961. Which of the following is an example of tertiary structure in a protein?
A. A multimeric protein
B. An a-helix
C. A P-pleated sheet
D. A globular domain

962. The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce:
A. Val-Lys + Glu-Met-Ser + Trp-Arg-Ala
B. Val-Lys-Glu-Met-Ser-Trp + Arg-Ala
C. Val-Lys-Glu-Met + Ser-Trp-Arg-Ala
D. Val-Lys-Glu + Met-Ser-Trp-Arg-Ala

963. What is shielding in NMR?
A. Using a curved piece of metal to block an opponents attack
B. Putting metal around an Rf source
C. When the magnetic moment of an atom blocks the full induced magnetic field from surrounding nuclei
D. Blocking parts of a molecule from Rf radiation

964. What is used to cool the superconducting coil?
A. Hydrogen
B. Ice
C. Dry ice
D. Liquid helium

965. Coupling causes the peaks in 1H NMR spectra to be split into
A. two peaks
B. multiple peaks equal to the number of hydrogens on surrounding atoms
C. multiple peaks equal to the number of surrounding carbon atoms
D. multiple peaks equal to the number of hydrogen on surrounding atoms, plus one

966. When placed in a magnetic field, all the random spins of the nuclei
A. stop
B. reverse direction
C. align with the magnetic field
D. rotate to 90° away from the induced field

967. Better understanding of the nuclei is possible,
A. with the help of wavelength spectrum
B. with the help of frequencies ranges
C. with the help of a mathematical translator called the fourier transfer algorithm
D. none of the above

968. All hydrogen atoms
A. have the same resonance frequency
B. resonate at different frequencies depending on their environment.
C. are attached to carbon
D. resonate at about the same frequency as carbon

969. Why is it important to use a deuterated solvent?
A. NMR uses least of this solvent
B. So the spectrometer can lock onto the sample to prevent the spectrum from drifting during aquisition
C. Expensive solvents work best with NMR
D. They dissolve polymer the fastest

970. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein
A. only at the ends of a-helices
B. only at the turns connecting p-strands
C. only on Pro residues
D. rarely

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