Test 1 Flashcards
(136 cards)
1
Q
Hypothesis
A
your proposed explanation/ critical component of good science. Must be testable, quantifiable, and faslifiable
2
Q
T or F: Science is used to prove things
A
False, it is used to disprove things
3
Q
Independent Variable
A
the variable being changed/tested
4
Q
Dependent variable
A
the results based on what is changed
5
Q
Controlled Variable
A
used as a reference or baseline to compare
6
Q
Emergent Properties
A
adding the puzzle pieces together to create the bigger picture
7
Q
Living things must (be) (10)
A
Complex, highly organized, collect energy & transform it, respond to stimuli, regulate, reproduce, grow & develop, and evolutionary adaptation.
8
Q
System
A
combination of components that form a more complex organization
9
Q
Evolution
A
the change in frequency of heritable variation over time within a population
10
Q
prokaryotic cells
A
lack internal membrane structures (nucleoid, plasma membrane, cell wall)
example: bacteria
11
Q
Eukaryotic Cell
A
complex internal membrane systems (membrane-bound organelles) (Plant/animal)
12
Q
Do larger animals have larger cells?
A
No, they just have more cells
13
Q
Why are cells so small?
A
a smaller cell has a higher surface to volume ratio, which facilitates the exchange of materials into and out of the cell (efficiency)
14
Q
Phospholipids contain
A
hydrophilic head
hydrophobic tail
Lipids, proteins, carbohydrates, nucleic acids
15
Q
Phospholipid Function (outside of cell)
A
selective Barrier to environment
transport of nutrients and waste
16
Q
Nucleus Structure
A
enclosed membrane
nuclear envelope
genetic material
nucleolus
nuclear pore complex
17
Q
Nucleus: Enclosed Membrane Function
A
selective barrier
18
Q
Nucleus: Nuclear Envelope Function
A
Double membrane to regulate content
19
Q
Nucleus: Genetic Material Function
A
encodes instructions to make proteins and RNA
20
Q
Nucleus: Nucleolus Function
A
ribosomal RNA produced and combined with proteins to assemble ribosomes
21
Q
Nucleus: Nuclear Pore Complex Function
A
makes instructions on how to make proteins
directs and controls protein production
22
Q
Ribosomes Structure
A
resides in nuclear envelope, rough ER, and Cytoplasm
23
Q
Ribosome Function
A
catalyze production protein
24
Q
Endomembrane system structure
A
interconnected membranous organelles with many metabolic functions
jelly-like
25
Endomembrane system function
protein production & transport
lipid production & transport
deals with toxic byproducts
deals with pathogens
secreation
vesicles travel through
26
Rough ER Structure
contains ribosomes
27
Rough ER Function
protein production attached ribosomes
membrane production in cooperation with smooth ER
28
Smooth ER Structure
No ribosomes
29
Smooth ER Function
synthesize lipids
metabolize carbs
store & regulate calcium
detoxify poison
30
Golgi Apparatus Function
modifies and packages products received in vesicles from the ER for transport and/or secretion. Can make the products functional (attach a sugar)
31
Golgi Apparatus Structure
cis face
cisternae
trans face
32
Golgi A: Cis Face Function
receives unfinished products coming from ER
33
Golgi A: Cisternae Function
membrane sac where reactions occur
34
Golgi A: Trans Face Function
transport/package products in vesicles and ship out
35
Lysosome Structure
membranous sac of hydrolytic enzymes
36
Lysosome Function
break down/metabolize/compartmentalize hydrolytic enzymes so they don't digest the cell
golgi a. packages products in these
malfunction associated with many diseases
37
Lysosomal Storage Diseases
breaking down things you don't want to break down OR not breaking down things you need to get rid of
can have no function, malfunction, or barely any function
38
Vacuole Structure
diverse maintenance compartments
39
Vacuole Function
hydrolysis
storage
pumps
40
Mitochondria & Chloroplast Purpose
change energy from one form to another
2 membranes
have their own genome
have their own ribosomes
41
Mitochondria Structure
vary in number depending on metabolic needs of cell type (skeletal muscle cell vs skin cell)
folded inner membrane and smooth outer membrane
matrix (inner area containing DNA, ribosomes, and other enzymes)
42
Mitochondria Function
converts sugar to usable energy (ATP)
(Grow and go)
43
Chloroplast structure
contains chlorophyll
thylakoids
stroma
44
Chloroplast Function
uses solar energy to produce sugar from carbon dioxide and water
45
Chloroplast: Thylakoids Function
internal membrane system where most photosynthesis reactions take place
46
Chloroplast: Stroma Function
fluid-filled space between inner membrane and thylakoids
contain DNA, ribosomes, and enzymes
47
Peroxisomes Function
metabolizes other molecules
(energy, detoxification, etc.)
