Exam 1 Flashcards

(122 cards)

1
Q

Prokaryotes

A

unicellular
Eubacteria and Archaebacteria

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2
Q

Eukaryotes

A

some unicellular, mostly multicellular

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3
Q

Endomembrane System

A

nuclear envelope, endoplasmic reticulum, Golgi apparatus, lysosomes, endoscopes

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4
Q

Cytoplasm

A

everything between plasma and membrane and nuclear envelope

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5
Q

Cytosol

A

Gel-like substance excluding the membrane-bound organelles

includes the cytoskeleton and nonmembrane-bound inclusions

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6
Q

Organelles

A

discrete membrane-bound sub cellular compartments specialized to carry out specific cellular functions

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7
Q

Rough Endoplasmic Reticulum

A

lots of surface area and membrane, layers of flattened membrance studded with ribosomes for synthesis of protein

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8
Q

Smooth Endoplasmic Reticulum

A

no ribosomes, smooth tubules, cholesterol biosynthesis, membrane biosynthesis, detoxification

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9
Q

Golgi Apparatus

A

processes and packages material for secretion out of cell or to different part of the cell

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10
Q

Lysosomes

A

intracellular digestion…uses enzymes to digest/break down large materials such as fats, proteins, carbohydrates

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11
Q

Central Vacuole

A

stores water, ions, organic molecules, toxic metabolites

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12
Q

Mitochondrion

A

oxidation of carbohydrates and fatty acids and production of ATP

has its own ribosomes

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13
Q

Chloroplasts

A

photosynthesis and starch production

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14
Q

Cytoskeleton

A

series of proteinaceous filaments and tubules
controls cell shape, cell motility, replication, secretion, gene expression, etc

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15
Q

Microfilaments

A

Cytoskeleton
made up of strands of the protein actin, often interact with strands of other proteins

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16
Q

Intermediate filaments

A

Cytoskeleton
made up of fibrous proteins organized into tough, roselike assemblages that stabilize a cell’s structures and help maintain its shape

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17
Q

Microtubules

A

Cytoskeleton
long, hollow cylinders made u pof many molecules of the protein tubule

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18
Q

matter

A

anything that takes up space and has mass

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19
Q

compound

A

contains two or more different elements in a defined ratio

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20
Q

Trace elements

A

small but important

Fe in Heme
Iodine in Thyroid Hormone

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21
Q

smallest unit of structure containing all of the chemical and physical properties of an element

