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BIOL 300 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

triacylglycerol molecules

A

6x the energy in glucose

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2
Q

Metabolism

A
  • controlled set of chemical reactions that occur in living cells to sustain life
  • allow organisms to grow and reproduce, maintain structures, and respond to the environment
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3
Q

Starting product of glycolysis

A

glucose

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4
Q

Glycolysis occurs in…?

A

cytoplasm

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5
Q

Glycolysis is an …. process

A

anaerobic

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6
Q

End products of glycolysis

A

2 pyruvate, 2 ATP, 2 NADH

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7
Q

Pyruvate oxidized to acetyl coA occurs when?

A

Between stages 1 & 2 of glycolysis

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8
Q

Pyruvate oxidized to acetyl coA occurs where?

A

Mitochondrial matrix

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9
Q

Pyruvate oxidized to acetyl coA is catalyzed by…?

A

Pyruvate dehydrogenase

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10
Q

Enzyme-coupled reaction

A

Two coupled half-reactions (spontaneous and non-spontaneous)

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11
Q

When do enzyme-coupled reactions occurs?

A

Steps 6 & 7 of glycolysis

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12
Q

What initiates Krebs cycle?

A

Generation of acetyl coA

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13
Q

Krebs cycle occurs where?

A

Mitochondrial matrix

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14
Q

Krebs cycle is an …. process

A

anaerobic

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15
Q

Oxidative phosphorylation

A

Reduces oxygen to water

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16
Q

Oxidative phosphorylation occurs in …?

A

mitochondrial membrane

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17
Q

Oxidative phosphorylation requires ….?

A

oxygen + 30 ATP

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18
Q

Products of the Citric Acid cycle

A

ATP, FADH2, NADH

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19
Q

Drosophila melanogaster

A

-revealed structure of adult multicellular organism

-DNA genome well-known

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20
Q

Transmission electron microscope

A
  • uses an electron beam to study the internal structure of thinly sectioned specimens
  • can see cellular components as small as 2 nm
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21
Q

polymerization

A

joining by covalent bonds

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22
Q

monosacccharides

A

joined by covalent, glycosidic bonds

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23
Q

peptide bond

A

covalent linkage between adjacent amino acids in protein chain

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24
Q

nucleic acids

A

long polymers of covalently bound nucleotides

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25
Q

phosphodiester bonds

A

bond formed between sugar and phosphate to form backbone of nucleic acids

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26
Q

Where are phosphodiester bonds located?

A

between 5’ and 3’ C

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27
Q

Metabolic pathways

A
  • connected in series
  • end product is starting material for next reaction
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28
Q

Where do electrons for proton gradient come from?

A

Krebs cycle

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29
Q

2 organelles that likely evolved from bacteria

A

mitochondria and chloroplasts

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30
Q

Type of microscope that requires 2 filters?

A

Fluorescent

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31
Q

Nonpolar amino acids are …?

A

Hydrophobic

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32
Q

How are images generated in confocal microscopy?

A

Single plane of focus (optical section)

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33
Q

amphipathic

A

having both hydrophobic and hydrophilic regions

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34
Q

Exceptions to central dogma

A

Viruses

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35
Q

Genes hold the code, but _____ determines function

A

expression

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36
Q

z-stack

A

images of a series of optical sections

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37
Q

prokaryotes

A
  • small, single-celled
  • most diverse of all cells
  • can adapt to extreme environments
  • 2 domains: bacteria and archaea
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38
Q

eukaryotes

A
  • can be single-celled or multicellular
  • membrane-bound nucleus
  • most have organelles
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39
Q

endoplasmic reticulum

A

“highway” of the cell

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40
Q

lysosome

A

waste disposal system

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41
Q

peroxisomes

A

provide a safe space in the cell to carry out biochemical processes that are harmful to the cell

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42
Q

Eukaryotes likely evolved as ___?

A

predators

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43
Q

What aids eukaryotes w/ movement?

A

cytoskeleton + large flexible membrane

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44
Q

Arabidopsis thaliana

A
  • common wall cress
  • produces thousands of offspring in 8-10 weeks
  • easily grown indoors
  • complete DNA sequence known
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45
Q

C. elegans

A
  • neurons of brain completely mapped
  • led to understanding of apoptosis
  • used in alcohol studies
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46
Q

Danio rerio

A
  • zebra fish
  • transparent for first 2 weeks of life
  • excellent for developmental studies
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47
Q

Hayflick limit

A

maximum # of times cell can divide

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48
Q

immortalized cell line

A

“transformed” cells can grow indefinitely

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49
Q

Cells are mostly comprised of ___?

