Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

cell bio > unit 1 terms > Flashcards

unit 1 terms Flashcards

(100 cards)

Start Studying
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

prokaryote

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

cytoplasm

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

cytosol

A

is everything inside the cytoplasm that is not inside any organelle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

cytology

A

the study of cellular structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

TEM

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Confocal microscopy

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

elements

A

chemically pure substances that cannot be chemically broken down.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Atoms

A

the basic unit of a chemical element

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

proton

A

positively charged, found in the nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

neutron

A

no charge, found in the nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

electron

A

negatively charged, found in orbitals surrounding the nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

atomic number

A

determined by the number of protons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

atomic weight

A

determined by adding up the number of protons and neutrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

covalent bond

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

electronegativity

A

the strength of pull that an atom has on their electrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

polar covalent bonds

A

electrons are shared unequally

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

non-polar covalent bond

A

electrons shared equally

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
electrostatic interactions
are forces that draw together oppositely charged atoms
26
solvent
substance in which other substances can dissolve
27
hydrophilic
(water-loving) can interact with water. includes DNA, RNA, most proteins, carbohydrates
28
hydrophobic
(water-fearing) molecules are unchanged, form few or no H-bonds, and do not dissolve in water
29
Acid
substances that release a proton
30
base
substances that steal a proton
31
Ph
the measure of how acidic/basic something is
32
monomer
one of one
33
nucleic acid
store information - the genetic code made up of nucleotide monomers (5 carbon sugar, nitrogen-rich ring compound(base) and phosphate group)
34
ATP
Adenosine triphosphate is a modified nucleotide -3 phosphate group linked together. When the bonds between phosphate groups are broken, energy is released.
35
phosphodiester bond
bond between nucleotides
36
Protein
are made up of monomers of amino acids that are linked by peptide bonds
37
Amino Acids
monomers that makeup proteins, one side free amino group and other side free carboxyl
38
peptide bond
bonds that link together amino acids to make proteins
39
Carbohydrates
made up of sugars (monosaccharides)
40
Monosaccharide
the monomers of carbohydrates
41
isomer
molecules with the same chemical formula but different structures
42
Glycosidic bond
the bond that links monosaccharides that make carbohydrates
43
Condensation reaction
when a water molecule is expelled
44
starch
what glucose is store as in plants
45
cellulose
made of long strands of glucose that provides structural support to plants
46
Glycogen
where glucose is stored in animals
47
Lipid
diverse group of non-polar molecules that are important for energy storage, structure, and signaling
48
Fatty acid
have long, hydrocarbon tail and a carboxyl group (-cooh), which behaves as an acid
49
Amphipathic
Possess both hydrophobic and hydrophilic regions
50
Saturated
no kink in chain
51
unsaturated
kink in the chain due to double bonds
52
Triacylglyceride
have 3 fatty acids joined by a glycerol molecule (small sugar)
53
phospholipids
Aggregate to form the phospholipid bilayer also known as the cell membrane.
54
1st law of thermodynamics
energy cannot be created or destroyed, only converted from one form to another
55
2nd law of thermodynamics
the universe (or any isolated system) is constantly moving towards disorder
56
entropy
the measure of disorder
57
catabolic
pathways break down larger molecules into smaller (polymer to monomer)
58
anabolic
pathways build larger molecules from smaller ones (monomer to polymer)
59
free energy (G)
Useful energy that is dissipated as heat which increases disorder
60
delta G
not constant, can be affected by different things such as the concentration of molecules in the reaction at any time.
61
equilibrium constant
delta g is equal to zero
62
coupled reaction
reactions that are energetically unfavorable can be coupled (linked) to second, energetically favorable reactions.
63
activated carriers
molecules that store energy in an easily exchangeable form, either as readily transferable chemical groups or as readily transferable electrons.
64
catalysis
the acceleration of a chemical reaction
65
activation energy
the minimum quantity of energy which the reacting species must possess in order to undergo a specific reaction.
66
substrate
the specific molecule each enzyme binds to
67
active site
A region on an enzyme that binds to a protein or other substance during a reaction.
68
polypeptide
what they call a chain of amino acids being held together by covalent peptide bonds
69
polypeptide backbone
the repeating sequence of amino acids that make up the core of a polypeptide chain
70
primary structure
amino acid sequence
71
secondary structure
structures that form in certain segments of the AA chain, provide structures
72
tertiary structure
full 3D conformation formed by an entire polypeptide chain
73
quaternary structure
when multiple polypeptides form a single complex
74
alpha helix
spirals. N-H of one AA is H-bonded to the C=O located 4AA away.
75
beta sheets
Form when H-bonds form between parts of the polypeptide chain that lie side by side. Give strength and stability to proteins.
76
coiled-coil
When two or more alpha-helices are wound around each other to form a supercoiled bundle.
77
disulfide bond/bridge
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
protein domain
any segment of a polypeptide chain that can fold independently into a compact, stable structure
79
protein families
proteins with similar sequences and 3D structure
80
prion
are misfolded proteins that cause infectious neurodegenerative diseases to occur.
81
phosphorylation
involves the transfer of a phosphate group from ATP to a hydroxyl group of an AA
82
kinase
what adds phosphates
83
phosphatase
what removes phosphates
84
turnover number
the maximal number of molecules of substrate converted to product per active site per unit time when the enzyme is saturated with substrate.
85
Michaelis constant (Km)
the substrate concentration at which the reaction rate occurs at 0.5 the Vmax
86
competitive inhibitor
mimic substrates and tie up enzymes
87
allosteric inhibitor
a molecule that binds to an enzyme's allosteric site to reduce or prevent the enzyme's activity.
88
feedback inhibition
when an enzyme early in a reaction pathway is inhibited by a late product of the pathway.
89
positive regulation
can also occur where an enzyme's activity is stimulated rather than inhibited.
90
91
centrifugation
removing cell parts, largest to smallest
92
gel electrophoresis
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
chromatography
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
ion exchange chromatography
Separates proteins by charge. often used in purification and quality control
95
anion exchange
uses positively charged beads (to extract negative charged proteins)
96
cation exchange
uses negatively charges resins or beads (to extract positively charged proteins
97
antibody
proteins that protect you when an unwanted substance enters your body
98
antigens
a substance that causes the body to produce an immune response against it
99
affinity chromatogrpahy
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
mass spectrometry
a method to analyze proteins which ionizes small chemicals (like short peptides) and sorts them based on mass-to-charge ratio

cell bio (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions