

glycosylated proteins/ sugary proteins are called what

A

glycoproteins

89
Q

helps relieve the stress on the ER causes by defective proteins

A

UPR. unfolded protein response

90
Q

an example of an ER protein folding disease is

A

cystic fibrosis

Psychology (25 decks)

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