A

carbon compounds

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50
Q

hydrophilic

A

dissolves in water (DNA, RNA, sugars)

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51
Q

non-covalent bonds

A
  • weaker
  • Molecular Dating
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52
Q

condensation reaction

A
  • creates bond
  • H2O is expelled as bond forms
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53
Q

hydrolysis

A
  • breaks bond
  • H2O is consumed
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54
Q

What makes up lipids?

A

fatty acids

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55
Q

carboxyl group

A
  • chemically reactive
  • behaves as an acid
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56
Q

saturated fats

A
  • no double bonds
  • pack together in solid mass (clogged artery)
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57
Q

unsaturated fats

A
  • contain at least 1 double bond
  • bonds produce kinks
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58
Q

Directionality

A

N –> C

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59
Q

RNA

A

bases: A, G, C, U
- usually single-stranded

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60
Q

Western blotting

A

allows visualization of proteins w/ use of antibodies that bind to proteins of interest

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61
Q

confocal microscopy

A

scans specimen w/ focused laser beam

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62
Q

Bonds in carbs

A

glycosidic

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63
Q

light microscope

A

uses a beam of light passing through one or more lenses to magnify an object

64
Q

electron microscope

A

forms an image by focusing beams of electrons onto a specimen

65
Q

confocal microscope

A

uses fluorescent stains and laser to make two- and three-dimensional images

66
Q

Scanning electron microscope

A

uses an electron beam to scan the surface of a sample, coated with metal atoms, to study details of its topography

67
Q

fluorescent microscope

A

used to visualize a specimen that has been labeled with a fluorescent dye; samples are illuminated with a wavelength of light that excites the dye, causing it to fluoresce

68
Q

chloroplast

A

organelle found in plant and algae cells where photosynthesis occurs

69
Q

ribosomes

A

protein synthesis

70
Q

mitochondria

A

powerhouse of the cell –> biochemical processes for respiration and energy production occur

71
Q

smooth ER

A

portion of ER responsible for creating lipids

72
Q

rough ER

A

portion of ER studded with ribosomes

73
Q

plasma membrane

A

selectively permeable phospholipid bilayer forming boundary of cells

74
Q

nucleus

A

control center

75
Q

golgi apparatus

A

stack of membranes in the cell that modify, sort, and package proteins from ER

76
Q

cytoskeleton

A

network of fibers that holds the cell together, helps the cell to keep its shape, and aids in movement

77
Q

exocytosis

A

Process by which a cell releases large amounts of material

78
Q

endocystosis

A

process by which a cell takes material into the cell by infolding of the cell membrane

79
Q

E. coli

A
  • Used to replicate bacterial growth.
  • Grow rapidly
  • Showed us how cells replicate their DNA and how they decode their DNA to make proteins
80
Q

N-terminus

A

the end of a polypeptide or protein that has a free amino group

81
Q

C-terminus

A

the end of a polypeptide or protein that has a free carboxyl group

82
Q

conformation

A

The particular three-dimentional shape of a protein molecule

83
Q

Catabolism

A

Metabolic pathways that break down molecules, releasing energy

84
Q

Catabolic pathways

A

Metabolic pathways that release energy by breaking down complex molecules into simpler compounds

85
Q

entropy

A

measure of disorder or randomness

86
Q

photosynthesis

A

conversion of light energy from the sun into chemical energy

87
Q

cellular respiration

A

process that releases energy by breaking down glucose in the presence of oxygen

88
Q

electron transport chain

A

A sequence of electron carrier molecules (membrane proteins) that shuttle electrons during the redox reactions that release energy used to make ATP

89
Q

NADPH

A

An electron carrier involved in photosynthesis

90
Q

NADH

A

reduced form of NAD+; an electron-carrying molecule that functions in cellular respiration

91
Q

alpha helix

A

A spiral shape constituting one form of the secondary structure of proteins, arising from a specific hydrogen-bonding structure

92
Q

Beta pleated sheet

A

The polypeptide folds back and forth on itself, forming a pleated sheet that is stabilized by hydrogen bonds between carbonyl groups in one chain and amide groups in the other chain
- can be parallel or antiparallel

93
Q

primary structure

A

amino acid sequence

94
Q

secondary structure

A

alpha helix and beta pleated sheet

95
Q

tertiary structure

A

full 3D conformation of a single polypeptide chain

96
Q

quaternary structure

A

complex of multiple polypeptide chains

97
Q

globular proteins

A

proteins that are water soluble

98
Q

fibrous proteins

A

structural sheets or strands

99
Q

disulfide bonds

A

hold extracellular proteins together

100
Q

ligand

A

A molecule that binds specifically to another molecule, usually a larger one

101
Q

substrate

A

The reactant on which an enzyme works

102
Q

binding site

A

the location on a receptor protein to which a ligand binds

103
Q

antibodies

A

Specialized proteins that aid in destroying infectious agents. Y shaped and attacks antigens

