NMR occurs when the nucleus changes its _______ driven by absorption of quantum of
energy. this energy is applied as ________ - ANSWER spin status, electromagnetic
radiation
is ^2H visible by NMR - ANSWER no
why does a higher field NMR give a better NMR signal - ANSWER higher field NMR gives
rise to bigger population difference between alpha and beta states and thus gives a
better NMR signal
in MRI tissue contrast is determined by differences in ____? - ANSWER T1 and T2
relaxation
______ coupling is mediated through chemical bonds connecting two spins - ANSWER
scalar
scalar coupling provides _______ information - ANSWER connectivity
______ coupling is mediated by two NMR active nuclei through space - ANSWER dipolar
dipolar coupling provides ____ information - ANSWER spatial
________ is used to identify amino acid side-chain spin system - ANSWER correlation
spectroscopy
, ________ is used to identify neighboring residues - ANSWER triple resonance
spectroscopy
nuclear overhasuer enhancement can be detected between protons within 5 angstroms.
T/F - ANSWER true
why does molecular size greatly limit NMR application in macromolecules - ANSWER
signal overlap and signal degeneracy
low dynamic regions of a protein usually give rise to a _____ exchanging NHs in a H/D
exchange NMR experiment - ANSWER slow
NMR linewidth is the full peak width at ______ height - ANSWER half maximum
NMR data for a compound were collected at three different temps. which temp makes
the compound most flexible - ANSWER 280K
NMR linewidth is directly related to ? - ANSWER transverse relaxation rate R2
theoretically if A-B exchanging rate Kex is way faster than the chemical shift difference
between A and B ______ will be observed - ANSWER a single peak at the average of A
and B chemical shifts
theoretically if A-B exchanging rate Kex is way slower than the chemical shift difference
between A and B ______ will be observed - ANSWER two separate peaks at A and B
chemical shifts
peptide bonds can undergo what transitions - ANSWER n to π*
π to π*
the amino acid residues in protein capable of absorbing in the near UV between
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