Cell Bio 1

Question 1

mass spectrometry

Answer 1

measure mass and determine
unknown chemicals –proteins
often first digested with trypsin

Question 2

x-ray diffraction

Answer 2

uses crystals of purified proteins and destructuretermines up to tertiary

Question 3

NMR spectroscopy

Answer 3

uses crystals of purified proteins and determines up to tertiary

Question 4

Immunoprecipitation

Answer 4

purify proteins from cells, add antibody, secondary antibody linked to beads, incubate, spin down the beads and run out on a gel. This allows protein complexes to be pulled out. Can label proteins ahead of
time or use a Western blot to identify proteins of interest.

Question 5

Immunohistochemistry/ immunofluorescence

Answer 5

(Antibody staining) to look at protein localization in cells – can also see if 2+ proteins co-localize to the same subcellular region of a cell (at “low” resolution).

Question 6

FRAP

fluorescene recovery after photobleaching

Answer 6

optical technique to quantify 2d lateral diffusion useful in studying membrane diffusion and protein binding

Question 7

Michaelis Constant

Answer 7

Km, the [S] (substrate concentration) at 1/2 V

Question 8

Michaelis and Menten equation

Answer 8

V=Vmax [S]/[S] + Km

reciprocal is Lineweaver-Burk plot (lower is better on this plot)

Question 9

competitive inhibitors

Answer 9

reversibly bind to active site and prevent substrate bindin

Question 10

non competitive inhibitors

Answer 10

reversibly bind another site on enzyme and prevent substrate interaction

Question 11

irreverisble inhibitors

Answer 11

covalently bind enzyme and prevent substrate interaction

ex: nerve gas, penicillin

Question 12

enzyme post translational modification

Answer 12

covalent modifications, most common is phosphorylation

causes conformational changes and alters interactions between active site and substrate

Question 13

allosteric enzyme modulation

Answer 13

non covalent interaction with another molecule

occurs outside of active site and causes conformational change in active site

Question 14

light microscopy equation for resolving power

Answer 14

distance = 0.61 wavelength/ refractive index sin alpha

Question 15

fluorescent light microscopy

Answer 15

light is reflected

Question 16

FRET

fluorescent resonance energy transfer

Answer 16

determines how close together in a cell 2 molecules are or follows activation of enzyme in situ (original place)

Question 17

laser scanning confocal microscopy

Answer 17

similar to fluorescent microscopy but uses lasers to light one color and one focal plane at a time

Question 18

scanning electron microscopy

Answer 18

reveals specimen topography

Question 19

transmission electron microscopy

Answer 19

very high res images but potential for artifacts

Question 20

subcellular fractionation

Answer 20

method to study organelles

homogenize cells and centrifuge, transfer and centrifuge to separate out through layers

Question 21

lysosomes

Answer 21

degrades cellular garbage and enzymes active only at pH 4.8

linked to Tay Sachs disease

Question 22

peroxisomes

Answer 22

single membrane, site of degradation of farry acids and toxins and bad oxygen
linked to adrenoleukdystrophy

Question 23

N-glycosidic linkage

Answer 23

attached to asparagine amino acid residue

Question 24

O-glycosidic linkage

Answer 24

attached to oxygen on serine or threonne resides

Question 25

glycoproteins and glycolipids

Answer 25

90% of cells carbohydrates linked to proteins and 10% linked to lipids

Question 26

Blood A type

Answer 26

GalNac to galactose

Question 27

Blood B type

Answer 27

galactose to galactose

Question 28

Blood O type

Answer 28

backbone, a and b add on to with carbohydrates

Question 29

nonionic detergent

Answer 29

a polar head group and nonpolar hydrocarbon chain

Question 30

peripheral membrane proteins

Answer 30

do not enter lipid bilayer, located entirely outside on either side attach via non covalent interactions with polar head groups or integral membrane proteins and dissociate by high salt RBC spectrin is example

Question 31

lipid anchored MP

Answer 31

proteins may be achored to membrane covalent attachment to hydrocarbon fatty acid/lipid covalent attachment to carbohydrates that are attached to phospholipid can be dissociated by enzymes that dissociate inositol-containing phospholipids

Question 32

single particle tracking

Answer 32

monitor protein movement by labeling antibody coated gold particles

Question 33

energy of solute movement for charged molecules

Answer 33

ΔG =(1.4 Kcal/mole) log10[Ci]/[Co] +zFΔEm

Question 34

patch clamping

Answer 34

used to study ion channels by microelectrodes and applying charge to patch of membrane

Question 35

Na+/glucose co transport

Answer 35

2 Na+ move down concentration gradient an 1 glucose moves against, without sodium, glucose would not be able to exit lumen, GLUT transporter then sends into blood

Question 36

dendrites

Answer 36

receive incoming info

Question 37

cell body

Answer 37

nucleus, metabolic hub

Question 38

axon

Answer 38

conducts outgoing impulses

Question 39

node of ranvier

Answer 39

where action potential happens

Question 40

terminal knob

Answer 40

transmits signal to next cell

Question 41

myelin sheath

Answer 41

insulator, speeds conductance

Question 42

phosphoglycerides

Answer 42

diaceylglycerides with small functional head group linked to glycerol backbone by phosphate ester bonds

Question 43

sphingolipids

Answer 43

ceramines formed by attachment of spingosine to fatty acids - rigid

Question 44

cholesterol

Answer 44

smaller and less amphipathic , only found in animals, carbon rings are flat and rigid