Final Exam Review from list Flashcards

1
Q

L1: what elements are most common in living organisms

A

HONC

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2
Q

L1: what is an electron, neutron and proton? how do they affect an element

A

electron- +1 charge, in nucleus, ID element mass

Neutron- no charge, in nucleus, give isotope mass

electron= -1 charge, in cloud, charge bonding

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3
Q

L1: what is mass number and atomic number

A

mass number is weight, proton and neutrons

atomic number is how it’s IDed how many protons

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4
Q

L1: characteristics of alpha, beta, gamma radiation

A

alpha: helium nucleus change atomic mass by 4 and atomic # by 2, penetrate top skin layer
beta: nuclear electron, atomic number +1 , sub-cutaneous
gamma: photon- energy wave, no effect on numbers, penetrate deep

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5
Q

L1: Isotopes vs elements

A

isotopes are different forms of the same element different number of neutrons. Only mass changes

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6
Q

L1: Radioactive Particles include

A

alpha, beta gamma

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7
Q

L2: Bohr Model - Absorption, Excitation, Relaxation, Fluorescence

A

absorption-
excitation -
relaxation -
fluorescence -

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8
Q

L2: Quantum Model – Orbitals and how they are organized

A

orbital: location and wave-like behavior of electrons

shell, subshell, orbital

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9
Q

L2: shell, subshell and orbital

A

shell: pathway followed by electrons around an atom’s nucleus ex. the 1st, 2nd, 3rd, 4th,etc shell(everything inside)
subshell: pathway in which an electron moves within a shell ex. s,p,d,f
orbital: describe wave-like behavior of an electron. ex. 1,3,5,7

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10
Q

L2: Electron configurations

A

where electrons go:

SPDF

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11
Q

L2: periodicity - electronegativity and atomic radius trends

A

electronegativity trend: right top is highest

atomic radius trend: left bottom

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12
Q

L2: valence shell and octet rule

A

valence shell: outer most shell that contains electrons

octet rule: elements are most stable when they fill their outermost S and P subshell

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13
Q

L2: Lewis dot structure

A

how many electrons in outer most shell and draw dots either 8 or less

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14
Q

L3: Ions – Anion vs Cation, from which rows in the periodic table?

A

cation: ion with pos. charge, gave up electron. first 3 rows
anion: ion with neg. charge, took electron last 3-4 rows

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15
Q

L3: Covalent Bonds – Polar vs Non Polar.

How many bonds does H, O, N, C want?

A
polar: share bonds, one wants it more
non-polar: share bonds, both want it the same amount
H: wants 2 bonds
o: wants 2 bonds
N: wants 3 bonds
C:  wants 4 bonds
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16
Q

L3: Electronegativity (Ionic, Polar, Non-Polar, how does HONC relate to this?

A

How bad element wants to steal or give away their electrons. Non-polar equal sharing. Polar- unequal sharing. Ionic: take/give up electron. - O>N>C=H +

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17
Q

L3: Single, Double, Triple bond shapes and properties

A

single: tetrahedral and freely rotate
double: trigonal planar, can’t rotate
triple: linear, can’t rotate

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18
Q

L3: How and why do chemical reactions occur?

A

when chemical bonds between atoms are being broken or formed

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19
Q

L3: What does equilibrium mean? What is K? What is G?

A
equal rates forward and backwards, equal energy 
add reactant =forward, 
add product = reverse, 
remove reactant = reverse. 
remove product = forward
K= rate of reaction  
G = 0 energy used
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20
Q

L4: what bonds are weak bonds

A

Hydrogen and VDW and Ionic

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21
Q

L4: Ionic when in water what happens to the charge, strength, etc.

A

Ionic bonds: electron is taken, in water, bond is weak, breaks and h2o surrounds it. still has partial charges

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22
Q

L4: Hydrogen bonds define

A

h-bonds: partial charges of a neg. and pos. attract

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23
Q

L4: Van Der Walls define and who bonds together

A

VDW: temporary attraction when long chains are by each other and the electron is close to outside element, the other side is partial neg. and when the electron goes to the other side, they swap positions

nonpolar weak bonds, induced

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24
Q

L5: Why is water so special?