104
Q

antigens

A

Foreign material that invades the body

105
Q

active site of enzyme

A

the region of an enzyme that attaches to a substrate

106
Q

positive feedback

A

Magnifies a process or increases its output

107
Q

negative feedback

A

Counteracts or stops process

108
Q

allosteric regulation

A
  • The binding of a regulatory molecule to a protein at one site that affects the function of the protein at a different site.
  • Changes the shape of the active site
109
Q

competitive regulation

A

the binding of a regulatory molecule to an enzymes active site which makes the enzyme inactive

110
Q

protein kinase

A

An enzyme that transfers phosphate groups from ATP to a protein, thus phosphorylating the protein

111
Q

GTP

A

energy source in protein synthesis

112
Q

protein phosphorylation

A

The covalent addition of a phosphate group to a side chain of a protein, catalyzed by a protein kinase

113
Q

GTP-binding proteins

A
  • Molecular switches in cells
  • Crucial role in intracellular signaling
  • When the protein hydrolyses the phosphate, it switches the protein to “off”
114
Q

motor proteins

A

A protein that interacts with cytoskeletal elements and other cell components, producing movement of the whole cell or parts of the cell

115
Q

chromatography

A

a process which separates the parts of a solution with special paper and a solvent

116
Q

electrophoresis

A

method of separating serum proteins by electrical charge

117
Q

mass spectometry

A

a technique that separates particles according to their mass

118
Q

X-ray crystallography (NMR)

A

determines protein structure

119
Q

receptor protein

A

information receptor that binds to other protein, triggering signal cascade

120
Q

ubiquitination

A

signal to degrade/move protein

121
Q

phosphorylation

A

turns p53 on and off

122
Q

hydrolysis of GTP causes __?

A

small shift in structure –> large change in function

123
Q

PDE5

A

breaks down cGMP

124
Q

effector proteins

A

effect targeted cell responses

125
Q

fast response time

A

phosphorylation turning proteins on and off (seconds to minutes)

126
Q

Barbiturates

A

sedation

127
Q

Nicotine

A

elevation of blood pressure

128
Q

Morphine/heroin

A

analgesic/euphoria

129
Q

Curare

A

paralysis

130
Q

Capsaicin

A

spicy food

131
Q

Menthol

A

cold/hot (Bengay)

132
Q

Viagra

A

blocks PDE5 + breaks down cGMP

133
Q

Nitric oxide gas

A

released from endothelial cells and diffuses into smooth muscle cells, causing prolonged relaxation

134
Q

slow response time

A

transcription and translation making more proteins (minutes to hours)

135
Q

protein machines

A

individual proteins collaborating to perform specific tasks

136
Q

proteins can walk along ___?

A

cytoskeleton

137
Q

phosphatase

A

removes phosphate

138
Q

“on/off” switch

A

phosphorylation (chemical modification)

139
Q

What does phosphorylation do?

A

changes shape of protein –> changes function of protein

140
Q

4 things signaling cascades do

A

relay, amplify, integrate, distribute

141
Q

What chains does post-translational modification effect?

A

Serine, threonine, tyrosine

142
Q

Post-translational modification form ___?

A

regulatory protein code (protein “to-do” list)

143
Q

Signaling cascade

A

External receptor –> intracellular signaling molecules –> effector proteins –> target cell responses

144
Q

acetylation

A

modulates p53 activity

145
Q

protein folding disorders

A

Alzheimer’s, prions, Parkinson’s

146
Q

Most hormones are ___?

A

small + hydrophobic

147
Q

feedback inhibition

A

enzyme acting early in a reaction pathway inhibited by late product of pathway

148
Q

What stabilizes folded protein shape?

A

Hydrogen bonds

149
Q

What is required to produce ATP?

A

membrane, proton pump, ATP synthase, source of high energy e- and H+

150
Q

covalent bonds

A

Molecular Marriage

151
Q

Final 3D shaped determined by?

A

amino acid sequence

152
Q

What regulates glycogen?

A

Hormones

153
Q

Excess sugar is converted into?

A

fatty acids

154
Q

Amino acids linked by?

A

peptide bonds

155
Q

Protein folding aided by?

A

molecular chaperones

156
Q
A

BIOL 300 (1 decks)

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