Study your flashcards anywhere!

Download the official Cram app for free >

  • Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key


Play button


Play button




Click to flip

75 Cards in this Set

  • Front
  • Back
Endosymbiotic Hypothesis
1)anaerobic prokaryote takes in small aerobic prokaryote (3 BYA)
2)aerobic heterotropic prokaryote w/ small prokaryote (eventually mitochondria) (2.5 BYA)
3)plasma membrane invagination (2 BYA)
4)proeukaryotic cell w/ precursors to ER & nuclear envelope
5)protist, fungal, & animal cells
6)photosynthetic cyanobacteria -> algal & plant cells
Structure of Plasma Membrane
Structure of Cell Walls
-carbohydrates (polysaccharides)
Structure of Organelles
-some DNA
Structure of Cytoskeleton
Structure of Ribosomes
Switch between monomers and polymers requires?
condensation & hydrolysis (taking & giving water molecules to form & break bonds)
-triglycerides: glycerol w/ 3 fatty acid hydrophobic tails
-saturated: no double bonds; solid at room temp
-unsaturated: double bonds; liquid at room temp
-steroids: hydrophobic; mostly signaling molecules
Steroid Examples
-leydig cells in testes: cholesterol is converted to testosterone using enzymes & a series of conversions
-granulosa cells in ovaries: cholesterol is converted to estrogen after a series of reactions
Phospholipid Structure
1)polar head (choline & phosphate)
2)glycerol backbone
3)fatty acid chains
Difference Between Beta & Alpha Configurations
-Beta has OH above plane
-Alpha has OH below plane
Glyogen Linkage
alpha (1-4) glycosidic linkage
Starch Linkage
alpha (1-4) glycosidic linkage
Cellulose Linkage
beta (1-4) glycosidic linkage
Polar Amino Acids
lycine, arginine, tyrosine, serine, threonine, glutamine
Non-Polar Amino Acids
leusine, isoleucine, valine, alanine, tryptophan
Side Chains w/ Unique Properties
glycine, cysteine, proline
Primary Protein Structure
-N-terminus -> C-terminus
-Amino Acid Sequence
-synthesis of bonding peptides takes place in the RIBOSOME
Protein Synthesized in?
mitochondria, chloroplast, & cytoplasm
Secondary Protein Structure
-alpha helix: contains hydrophobic AA; hydrogen bonds that can break to change length of coil (1 helix = 3.6 residues)
-beta pleated sheet: alternates hydrophobic & hydrophilic (lysine->leusine); held side by side by hydrogen bonds
-hair pin loops: covalent bonds of disulfide bridge holds parts of structure together (strong bonds)
Tertiary Protein Structure
-3-D folding (Native)
Quaternary Protein Structure
-Protein made up of 2 or more subunits needed together to function properly
Chemical Denaturation
Urea & Mercaptethanol: denatures proteins; some refold but others are permanently deformed
Substrate to Product
(with help of enzyme)
energy is released
Product to Substrate
(requires input of energy from ATP or GTP)
Glucose + ATP ->
Glucose-6-Phosphote + ADP
with help from hexokinase
R-Group determines?
how substrate is oriented in active site
Enzyme Mechanism Image
1)maintain substrate orentation
2)alter substrate ionic structure
3)exert stress on substrate bonds
Enzyme Regulation
1)synthesize & degrade enzyme (not efficient)
2)posy-translation phosphorylation (modify enzyme)
3)presence or absence of cofactor (such as Mg2+ ion)
4)protein allosteric actuator (important in mitosis)
5)PH of cellular compartment (changes charge on enzyme)
6)temperature (changes shape and motion of enzyme)(causes hydrogen bonds of a-helix and b-sheets to break)
Michaelis-Menten Equation
V = Vmax[s/s+km]
Michaelis Constant
km = s; V = Vmax/2
-if value of km is larger, binding affinity is lower
-if value of km is smaller, binding affinity is higher
stick to lipids, proteins, or carbohydrates
make certain things visible under UV light. antitubulin antibodies make tubulin visible with flurochromes
Light Microscope
Magnification: 10x - 1000x
Resolution: 0.2um
(visible, UV, confocal scanning laser microscope)
Magnification: 1000x - 500,000x
Resolution: 0.002um
-if electron goes through = white; if not = black
1)Fix (preserve) specimen using formaldehyde or gluteraldehyde
2)Wash (Buffer) to get rid of excess preservative
3)Dehydrate using increasing concentrations of alcohol or acetone
4)Embed in plastic
5)Harden & Trim excess plastic
6)Section using ultramicrotome w/ diamond knife
7)Stain with heavy metal
8)Put into TEM
1)Fix (preserve) specimen using formaldehyde or gluteraldehyde
2)Wash (Buffer) to get rid of excess preservative
3)Critical Point Dry (freeze dry) sublimation: gas to solid
4)Coat with heavy metal
5)Put in SEM
1)Culture medium with radioactive monomer of what you are looking for
5)embed in plastic & trim
7)dip slides into radiation sensitive emulsion in dark room
8)place in dark box to develop until ready for use
-silver grains show up light on film to see if cell was making what you are looking for