A

float when solid, H bonding

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25
L5: Cohesion
water w/ water - hydrogen bonds
26
L5: Adhesion
water w/polar substance- hydrogen bond
27
L5: what is specific heat
``` cal = 1 gram raised 1 degree C cal = g x temp change ```
28
L5: % solution
= g solute/100 mL solution
29
L5: What is a mole?
unit of measurement ex. a dozen = 12 eggs
30
L5: Molar solution
mole solute/ L solution
31
L6: How to calculate pH
pH = -log [H+]
32
L6: How to calculate pOH
pOH- = -log [pH-]
33
L6: pH and pOH together is equal to what number? What equation
pH + pOH- = 14 | [H+] x [OH-] = 1 x 10^ -14
34
L6: Buffer
resists change | HA(weak acid) dissociates H+(proton) and A-(conjugate base)
35
L7: what is an isomer
same molecular formula, different structure
36
L7: difference of Structural, Geometric, Enantiomers, Diastereomers isomers
Structural: same molecular formula, different pattern of bonds, atoms connected in different order Geometric: same molecular formula, same bond pattern, different spatial arrangement around a double bond (cis or trans) Enantiomer: mirroring the bonds from the two Diastereomer: mixture of same bond and mirrored bonds
37
L8: Alkyl structure,
``` H I R-C-R Non-polar I H ```
38
L8: sulfhydryl structure,
R-S-H
39
L8: hydroxyl structure,
R- O-H
40
L8: carbonyl structure
.. O .. II R-C-R
41
L8: carboxyl structure,
.. H .. II R-C-OH
42
L8: phosphate structure,
``` ...... O ... .... I R-O-P-OH Acidic, polar ionic ........ I ...... OH ```
43
L8: amino structure
... H ... I R-N-H
44
L8: Polysaccharide monomer and bond name
monosaccharides and Glycosidic
45
L8: Protein monomer and bond name
Amino acids and peptide
46
L8: Nucleic Acid monomer and bond name
nucleotides and phosphodiester
47
L8: lipids monomer and bond name
fatty acid and glycerol, and ester
48
L8: condensation is when what happens
when a bond forms and water is a byproduct
49
L8: hydrolysis is when what happens
water used to break bonds, put back in
50
L9: Names3 types of Monosaccharides
Fructose galactose ribose/deoxyribose
51
L9: Names/types of Disaccharides
Maltose=glucose + glucose sucrose=glucose + fructose lactose=glucose + galactose
52
L9: define of Oligosaccharides and function
sugars of 3-40 monomers, many different simple sugars, highly branched cell recognition/signaling and cell defense
53
L9: Names/types of Polysaccharides animals/plants
starch(plants), glycogen(animals), cellulose(plants), chitin(insects)
54
L9: Chemistry name for a mono saccharides
glucose
55
L9: Functional Groups common to carbs.
hydroxyl and carbonyl
56
L9: What are the monomers, polymers, bond between monomers, functional groups used. of carbs
two or more monosaccharides held together by glycosidic bond from condensation between hydroxyl and hydroxyl
57
L9: Alpha 1-4, alpha 1-6, beta 1-4: structure, polymers, plants vs. animals
storage--> alpha-monomers structural --> beta monomers storage: plants --> 1) amylose alpha 1-4 helical. 2) amylopectin: alpha 1-4 helical and alpha 1-6 branched. 3) animal --> glycogen: a1-4 helical and a1-6 branched structural: plants --> 1) cellulose: b1-4 lines (wood). animals --> 2) chitin b1-4 lines (exoskeleton)
58
L10: functional groups common to fats
carboxyl and hydroxyl
59
L10: What are the monomers, polymers, bond between monomers of fats
polymer: lipid monomer: fatty acid& glycerol bond: ester
60
``` L10: Differences between saturated/unsaturated. state at room temp where comes from structure bonding ```
``` saturated: solid room temp from animals structure- linear max hydrogen bonds and no double bonds ``` ``` unsaturated: liquid room temp 1 or more double bonds double bond replace 2 hydrogen crocked if cis/ straight across if trans, in plants ```
61
L10: What is a phospholipid?
2 fatty acids (hydroxyl) tails and phosphate (polar head) | create bilayer
62
L10: What makes a fat more liquid vs. solid?
bonding, if there are max hydrogen bonds it's solid, if there are bonds missing or double, liquid
63
L11: Functional Groups common to nucleic acids.
Hydroxyl and Phosphate
64
L11: monomer, polymer and bond between monomer of nucleic acids
