Cell Biology

Front 1

Homotypic Adhesion

Back 1

two or more same proteins interacting with each other

Front 2

Adherin (protein)

Back 2

Without calcium- floppy, loose
With calcium- rigid, straight, won't pull apart with calcium

link through side chain tryptophan (amino acid)

Front 3

Caveolin/ Caveola (protein)

Back 3

help form vesicles from cell membrane

Front 4

4 essential elements

Back 4

Carbon, Hydrogen, Oxygen, Nitrogen

others: phosphorus, silicon, sulfur

Front 5

Bonds

Back 5

Strongest-Weakest bonds
1. Covalent
2. Ionic
3. Hydrogen
4. Van Der Waals Interactions
5. Hydrophobic/ Hydrophilic Interactions

Front 6

Phosphorylation

Back 6

Kinases adding phosphates

Front 7

Phosphatases

Back 7

subtract phosphates

Front 8

Post Translational Modification

Back 8

Phosphorylation
Gylosylation (adding of sugars)
- O-linked glycosylation is when sugar is added onto oxygen on amino acid side chains
-N-linked when sugar is added onto nitrogen on amino acid side chain

Front 9

Cadherin

Back 9

dominated by beta sheets

Front 10

resolution

Back 10

0.61*wavelength (slide like symbol) / n * sin x

n=refractive index

Front 11

Myosin/Actin interactions

Back 11

result in a phosphate being released when myosin attacks

Front 12

Negative amino acids

Back 12

Aspartic Acid: Asp
Glutamic Acid: Glu

*Acidic

Front 13

Positive amino acids

Back 13

Arginine: Arg
Lysine: Lys
Histidine: His

*Basic

Front 14

Hydrophobic Interactions (non-polar) Actin/Myosin/Amino Acids

Back 14

Actin: Ala, Ile
Myosin: Met, Pro, Phe, Pi-e?

Front 15

Ionic Actin/Myosin/Amino Acids

Back 15

Actin: Asp, Glu (all negative)
Myosin: Arg, Lys, His (all positive)

Front 16

Enzymes

Back 16

Kinases- phosphorylation- add on phosphates

Phosphatase- removes phosphates

Proteases- breaks down proteins

Nucleases: break down nucleic acids

Front 17

Polyclonal

Back 17

Antibodies from many different B cells

Front 18

Monoclonal

Back 18

antibody from one B cell

Front 19

Immunoprecipitation

Back 19

use of antibodies to precipitate other proteins in mixtures by bonding to them

Front 20

Know what peptide bond looks like

Back 20

in notes

Front 21

dsRNA

Back 21

eliminates proteins
cell thinks dsRNA is a virus because it is double stranded

Front 22

Membrane Principles

Back 22

- continuous
- semi-permeable
- fluid
- assymmetry

Front 23

Phospholipids

Back 23

Heads- hydrophilic
Tails- hydrophobic

Front 24

Cholesterol (sterol)

Back 24

stabilizes membrane
between phospholipids

Front 25

RBC's

Back 25

Model for understanding the plasma membrane

Front 26

Lipid Raft

Back 26

affiliated frequently with caveolin

Front 27

Enzyme Characteristics

Back 27

- can be proteins or RNAs
- have active site which binds to substrate
- accelerate reactions by lowering activation energy

Reactions
1. binding of substrate rearranges electrons in the substrate, creating partial negative and positive charge that favor a reaction
2. enzyme binds to two substrate molecules and orients them precisely to encourage a reaction
3. Enzyme strains the bound substrate molecules, forcing it toward a transition state to favor a reaction

Front 28

Lysomal Enzymes

Back 28

Nucleases: DNase, RNase

Front 29

Negative/Postive Feedback

Back 29

Negative- enzyme turned off

Positive: addition of ADP molecule to substrate

Front 30

Allosteric Regulation

Back 30

Addition of sugar+ADP which activates enzyme

Front 31

CTP

Back 31

inactivates enzymes

Front 32

Breaking Cells and Tissues

Back 32

- with high frequency
- detergent (breaks down lipids and creates holes in membrane)
-force cells through small hole using high pressure
-close fitting rotating plunger and the thick walls of a glass vessel

Front 33

Phospholipids Structure/Charges

Back 33

Charges- see notebook

Head

top- Choline (+)
middle- Phosphate (-)
bottom- glycerol (neutral)

Tails

Crooked tail- unsaturated fatty acid tail (has double bonds)

Straight tail- saturated fatty acid tail (no double bonds)

Front 34

Junctions in membrane

Back 34

restrict membrane protein motility

Front 35

Hypotonic, Hypertonic, Isotonic

Back 35

hypotonic- more salt inside than outside cell
- water moves in to equal ion concentration
-cell swells

hypertonic- more salt outside cell than inside
-water moves out to equal ion concentration
-cell shrinks

Isotonic- normal and equal concentration inside and outside cell

Front 36

Flourescence Microscopy

Back 36

Red- Actin
Blue- DNA (chromosomes)
Green- Microtubules

Front 37

Membrane Proteins

Back 37

Majority have transmembrane alpha helix domains, but a beta barrel can also serve as a transmembrane structure

Front 38

Restriction of membrane protein mobility can be caused by:

Back 38

1. linkage with the cytoskeleton
2. linkage with a extracellular matrix
3. linkage via cell to cell adhesion
4. junction based restrictions of apical (top) and basolateral (bottom+side) membrane domains

Front 39

Transport Across Membrane

Back 39

Small Hydrophobic Molecules (O2, CO2, N2, benzene)- YES

Small Uncharged Polar Molecules (H20, glycerol, ethanol)- YES

Larger Uncharged Polar Molecules (amino acids, glucose, nucleotides)- NO

Ions (H+, Na+, HCO3-, K+, CA2+, Cl-, Mg2+)- NO

Front 40

Low concentration of solute outside cell and high concentration of solute inside cell...

Back 40

results in water flowing into cell through osmosis swelling and bursting the cell (Hypotonic)

Cells deal with this...

Animal cells- send ions out of cell

Plant cells- have central vacuole to pump out water and has a cell wall

Protozoan- has discharging contractile vacuole

Front 41

Channel Protein

Back 41

requires no energy (passive transport)

Front 42

Transporter Protein

Back 42

requires energy like ATP (active transport)

Front 43

Diffusion

Back 43

molecule passes through membrane (passive transport)

Front 44

Potassium Sodium

Back 44

in slide show Lecture 13

Front 45

Uniport

Back 45

transports one molecule into cell

Front 46

Symport

Back 46

transports two molecules into cell at the same time
- coupled transport

Front 47

Antiport

Back 47

Transports one molecule into cell and one molecule to the outside
-coupled transport

Front 48

Coupled Transporter

Back 48

transports 3 molecules into cell and 1 outside

Front 49

ATP driven pump

Back 49

uses ATP molecule to transport molecule outside cell

Front 50

Light Driven Pump

Back 50

Light drives and provides energy for the transportation of a molecule to outside the cell

Front 51

Rate of Transport of Diffusion

Back 51

constant rate

Front 52

Rate of transport-mediated diffusion

Back 52

rate rises exponentially

Front 53

Aquaporins

Back 53

water channels

Front 54

Patch Clampings

Back 54

easy way to study channel function