-Protein: Leucine
-DNA: Thyamine
-RNA: Uracil
Protein Biochemistry/Enzymology
1)homogenize (in ice to prevent denaturation)
2)pour homogenate into 2 tubes
3)centrifuge to get pellet & supernatant
Sucrose Gradient Centrifugation
-centrifuge seperates by size
-in order to seperate components of smae size u need to seperate by density
SDS-Polyacrylamide Gel Electrophoresis
1)dissolve protein in SDS buffer (has a negative charge & coats protein with negative charge)
2)Heat protein sample to denature
3)Pour gel between glass plates
4)Gel Polymerizes from gel to liquid
5)Load sample and MW markers into reservoirs
6)Electrophoresis protein
7)observe MW (heavier at top lighter at bottom)
Plasma Membrane Composition
Lipid: 35-40%
Protein: 45-55%
Carbs: 2-10%
Plasma Membrane Function
-selective permeability
-transport in/out of the cell
-link cytoplasm to ECM
-Enzyme Linked / Receptor Linked
Integral Proteins
-extracullular domain (polar r-group)
-transmembrane domain (hydrophobic a-helix 12-14 AA)
-cytoplasmic domain (polar r-group)
several sugars
Blood Group Antigens
-A, B, AB, O
-have same 5 sugars and membrane lipids & protein
-differ in terminal sugar
-AB can receive any blood, O only O (can't have foreign material)
Fluorescence Recovery After Photobleaching
1)Stain protein with antibody (red fluorochrome)
2)Wash away unbound antibody
3)select target area
4)"Zap" with a soft laser
5)Bleaches Flurochrome antibody from red to no color
6)observe with UV microscope
7)Recovery (do colored proteins move back into uncolored space)
Allosteric Inhibitor
changes the shape of an enzyme
Negative Feedback
end product of reaction goes to feedback site to stop production (auto regulation)
Pellet Containing Nuclei & Unbroken cells
800g for 10 min (gives postnuclear supernatant)
Pellet containing mitochondria, lysosomes, & microbodies
12,000g for 20 min (gives postmitochondrial supernatant)
Pellet containing microsomes (small fragments of membranes)
50,000g for 2 hrs (give postmicrosomal supernatant)
Pellet containing ribosomes
300,000g for 3 hrs (gives postribosomal supernatant)
Sucrose Gradient Centrifugation
sucrose density gradient with sample at 65,000 for 2 hrs
1)Lysosomes (1.12 g/mol)
2)Mitochondria (1.18 g/mol)
3)Microbodies (1.23 g/mol)
mass of one hydrogen atom
Use to find MW after SDS-PAGE
Log graph of weight v. distance
Most Abundant Phospholipids
1)Phosphatidic Acid
-PC most abundant facing outward
-PS most abundant facoing inward
lateral movement of proteins and phospholipids in PM. changes shape of membrane (flip-flop takes a lot longer)
N-Linked glycosylation
takes place in Lumen of RER then goes to plasma membrane
O-Linked glycosylation
takes place in Golgi Apparatus
(Serine or Threonine)
Non-ionic detergents
solubilize membrane proteins without disrupting their structure
Identifying Transmembrane Domains
-adding trypsin to intact cell takes off part of protein in ECM
-adding trypsin to permeabilized cell takes off part of protein in cytoplasm
-SDS-PAGE allows us to see the effects of each piece of protein removed (does move down a lot in gel?)
creates a border & fences in some free moving integral proteins
How can you tell if glucose transport is moving in membrane?
-find antibody specific to that protein
-FRAP analysis -> lateral movement (restricted to apical surface of PM)
Carrier Mediated
channel has to change its shape
into cell
out of cell
Non-Mediated Channel
does not have to change shape
Active Transport
ATP used to pump against gradient
channel open to cytoplasm & closed to EC space
channel open to EC Space & closed to cytoplasm
Steps of Na+/K+ ATPase transport
1)3 sodium ions enter channel and bind to binding sites
2)ATP is hydrolyzed (supplies 7kCal of energy) & phosphate is transfered to protein
3)Conformation changes from E1 to E2
4)Sodium leaves and Potassium enters the channel & attaches to binding sites
5)Phosphate is lost
6)Channel returns from E2 to E1
7)Potassium enters the cell
(3 Na+ out & 2 K+ in creates a -70mV charge inside the cell
Inside = 10mM Na; 100mM K
Outside = 100mM Na; 10mM K
Cystic Fibrosis
thick mucous coats lungs where bacteria grows which complicates breathing (also effects pancreas, seminiferous tubules, and fillopian tubes)
Healthy Person's Lungs
1)cAMP opens active site of PKA
2)Protein Kinase A puts phosphate on 4 serines which pulls the R-group away from the channel (requires 4 ATP)
3)ATP binds to Nucleotide Binding Domain 1 & 2 to move channel open laterally
4)Cl- moves through channel
5)H2O follows and dilutes mucous to get rid of it easier
6)Phosphatase removes phosphates and channel closes again
-If channel doesn't open all the way?
-If channel doesn't open at all?
-V-max is lowered
-problem with NBD 1 or 2 (no lateral opening)