polymer: nucleic acids monomer: nucleotides bond: phosphodiester
65
L11: Differences between DNA and RNA
DNA: nucleus, long term info storage, double stranded RNA: in cytosol, short term info(messenger), single strand, protein synthesis
66
L11: Purine vs Pyrimidine
purine: two ringed | pyrimidine 1 ring
67
L11: Central Dogma - DNA to RNA to Protein
DNA split, RNA comes in and reads a little bit and takes out of nucleus and give to ribosomes. Ribosomes translate to protein
68
L12: Functional Groups common to amino acids.
amino and carboxyl
69
L12: What are the monomers, polymers, bond between monomers to amino acids
monomer: amino acid polymer: protein bond: peptide
70
L12: Primary, Secondary, Tertiary, Quaternary
Primary: amino acid sequence Secondary: Hydrogen backbone, helices or sheets Tertiary: bonds rest of the molecule, 3D structure Quaternary: associated with 2 or more folded peptides into a protein
71
L12: What does denaturation do? 4 things
break all weak bonds don't break covalent bonds secondary, tertiary and quaternary heat, detergent, strong acid/strong base
72
L13: What makes up a plasma membrane? Asymmetric why?
lipids and proteins, phospholipid bilayer. asymmetric because lipids from the top can't 180 and go to the bottom both sides of the phospholipid are different from each other
73
L13: Types of proteins and oligosaccharides on the plasma membrane
transmembrane integral peripheral lipid anchored protein Glycolipids and glycoprotein
74
L13: FRAP and Hybridomas
FRAP: a cell was coated in a fluorescent color and a part of the cell was bleached. Waited to see if the bleach separated Hybridomas: part of a human cell (colored) and part of a mouse cell (colored) and waited to see if the color mingled together
75
L13: How do plants and animals govern membrane fluidity?
plants: chain/tail length cis unsaturated/ saturated animals: cholesterol "fluidity buffer" regulate internal temp
76
L14: What is part of the endomembrane system? 7 organelles
nucleus, RER, SER, Golgi, Lysosome, Plasma Membrane, Vacuole
77
L14: Structure and function of the organelles
nucleus: holds DNA RER: Protein synthesis SER: phospholipid synthesis Golgi: receive, ships, processes protein and lipids and exports Lysosome: break down macromolecules, hydrolases Plasma Membrane: outer cell membrane Vacuole: unique to plant cells
78
L14: Differences between animals and plants?
plant: double membrane, chloroplast, thylakoid, DNA floating around animal: 1 membrane, dna in nucleus,
79
L15: Semi-autonomous organelles?
organelles with DNA, plant and animals
80
L15: Structure and function of peroxisome, mitochondria, chloroplasts
peroxisome: single membrane w/ crystalline core. detox, get rid of Oxygen and oxidizes large fatty acids mitochondria: powerhouse of cell, make ATP, double membrane, matrix and circular DNA chloroplasts: solar powerhouse, triple membrane, thylakoid and circular DNA
81
L15: Structure and function of microtubules, actin filaments, intermediate filaments
microtubules: tube, chromosome separation, cell motility (part of cell move but not whole) actin filaments: 2 stranded rope, cell division, cell movement and muscle contraction intermediate filaments: cable/rope(bungee cord) resist pulling forces, give nucleus its shape, connect skin cells
82
L16: Difference between prokaryotes and eukaryotes
prokaryotes: bacteria, no nucleus (nucleoid) eukaryotes: animal/plants, circular DNA
83
L16: Difference between bacteria and archaea
Bacteria contain peptidoglycan in the cell wall; archaea do not
84
L16: Difference between gram+ and gram-
gram+ thick layer of peptidoglycan, protect cell gram- thin peptidoglycan layer, less protection
85
L16: Define the 3 types of DNA sharing
transformation: eats a plasmid transduction: bacteriophage lands on bacteria, abducts some bacteria DNA, breaking the og DNA, some of the OG DNA gets sent off and gives it to a diff. bacteria conjugation: attach bacteria together sex pili and transfer plasmid
86
L17: Structure and types of viruses
