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cell bio > unit 1 terms > Flashcards

unit 1 terms Flashcards

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Biology 101 flashcards
1
Q

cell theory

A

Was first proposed in 1839, it was the concept that all living organisms are made of cells and all these cells are formed by the reproduction of existing cells.

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2
Q

prokaryote

A

-small
-lack a nucleus
-have little to no organized internal structure
-replicate quickly

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3
Q

Eukaryotes

A

-large
-can be single cell or multicellular
-contains organelles such as: nucleus, mitochondria/chloroplast, endomembrane system, cytoskeleton
-some have cell walls
-some have flagella

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4
Q

bacteria

A

A member of a large group of unicellular microorganisms which have cell walls but lack organelles and an organized nucleus, including some that can cause disease.

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5
Q

cytoplasm

A

is everything in a cell, except for the contents of the nucleus

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6
Q

cytosol

A

is everything inside the cytoplasm that is not inside any organelle

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7
Q

cytology

A

the study of cellular structure

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8
Q

SEM

A

specimens are coated with a film of metal (platinum or gold) that causes the electrons to scatter. shows a 3D image of the cell exterior.

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9
Q

TEM

A

shows high resolution imaging of thin sections of the cell’s interior structure

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10
Q

fluorescence microscopy

A

Uses filters to select specific wavelengths of light that will excite fluorescent tags. Is useful to look at specific components of the cell.

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11
Q

Confocal microscopy

A

uses a laser beam to take optical sections of specimens. More details than fluro

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12
Q

elements

A

chemically pure substances that cannot be chemically broken down.

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13
Q

Atoms

A

the basic unit of a chemical element

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14
Q

proton

A

positively charged, found in the nucleus

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15
Q

neutron

A

no charge, found in the nucleus

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16
Q

electron

A

negatively charged, found in orbitals surrounding the nucleus

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17
Q

atomic number

A

determined by the number of protons

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18
Q

atomic weight

A

determined by adding up the number of protons and neutrons

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19
Q

ionic bond

A

forms when one electron transfers from one atom to another, leaving both atoms with a full outermost shell and opposite charges that hold them together.

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20
Q

covalent bond

A

form when two atoms share one or more pairs of electrons to fill their outermost shell.

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21
Q

electronegativity

A

the strength of pull that an atom has on their electrons

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22
Q

polar covalent bonds

A

electrons are shared unequally

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23
Q

non-polar covalent bond

A

electrons shared equally

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24
Q

hydrogen bonds

A

weak bonds formed between a H with a slight positive charge, and another molecule’s atom with a slight negative charge. Individually they are weak, but many H-bonds working together can be very strong.

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25
Q

electrostatic interactions

A

are forces that draw together oppositely charged atoms

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26
Q

solvent

A

substance in which other substances can dissolve

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27
Q

hydrophilic

A

(water-loving) can interact with water. includes DNA, RNA, most proteins, carbohydrates

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28
Q

hydrophobic

A

(water-fearing) molecules are unchanged, form few or no H-bonds, and do not dissolve in water

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29
Q

Acid

A

substances that release a proton

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30
Q

base

A

substances that steal a proton

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31
Q

Ph

A

the measure of how acidic/basic something is

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32
Q

monomer

A

one of one

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33
Q

nucleic acid

A

store information - the genetic code
made up of nucleotide monomers (5 carbon sugar, nitrogen-rich ring compound(base) and phosphate group)

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34
Q

ATP

A

Adenosine triphosphate is a modified nucleotide -3 phosphate group linked together. When the bonds between phosphate groups are broken, energy is released.

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35
Q

phosphodiester bond

A

bond between nucleotides

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36
Q

Protein

A

are made up of monomers of amino acids that are linked by peptide bonds

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37
Q

Amino Acids

A

monomers that makeup proteins, one side free amino group and other side free carboxyl

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38
Q

peptide bond

A

bonds that link together amino acids to make proteins

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39
Q

Carbohydrates

A

made up of sugars (monosaccharides)

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40
Q

Monosaccharide

A

the monomers of carbohydrates

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41
Q

isomer

A

molecules with the same chemical formula but different structures

42
Q

Glycosidic bond

A

the bond that links monosaccharides that make carbohydrates

43
Q

Condensation reaction

A

when a water molecule is expelled

44
Q

starch

A

what glucose is store as in plants

45
Q

cellulose

A

made of long strands of glucose that provides structural support to plants

46
Q

Glycogen

A

where glucose is stored in animals

47
Q

Lipid

A

diverse group of non-polar molecules that are important for energy storage, structure, and signaling

48
Q

Fatty acid

A

have long, hydrocarbon tail and a carboxyl group (-cooh), which behaves as an acid

49
Q

Amphipathic

A

Possess both hydrophobic and hydrophilic regions

50
Q

Saturated

A

no kink in chain

51
Q

unsaturated

A

kink in the chain due to double bonds

52
Q

Triacylglyceride

A

have 3 fatty acids joined by a glycerol molecule (small sugar)

53
Q

phospholipids

A

Aggregate to form the phospholipid bilayer also known as the cell membrane.

54
Q

1st law of thermodynamics

A

energy cannot be created or destroyed, only converted from one form to another

55
Q

2nd law of thermodynamics

A

the universe (or any isolated system) is constantly moving towards disorder

56
Q

entropy

A

the measure of disorder

57
Q

catabolic

A

pathways break down larger molecules into smaller (polymer to monomer)

58
Q

anabolic

A

pathways build larger molecules from smaller ones (monomer to polymer)

59
Q

free energy (G)

A

Useful energy that is dissipated as heat which increases disorder

60
Q

delta G

A

not constant, can be affected by different things such as the concentration of molecules in the reaction at any time.

61
Q

equilibrium constant

A

delta g is equal to zero

62
Q

coupled reaction

A

reactions that are energetically unfavorable can be coupled (linked) to second, energetically favorable reactions.

63
Q

activated carriers

A

molecules that store energy in an easily exchangeable form, either as readily transferable chemical groups or as readily transferable electrons.

64
Q

catalysis

A

the acceleration of a chemical reaction

65
Q

activation energy

A

the minimum quantity of energy which the reacting species must possess in order to undergo a specific reaction.

66
Q

substrate

A

the specific molecule each enzyme binds to

67
Q

active site

A

A region on an enzyme that binds to a protein or other substance during a reaction.

68
Q

polypeptide

A

what they call a chain of amino acids being held together by covalent peptide bonds

69
Q

polypeptide backbone

A

the repeating sequence of amino acids that make up the core of a polypeptide chain

70
Q

primary structure

A

amino acid sequence

71
Q

secondary structure

A

structures that form in certain segments of the AA chain, provide structures

72
Q

tertiary structure

A

full 3D conformation formed by an entire polypeptide chain

73
Q

quaternary structure

A

when multiple polypeptides form a single complex

74
Q

alpha helix

A

spirals. N-H of one AA is H-bonded to the C=O located 4AA away.

75
Q

beta sheets

A

Form when H-bonds form between parts of the polypeptide chain that lie side by side. Give strength and stability to proteins.

76
Q

coiled-coil

A

When two or more alpha-helices are wound around each other to form a supercoiled bundle.

77
Q

disulfide bond/bridge

A

covalent bonds that occur between -SH groups in cysteine residues. Not responsible for protein shape, but rather reinforces the 3D structure a protein takes due to non-covalent interactions.

78
Q

protein domain

A

any segment of a polypeptide chain that can fold independently into a compact, stable structure

79
Q

protein families

A

proteins with similar sequences and 3D structure

80
Q

prion

A

are misfolded proteins that cause infectious neurodegenerative diseases to occur.

81
Q

phosphorylation

A

involves the transfer of a phosphate group from ATP to a hydroxyl group of an AA

82
Q

kinase

A

what adds phosphates

83
Q

phosphatase

A

what removes phosphates

84
Q

turnover number

A

the maximal number of molecules of substrate converted to product per active site per unit time when the enzyme is saturated with substrate.

85
Q

Michaelis constant (Km)

A

the substrate concentration at which the reaction rate occurs at 0.5 the Vmax

86
Q

competitive inhibitor

A

mimic substrates and tie up enzymes

87
Q

allosteric inhibitor

A

a molecule that binds to an enzyme’s allosteric site to reduce or prevent the enzyme’s activity.

88
Q

feedback inhibition

A

when an enzyme early in a reaction pathway is inhibited by a late product of the pathway.

89
Q

positive regulation

A

can also occur where an enzyme’s activity is stimulated rather than inhibited.

90
Q
A
91
Q

centrifugation

A

removing cell parts, largest to smallest

92
Q

gel electrophoresis

A

uses an electric current to separate proteins in a gel matrix. The direction and speed at which the proteins move depends on their size and charge.

93
Q

chromatography

A

a method that uses different materials to separate the individual components of a complex mixture into proteins based on the properties of the proteins.

94
Q

ion exchange chromatography

A

Separates proteins by charge. often used in purification and quality control

95
Q

anion exchange

A

uses positively charged beads (to extract negative charged proteins)

96
Q

cation exchange

A

uses negatively charges resins or beads (to extract positively charged proteins

97
Q

antibody

A

proteins that protect you when an unwanted substance enters your body

98
Q

antigens

A

a substance that causes the body to produce an immune response against it

99
Q

affinity chromatogrpahy

A

used to separate proteins by using matrix beads coated in antibody-specific solutions for desired proteins. This lets the protein bind, while the impurities flow away. Then, using a changing pH or high salt, wash the protein to disrupt purities.

100
Q

mass spectrometry

A

a method to analyze proteins which ionizes small chemicals (like short peptides) and sorts them based on mass-to-charge ratio

cell bio (2 decks)

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