A

atom

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22
Q

strong and stable bond resulting from electron sharing

A

covalent bond

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23
Q

Molecule

A

two or more atoms held together by covalent bonds

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24
Q

measure of how strongly an atomic nucleus attracts and holds onto electrons

A

electronegativity

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25
if a covalent bond is formed between two atoms of the same type, the electrons are shared equally
Nonpolar Covalent Bonds
26
unequal electron sharing
Polar Covalent Bond
27
Weak Bonds
hydrogen bonds, ionic bonds, van der Waals Interactions
28
when a Hydrogen covalently bonded to one electronegative atom is attracted to another nearby electronegative atom weak bonds
Hydrogen bonds
29
electronegativity difference may be so large as to literally pull electrons from the outer shell crystal
Ionic Bonds
30
molecules with nonpolar bonds can have localized regions of partial positive or partial negative charge determine: 3D shape of proteins, interactions between enzyme and substrate, interactions of antigen-anitbody interactions
van der Waals Interactions
31
Properties of water
adhesion and cohesion moderation of temperature (high specific heat) heat of vaporization evaporative cooling solid H2O is less dense than liquid H2O
32
Plasma Membrane
the membrane found in all cells that separates the interior of the cell from the outside environment
33
Nucleus
stores DNA/genetic info
34
Nucleolus
The nucleolus is a spherical structure found in the cell's nucleus whose primary function is to produce and assemble the cell's ribosomes. The nucleolus is also where ribosomal RNA genes are transcribed.
35
What do chemical bonds result from
interactions between valence shell electrons between elements
36
Four different basic types of molecules
lipids, proteins, carbohydrates, nucleic acids
37
macromolecules
carbohydrates, proteins, lipids, and nucleic acids form huge molecules
38
monomer
subunits that make up macromolecules
39
polymer
chain of covalently attached monomers
40
dehydration synthesis
removes a water molecule, forming a new bond one H2O released for every monomer added to the polymer
41
hydrolysis
one molecule of H2O added for every monomer removed from the polymer
42
saccharide
sugar monosaccharide, polysaccharide, etc monosaccharides have common structure
43
names that usually end in the suffix -ose
carbohydrates
44
covalent bond connecting monosaccharides
glycosidic linkage
45
functions of polysaccharides
energy storage structure protection starch glycogen
46
structural polysaccharides
polymers of ß-form monosaccharides form rigid rods rather than loose helices cellulose
47
cellulose
plant cell walls most abundant organic molecule on Earth dietary fiber
48
functions: energy storage, protection, recognition, and structural integrity
carbohydrates
49
Functions: energy storage, biomembrane structure, hormones characterized by hydrophobicity
lipids
50
No C=C
saturated
51
One C=C
monounsaturated
52
Many C=C
polyunsaturated
53
why is water a universal solvent
hydrogen bonding H2O forms a hydration shell, separating ions allowing them to dissolve in water
54
increases the relative concentration of h+ in a solution
acid
55
decreases the relative concentration of H+ in a solution
base
56
why is carbon structurally loved in organic stuff
4 valence electrons, so it either needs 4 more or 4 less forms single, double, or triple covalent bonds
57
hydrocarbons
hydrogens and carbons nonpolar covalent bonds relatively unreactive
58
molecules with the same molecular formulae but with distinct arrangements of the atoms
isomers
59
specialized form of structural isomer where they differ in the arrangement of groups across a C=C
geometric isomers cis = same side trans = opposite side
60
mirror image isomer molecules that differ in the orientation of atoms around an asymmetric carbon
enantiomers
61
animal lipids
usually saturated fatty acids tails pack tightly solid at room temperature
62
plant lipids
usually unsaturated fatty acids tails pack more loosely liquid at room temperature oils
63
phosphlipids
hydrocarbon chains hydrophobic tail and hydrophilic head = amphipathic bilayer segregates inside from outside
64
steroids
4 fused carbon rings hydrophobic
65
Protein functions
Catalysts structure communication transport motility defense recognition regulation storage
66
protein monomer
amino acid
67
amino acid structure
amino group and carboxyl group different R groups
68
Polymer formation
amino group and carboxyl group are bonded with a peptide bond dehydration synthesis --> water is released
69
four levels of protein structure
primary, secondary, tertiary, quaternary
70
protein structure that genetically determines linear sequence of amino acids
primary structure
71
protein structure with hydrogen bonds within the backbone
secondary structure
72
protein structure with molecular interactions between R groups within the chain
tertiary structure
73
protein structure with subunit interactions
quaternary structure
74
Spontaneous protein folding in Isolation
normal protein --> denaturation --> de natured protein --> renaturing (though not always)
75
factors that impact final protein structure
temperature, ionic strength, pH
76
correct protein folding
molecular chaperonin...fold molecules in teh right shape
77
mutation that results from misfolded proteins
sickle cell disease anemia
78
long, linear chains off covalently bonded nucleotide monomers Function: storage and transmission of genetic informations
Nucleic Acids
79
two types of nucleic acids
Ribonucleic Acid (RNA) Deoxyribonucleic Acid (DNA)
80
nucleic acid monomer
nucleotide base + sugar
81
Purines
Adenine and Guanine RNA and DNA
82
Pyrimidines
Cytosine (DNA and RNA) Thymine (DNA) Uracil (RNA)
83
bond that joins nucleotides
phosphodiester bond
84
Base pairing
A and T G and C
85
Metabolism
collection of all biochemical reactions occurring in a cell
86
breakdown of larger, more complex molecules into smaller, less complex molecules releases chemical energy
catabolism
87
synthesis of larger, more complex molecules from smaller, less complex molecules requires input of energy
anabolism
88
Energy can be transferred and transformed but it cannot be created or destroyed
1st Law of Thermodynamics
89
during every transformation, some energy becomes unusable to use --> heat
2nd Law of Thermodynamics
90
unusable energy
entropy
91
measure of disorder of the universe
entropy
92
any process that occurs without input of energy
spontaneous
93
energy available in a system to do work
free energy (G)
94
total energy in a system
enthalpy
95
∆G = ∆H - T∆S
amount of usable energy = total amount of energy - amount of usable energy
96
spontaneous reaction
free energy is reduced ∆G is negative = exergonic
97
∆G is negative
exergonic
98
nonspontaneous reaction
free energy is increased ∆G is positive = endergonic
99
∆G is postive
endergonic
100
∆G is 0
equilibrium
101
is all reactions are at equilibrium...
no free energy change --> no work --> dead cell
102
anabolic reactions building large molecules
chemical work
103
directed movement ciliary beating, muscle contration, chromosome separation
mechanical work
104
building gradients pumping substances across a membrane against a gradient
transport work
105
generating light
bioluminescence
106
what forms glycosidic linkage
dehydration synthesis
107
what are nucleotides made of
nitrogenous base, 5C sugar, phosphate group
108
What impacts optimal enzyme conditions?
temperature (optimal is 37 degrees C) pH
109
Saturation
rate of product formation is at a maximum all functional enzyme molecules are binding substrate and converting it into product at MAX SPEED
110
Enzyme effector molecules
Activators and Inhibitors
111
Increase rate of product formation (in enzyme)
activators
112
decrease rate of product formation (in enzyme)
inhibitors
113
nonprotein enzyme activators
Cofactors organic cofactor = coenzyme
114
types of enzyme inhibitors
irreversible inhibitors and reversible inhibitors
115
Covalent attachment to enzyme usually at active site
Irreversible inhibitors
116
noncovalent attachment to enzyme
reversible enzyme inhibitors
117
Types of reversible enzyme inhibitors
competitive and noncompetitive
118
how can the effect of a competitive inhibitor be reduced
by increasing the concentration of substrate
119
binds to enzyme away from active site changing structure of enzyme, reducing ability of enzyme to function normally
noncompetitive inhibitor
120
molecules that bind to an enzyme away from the active site
Allosteric regulatory molecules
121
molecules that change the conformation and activity of the enzyme
regulatory molecules
122
Conformations of multisubunit enzymes
functional and nonfunctional