Structure genome: composed of nucleic acids, sd dna, ds dna, ss rna, ds rna protein coat: called capsid, package and protect genomic material viral envelope: outer membrane of phospholipids and proteins, stolen from host, still has viral glycoproteins accessories:proteins essential for viral life cycle not all viruses need help virus carry out job allows virus to do things host can't do
87
L17: Stages of Lysogenic and Lytic
Lytic: 1. attachment 2. entry 3. synthesis 4. assembly 5. release Lysogenic: 1. attachment 2. entry 3. integration 4. activation 5. synthesis 6. assembly 7. release
88
L17: How does a vaccine work?
destroy virus part of virus can't give you the illness vaccines are preventative doesn't cure it
89
L18: Anabolic vs. Catabolic
Anabolic: building something up Catabolic: a catastrophe breaking down
90
L18: Potential vs. Kinetic
Potential energy is the stored energy | Kinetic energy is the energy of an object or a system's particles in motion
91
L18: Define 1st and 2nd laws of thermodynamics using enthalpy, entropy, and free energy.
1. energy is never created or destroyed 2. entropy(chaos) of the universe is always increasing * *no energy transfer is 100% efficient enthalpy: total potential energy entropy: energy/heat lost during reaction free energy: energy available to do work useful energy
92
L18: Delta G >0; <0; =0
``` ΔG >0:requires energy endergonic-takes energy non-spontaneous = must be forced to happen ΔG <0:give off energy exergonic- releases energy spontaneous- naturally happens ΔG =0: reaction is at equilibrium ```
93
L18: How can you get a non-spontaneous reaction to become spontaneous?
1. change temp 2. add reactants remove products 3. couple endergonic with an exergonic reaction
94
L19: Energy of Activation?
energy needed to go 'over the hump'/ strain and pull chemical bonds before being broken an formed into new and release energy
95
L19: How can you change reaction kinetics/rate?
add catalyst add reactant remove product change temp
96
L19: How can you regulate an enzyme?
phosphorylation temp pH cofactor/coenzyme
97
L19: How can you inhibit or activate and enzyme? Competitive, Non-Competitive, Feedback
Competitive inhibition: blocks active site Non-competitive regulation: dont touch active site if open and an enzyme attaches to it (not in the active site) it will become inactive BUT if active site is closed and an enzymes attaches to it (not active site) it will become active Feedback regulation: if an substrate somewhere in the line comes and binds to the enzyme if attach to active site its called competitive if attach to nonactive site it's called non-competitive
98
L20: Redox; OilRig
reduction oxidation oxidation is loses electrons reduction is gaining electrons
99
L21: Where does glycolysis happen?
cytosol
100
L21: What goes in and what comes out glycolysis?
``` in:1 glucose 2 ATP 2 Pi 4 ADP 2 NAD+ ``` out: 2 Pyruvate 2 ADP 2 NADH 2 H2O
101
L21: Where does fermentation happen?
cytosol
102
L21: What goes in and what comes out fermentation?
in: pyruvate and NADH out: Lactate or ethanol and co2 NAD+
103
L21: What is anaerobic vs aerobic? Why would a cell use one or the other?
anaerobic: no oxygen produce energy without the presence of oxygen aerobic: has oxygen, energy can continue to other parts of the cell respiration
104
L21: PFK?
phosphofructokinase (PFK) is negatively inhibited by ATP and citrate and positively regulated by ADP.
105
L22: Where are Pyruvate bridge, Citric Acid Cycle, Beta Oxidation, electron transport chain
Pyruvate bridge: mitochondria Citric Acid Cycle: matrix Beta Oxidation: mitochondria electron transport chain: inner membrane mitochondria
106
L22: what goes in and out of Pyruvate bridge, Citric Acid Cycle, Beta Oxidation, deamination…
Pyruvate bridge: in: pyruvate NAD+ CoA out: Acetyl-CoA NADH CO2 Citric Acid Cycle: in:1Acetyl-CoA 3 NAD+ 1 FAD 1 ADP+Pi ``` out:2 CO2 3 NADH 1 FADH2 1 ATP 1 CoA ``` Beta Oxidation: in: NAD+ and FAD out:NADH and fADH2 ``` electron transport chain: in: NADH FADH2 O2 H+ Pi and ADP ``` out: H2O ATP NAD+ FAD
107
L22: what is deamination
Lysosome through hydrolases will break down protein to amino acids Remove amino, left with hydroxyl, Put in kreb cycle based on number of carbons
108
