hapter 5 Instrumental methods of studying proteins 1. Three dimensional structur
ID: 210194 • Letter: H
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hapter 5 Instrumental methods of studying proteins 1. Three dimensional structures of proteins in solid form may be generated using which 2. Three dimensional structures of proteins in solution may be generated using which 3. Locations of proteins in cells may be determined using which method? A) Western 4. In the Edman Method, derivatized amino acids are usually identified using which S. MALDI is an adapted form of: a) NMR b) mass spectrometry c) HPLC d) gel 6. In SDS-PAGE, what does SDS not do? A) unravel proteins b) separate subunits c) 7. In an SDS-PAGE experiment, hemoglobin, myoglobin and cytochrome C are used. method? A) X-ray crystallography b) NMR c) Edman method d) mass spectrometry method? A) X-ray crystallography b) NMR c) Edman method d) mass spectrometry blotting b) ELISA c) fluorescence microscopy d) HPLC method? A) Western blotting b) ELISA c) fluorescence microscopy d) HPLC electrophoresis render all proteins negatively charged d) break proteins into amino acids Myoglobin and cytochrome C are monomeric proteins having molar masses of around 60 Kd. Hemoglobin is a tetrameric protein having 4 subunits, each having a molar mass of around 60 Kd. Hemoglobin and myoglobin have negative charges in pH 7 buffer in the absence of SDS, while cytochrome C has a positive charge. Under SDS-PAGE conditions, one would expect to see: a) cytochrome C traveling towards the cathode, with hemoglobin and myoglobin traveling toward the anode. Myoglobin would travel fastest. B) cytochrome C traveling towards the cathode, with hemoglobin and myoglobin traveling toward the anode. Hemoglobin would travel fastest C) cytochrome C traveling towards the cathode, with hemoglobin and myoglobin traveling toward the anode at about the same rate d) All 3 proteins traveling towards the anode at about the same rate A very sensitive spectrophotometric/fluorimetric method which uses antibodies and is 8. used for measuring concentrations of specific proteins in solution is: a) Western blotting b) ELISA c) reverse fluorimetry d) anion flux densitometry 9. Lys has an isoelectric point around 10, Ala around 5.6 and Asp around 2.7. If a pH 7.0 buffer is used with a cationic, anion exchange column, which amino acid would come off the column first? A) Lys b) Ala c) Asp d) all would travel at the same rate 10. X-Ray Crystallography can only be used when proteins: a) have only 1 subunit b) have only 1 domain c) have a coiled-coil structure d) form crystals Chapter 6. Enzyme Basics Match each item in column A with the best match in column B A. Induced fit B. Active site Binds to active site Unchanged by enzyme-Explanation / Answer
1. A) X- ray crystallography
X Ray crystallography measures the the angles of diffraction, that have come up as a result of incidence of x rays onto the crystal atoms. This diffraction results in production of a 3d structure as the different intensities of angles would be measured. NMR is only used to study the generated 3d structure in solid form and cannot generate a 3d structure.
2. B) NMR
In solutions, the three dimensional structures are generated using nuclear magnetic resonance and the resolution provided by nmr in solution is comparable to the resolution of that seen in x Ray crystallography in the solid form.
3. C) fluorescence microscopy
This is the method where phosphorescence and flourescence is used for studying the properties of inorganic as well as organic substances. In the western blot, only the presence or absence of a protein would be determined and not its locations. In HPLC, separation is done.
4. A) Western blotting
Western Blotting can be used for visualisation of derivatives proteins. Flourescence microscopy only shows the location of the proteins and HPLC is used for separation of proteins.
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