produces hydrogen peroxide as byproduct
(H2O2 toxic to cells, converts it to water)
48
Cytoskeleton Structure
microtubules
microfilaments
intermediate filaments
49
Cytoskeleton Function
shape, anchor, movement
interacts with motor proteins
"train track"
50
Cytoskeleton: Microtubule Structure
composed of tubulin protein
compression-resisting properties
cell shape
51
Cytoskeleton: Microtubule Function
guides movement interaction with motor proteins
52
Cytoskeleton: Microfilaments Structure
composed of actin protein
tension-bearing (pulling)
53
Cytoskeleton: Microfilament Function
muscle contraction with myosin, amoeboid movements
54
Cytoskeleton: Intermediate Filament Structure
more permanent structure
55
Cytoskeleton: Intermediate Filament Function
reinforce the shape of cells and organelles
56
Cell Wall Structure
cellulose fibers and protein of plants (plants and fungi)
57
Cell Wall Function
chemical and mechanical protection
58
Extracellular Matrix Structure
glycoproteins and proteoglycans (animal)
59
Extracellular Matrix Function
protection and communication
60
Tight Junction
cells pressed tightly and bound by proteins
things cannot pass easily between them
61
Desmosomes
anchor cells together
attach to intermediate filaments
loosely bound together
things can flow between the cells
62
Gap Junctions
connective channels between cells
specific channels from the inside of one cell to the inside of another
they have to communicate very quickly
63
Atom
smallest identifiable form of matter
64
Element
different personalities/ difference in subatomic particles/ interact with environment based on their makeup
65
Neutrons
no electrical charge
located in nucleus
66
Protons
positively charged
located in nucleus
# determines identity of atom
67
Electrons
Negatively charge
located outside nucleus in cloud-like state
68
The chemical behavior of an atom is determined by
the distribution of electrons in the electron shells
69
Covalent Bond
sharing of a pair of electrons
strongest bonds/takes the most energy to pull apart
70
Molecules
formed when two or more atoms join by covalent bonds
71
Single/Double Covalent Bonds
of electrons they are sharing
72
Electronegativity
attraction for the electrons in a covalent bond
the more electronegative an atom, the more strongly it pulls
73
Nonpolar Covalent Bond
atoms have similar electronegativities
share electrons equally (amount of time negative charge spends on one side is the same on both)
74
Polar Covalent Bonds
H2O
atoms have different electronegativities
share electrons differently
75
Hydrogen Bonds
forms when a hydrogen atom covalently bonds to one electronegative atom is also attracted to another electronegative atom
Not as strong/can form and break pretty easily
76
Polarity of a water molecule
allows them to form hydrogen bonds with each other and with other polar molecules
77
Weakest to highest Electronegativity (O, C, H, N)
H (low)
C (low)
N ( higher)
O (highest)
78
Ionic Bonds
an attraction between anions and cations
79
Ion
atoms with more or fewer electrons than usual (charged atom)
80
Anion
negatively charged
81
Cation
positively charged
82
Hydrophilic
Polar molecules tend to form hydrogen bonds with each other
83
Hydrophobic
nonpolar do not like things with polar charge
84
Ionic Compounds
Salts
85
Weak Noncovalent bonds
reinforce the shapes of large molecules
help molecules interact with each other
86
Polymer
macromolecules are made of these; built from monomers
87
Lipids
hydrophobic
have a lot of carbon and hydrogen atoms
form nonpolar covalent bonds
very diverse group of molecules
88
Fat Structure
constructed from a single glycerol and 3 fatty acids
89
Triglyceride
at 3 spots there are 3 different fatty acid chains
energy storage molecule
fatty acid chains = long tails
super high in energy (H, C)
90
Fatty Acid Characteristics
vary in length
vary in # and locations of double bonds between carbons
locations change structure and bond
have carboxyl group at one end
store large amounts of potential energy
91
Saturated Fatty Acid
have maximum number of hydrogen atoms possible
single bonds
straight line
solid at room temp
high in energy
92
Unsaturated Fatty Acid
have one or more double bonds between carbons in the fatty acid
bent line
liquid at room temp
high in energy
93
Hydrogenation
hydrogen added under pressure to saturate unsaturated fats.