L23: Where and how are NADH and FADH2 used?
NADH goes to complex 1 | FADH2 goes to complex 2
109
L23: What is the role of Complex 1, 2, 3, 4?
transfer electrons
110
L23: What does oxygen do?
take H+ and make water
111
L23: What does the ATP synthase do?
turbine, brings H+ to the inside of matrix and create ATP
112
L24: What is absorption? Where is light absorbed in photosynthesis?
def: process in which light is absorbed and converted into energy chloroplast
113
L24: Where do the light reactions happen?
thylakoid
114
L24: What goes in and what comes out?
In:H2o NADP+ light ADP +Pi Out: NADPH O2 H+ ATP
115
L24: What are pigments and photosystems?
pigment: light capturing molecule photosystem: gather light, collect energy and pass through complex structure that can collect light and pass that energy alone in excited electrons
116
L24: What types are light are the best and which are the worst for photosynthesis?
best: purple, red and blue worst: green
117
L25: Where does the Calvin Cycle happen?
stroma
118
L25: What goes in and what comes out?
``` In: 3 RuBP 3 Co2 9 ATP 6 NADPH ``` ``` Out: 3 RuBP 1 G3P 9 ADP 6 NADP+ ```
119
L25: What are the 3 phases?
Fixation: add CO2, enzyme RuBP Reduction: Add phosphates, something is gaining electrons Regeneration: Fix NADH, ATP imbalances
120
L25: What is cyclic electron flow?
when electrons are backed up and FD goes back to PQ and creates a circuit
121
L26: Diffusion vs. Osmosis
diffusion: movement of particles so that they spread out into avaible space try to go to equilibrium osmosis: Diffusion(movement of particles so that they spread out into avaible space) of water
122
L26: What is an electrochemical gradient?
measure of the free energy available to carry out the useful work of transporting the molecule across the membrane
123
L26: Hypo, hyper, iso osmotic
Hypoosmotic: lower solute concentration hyperosmotic: higher solute concentration isosmotic: equal solute concentration
124
L26: Hypo, hyper, iso tonic
Hypotonic: cell swells hypertonic: cell shrinks *raisin* isotonic: no change in cell
125
L27: Differences between active and passive transport? Energy and gradients
energy required: active up/with the gradient [low] --> [high] no energy required: passive down/against the gradient [high] --> [low]
126
L27: 3 types of passive transport
Simple diffusion – movement of small or lipophilic molecules Osmosis – movement of water molecules Facilitated diffusion – movement of large or charged molecules via membrane proteins
127
L27: 3 types of active and what they do
``` Primary active transport: "pump" directly uses ATP [low]-->[high] (against gradient) type of carrier 2 kinds (uniport and cotransport) ``` secondary active transport: gradients move 2 molecules at once(antiport, symport) electron driven transport:
128
L27: 3Na+/2K+ Pump and steps
1. 3 na+ bind to intracellular die of pump 2. ATP add phosphate to pump 3. Conformational shift (flip to outside/other side) 4. 3 Na+ go outside 5. 2 K+ bind to extracellular side of pump 6. phosphate removed 7. conformational shift (flip to inside) 8. 2 K+ go inside 9. repeat
129
L28: Difference between endocytosis and exocytosis
endo: into cell exo: out of cell
130
L28: 4 different types of vesicle transport
phagocytosis: eat cell pinocytosis: drink cell receptor mediated endocytosis: picky eater in cell receptor= bind specific molecule exocytosis: exit/out cell
131
L29: 3 stages of cell signaling
reception, transduction, response
132
L29: 5 types of cell signaling and their characteristics
gap function: direction connection of 2 cell cytoplasm very short range very specific cell to cell: direct contact of 2 cells very short range and very specific synaptic transmission: neuron releasing signal onto another cell short/ long range specific paracrine: signaling to nearby cells medium range general endocrine: signaling to cell far away using the blood stream long range general
133
L29: What does a Kd tell you about a ligand receptor interaction?
how tightly ligand binds to receptor
134
L29: Why do only certain cells respond to a signal?
a cell has to have the right receptor for that signal