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17.1 quiz#1

Terms

undefined, object
copy deck
nucleoli
regions of RNA synthesis
phase contrast microscope
zernike, light travel faster or slower 1/4 wavelength than other deflected, creates degrees of brightness
nucleus
transcription
SDS
unfolds the tertiary structure, solubilizes proteins, adds negative charge
fluorescent compound
DAPI
4'6 diamido 2 phenylindole
nonpolar amino acids
have C's and H's, SH
tertiary structure
3D conformation that results from folding of the polypeptide chain into a shape from hydrophobic and hydrophilic interactions
(ex: globular prots)
mercaptoethanol
reducing agent(reduces disulfide bonds)
all prots have
primary and secondary(alpha helix & beta plated sheets)

primary and secondary=1 polypeptide
electron beams
small wavelengths, magnets used to focus the beams
coiled coil
amphipathic helix wrapping around another amphipathic helix, form dimers and polymerize, secondary structure
ionic amino acids
have an attached part with a - or positive charge
hydrophobic aa residues within helix are spaced
alternately 3 or 4 positions apart in the sequence
higher percentage of agarose gel
smaller pore size of gel making it better to separate small and shorter particles
secondary antibody recognizes
primary antibody coupled w/dye and is where fluorescence is coming from
euk
cytoskeleton-> basal bodies-> cilium
primary antibody

secondary antibody
primary-IgG

secondary-antiIgG
immunofluorescence
chemicals absorb light at 1 wavelength and emit at longer wavelength and less energy
axoneme
bundle of mts; bends due to sliding of mts, this bending moves the cilia
electrophoresis
based on a principle that charged molecules migrate in an electric field and separate charge and size
denaturing electrophoresis
prots are denatured w/sodium dodecyl sulfate and have a net negative charge
indirect binding of secondary to primary antibody
see specificities of primary antibody
quaternary
2 or more indep folded prot chains loosely held together by weak bonds
antibodies
prot molecules produced by B cells of vertebrates(immunoglobulins)
bind to foreign entities(antigens) w/high specificity(light and heavy chains)
polar amino acids
have OH groups, NH2 groups
cytoskeleton
intermediate filamts
mts--dynein
actin--myosin
native electrophoresis
separate proteins in a buffered environmt that maintains native charge and configuration
primary antibody recognizes
cell specific antigen

Deck Info

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