94
Trans-Fats
common in processed food
less likely to be broken down
induce cholesterol production
heart disease risk
95
Phospholipids
2 fatty acids
phosphate group
Head = polar (hydrophilic)
Tail = nonpolar (hydrophobic)
Results in bilayer arrangement in cell membrane
96
Steroids Structure
lipids with 4 infused rings
ex: cholesterol
97
Proteins
extremely abundant in cells
diverse 3D structure
diverse functions
98
Polypeptide
protein consisting of more than 1 peptide
polymer of amino acids
99
Amino Acids
20 different ones used to build proteins
differ in their properties due to differing R-groups
linked by peptide bonds (strong covalent bonds)
100
R-group
20 unique ones
simple to complex
different properties
101
4 groups of amino acids
nonpolar/hydrophobic
polar/hydrophilic
charged/acidic
charged/basic
102
Nonpolar/hydrophobic
hydrocarbons
103
Polar/Hydrophilic
N and C are highly electronegative and H and O are not = polar
form hydrogen bonds with each other
104
Charged Acidic
full negative charge in R-group
Ionic
105
Charged Basic
Full positive charge in R-group
Ionic
106
Protein: Primary structure
unique sequence of amino acids
where amino acids go determine function of protein
107
Protein: Secondary Structure
Folding/coiling into a repeating configuration
result of hydrogen bonding between amino acid functional groups
beads on a string
(helix/pleated sheet)
108
Protein: Tertiary Structure
3D shape of polypeptide
109
Protein: Quaternary Structure
aggregation of 2 or more polypeptide subunits
110
Protein conformation depends on
physical and chemical conditions of the protein's environment
111
Denaturation
protein unravels and loses its shape
112
Plasma Membrane
exhibits selective permeability
113
6 Membrane Protein Functions
enzymatic function
signal transduction
intercellular joining
attach cytoskeleton to ECM
cell-cell recognition
receptor
114
Cell-Cell Recognition
ability to distinguish one cell type from another
important for development of tissues and organs, immune system, and transplants
115
Hydrophobic molecules and the Membrane
lipid soluble and can pass through membrane rapidly
116
Polar (hydrophilic) Molecules and the Membrane
do not pass membrane quickly
117
Transport Proteins
allow passage of hydrophilic substances across memebrane
118
Passive Transport
diffusion of a substance across a membrane with no energy
119
Diffusion
tendency for molecules of any substance to spread out evenly into the available space
120
Concentration Gradient
the difference in concentration of a substance over space
substances diffuse down
121
Active Transport
Needs energy to cross membrane
Travels against the concentration gradient
122
Osmosis
the movement of water a cross a semipermeable membrane
123
Tonicity
The ability of a solution to cause a cell to gain or lose water
always relative
124
Isotonic Solution
Same concentration
the environment inside the cell is isotonic to the outside of the cell/the outside of the cell is isotonic to the inside of the cell
125
Hypertonic Solution
Above the concentration
Concentration of solute is higher/water is lower = cell loses water
if a cell is placed in a hypertonic solution, the water will flow out of the cell, causing it to shrink
126
Hypotonic Solution
below the concentration
solution is hypertonic relative to the inside of the cell with is hypotonic
if a cell is placed in a hypotonic solution, water will flow into the cell, causing it to swell and possibly burst
127
Osmoregulation
adaptations to deal with hypertonic or hypotonic environments
128
Facilitated Diffusion
passive transport aided by proteins (no energy)
129
Most difficult to least difficult transporting across membrane
Ions, Large polar (most difficult)
Small polar, large nonpolar
small nonpolar (least difficult)
130
Gated Channels
opened when bound to signal molecules or receive other stimuli
131
Carrier Proteins
bind to a specific molecule inducing a substle shape change that translocates the solute-binding site across the membrane
132
Cotransport
uses energy from the diffusion of one molecule to power the active transport of another
133
Exocytosis
transport vesicles migrate to the plasma membrane, fuse with it, and release their contends (natural/protien-induced)
134
Endocytosis
the cell takes in macromolecules by forming new vesicles from the plasma membrane
phagocytosis/pinocytosis/receptor-mediated endocytosis
135
Phagocytosis
food/large molecules
136
Pinocytosis
water and small dissolved solutes
