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31 Cards in this Set
- Front
- Back
nucleoli
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regions of RNA synthesis
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phase contrast microscope
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zernike, light travel faster or slower 1/4 wavelength than other deflected, creates degrees of brightness
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nucleus
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transcription
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SDS
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sodium dodecyl sulfate-ionic detergent(binds to prot and gives it a negative charge)
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fluorescent compound
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DAPI
4'6 diamido 2 phenylindole |
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nonpolar amino acids
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have C's and H's, SH
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tertiary structure
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3D conformation that results from folding of the polypeptide chain into a shape from hydrophobic and hydrophilic interactions
(ex: globular prots) |
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mercaptoethanol
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reducing agent, denatures protein, reduces the disulfide bonds
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all prots have
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primary and secondary(alpha helix & beta plated sheets)
primary and secondary=1 polypeptide |
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electron beams
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small wavelengths, magnets used to focus the beams
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coiled coil
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amphipathic helix wrapping around another amphipathic helix, form dimers and polymerize, secondary structure
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ionic amino acids
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have an attached part with a - or positive charge
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hydrophobic aa residues within helix are spaced
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alternately 3 or 4 positions apart in the sequence
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higher percentage of agarose gel
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smaller pore size of gel making it better to separate small and shorter particles
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secondary antibody recognizes
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primary antibody coupled w/dye and is where fluorescence is coming from
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mercaptoethanol
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reducing agent(reduces disulfide bonds)
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euk
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cytoskeleton-> basal bodies-> cilium
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primary antibody
secondary antibody |
primary-IgG
secondary-antiIgG |
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SDS
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unfolds the tertiary structure, solubilizes proteins, adds negative charge
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immunofluorescence
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chemicals absorb light at 1 wavelength and emit at longer wavelength and less energy
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axoneme
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a bundle of mts(cilia & flagella)
has 9 pairs of outer mts surrounded by 2 central mts enclosed by a plasma mem |
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electrophoresis
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based on a principle that charged molecules migrate in an electric field and separate charge and size
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denaturing electrophoresis
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prots are denatured w/sodium dodecyl sulfate and have a net negative charge
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indirect binding of secondary to primary antibody
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see specificities of primary antibody
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quaternary
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2 or more indep folded prot chains loosely held together by weak bonds
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antibodies
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prot molecules produced by B cells of vertebrates(immunoglobulins)
bind to foreign entities(antigens) w/high specificity(light and heavy chains) |
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polar amino acids
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have OH groups, NH2 groups
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cytoskeleton
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intermediate filamts
mts--dynein actin--myosin |
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native electrophoresis
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separate proteins in a buffered environmt that maintains native charge and configuration
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axoneme
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bundle of mts; bends due to sliding of mts, this bending moves the cilia
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primary antibody recognizes
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cell specific antigen
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