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29 Cards in this Set
- Front
- Back
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Native gel electrophoresis allows researchers to run proteins on a gel without ____ them, retaining their native ___ and ___
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denaturing
structure and activity |
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The native gel does not contain ___, ___ or ___
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SDS
B-Mercaptoethanol stacking gel |
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In a native gel proteins will migrate based on ___ and ___
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size and charge
|
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The buffer used in the native gel generally has a pH of 9 so most proteins will carry a ___ charge and migrate towards the anode.
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negative
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Proteins with high pIs will migrate in the ____ direction towards the negative electrode
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reverse
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The proteins in native gels retain their ___ structure
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tertiary
|
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Sample bands on the native gel are __ than that of the SDS page and ___ to resolve
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thicker
harder |
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Native gel does not allow for accurate determination of ___
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molecular weight
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Native gels can be used to determine the degree of ___ on serines, threonines, and tyrosines
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phosphorylation
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Proteins of different oligomeric states will migrate ___ on a native gel
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differently
(monomers, dimers, trimers, tetramers) |
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A heterodimer in SDS PAGE will migrate as ___ and appear as ___ band(s)
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monomers
two |
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A heterodimer in native gel will migrate as ___ and appear as ___ band(s)
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a dimer
single |
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A trimer would appear ___ a dimer on a native gel
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above
|
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To determine if a protein forms dimers you can fuse a protein to __ and mix it and look on a gel
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GST or MBP
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IF the native protein naturally forms dimers then ___, ___, and ___ will form creating ___ bands
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N:N .. N:N-MBP .. and
N-MBP:N-MBP three |
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SDS could not be used for this because: ______
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The dimers would dissociate
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On an SDS PAGE a heterodimer (two diff. proteins) would appear as ___ band(s), a homodimer (two same proteins) would appear as ____ band(s)
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two
one |
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Pore-limited gel electrophoresis allows for an estimation of ___, the resolving gel is __-__% acrylamide and is poured with no SDS
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molecular weight
3-25% |
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Proteins will migrate until they reach a point at which the pore size is ___ for them to pass, and by including standards you can estimate the Mw
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too small
|
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Isoelectric focusing (IEF) separates proteins based on ___ alone
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charge
|
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Proteins are separated by their ___s
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pI
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A protein will not move in a feild when it has a net ___ charge when the pI is equal to the ___ of a buffer
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neutral
pH |
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A ___ gradient is set up in the IEF gel by the inclusion of vaarious buffers and ampholytes (low Mw zwitterions)
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pH
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During the pre-running phase, each of the ampholytes (which have many positive and negative charges and various pIs) migrate to a position where the ___ = ___ establishing a gradient
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pH = pI
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Two-dimensional gel electrophoresis is a combination of ___ and ___
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IEF and SDS PAGE
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An ___ gel is run first and then the gel is placed horizontally across the top of the stacking gel of a slab of ____
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IEF
SDS PAGE |
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The proteins are first separated by their __ and then by their __ providing outstanding resolution
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pI
Mw |
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2D gel electrophoresis can be used to can be used to compare cells under different ____ states, such as cells at normal vs. high temperatures or normal vs. cancer cells or heart disease cells
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physiological
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You can increase resolution even further by doing 3D gel electrophoresis in which you run a ___, ___, then ___
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native gel
IEF SDS-PAGE |
