108569
Description
Mind Map by sophie_connor, updated more than 1 year ago
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Created by sophie_connor
over 11 years ago
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Nuclear Magnetic Resonance
- What does it do?
- Determines
structures of
biological
macromolecules
- Study time
dependent
phenomena
- Reaction
kinetics
- Molecular
recognition
- Protein
folding
- Reaction
kinetics
- Energy levels of atomic nuclei are
split by a magnetic field
- Transitions between energy levels can be induced
by exciting the sample with radiation whose
frequency is equivalent to the energy difference
between the two levels
- Transitions between energy levels can be induced
by exciting the sample with radiation whose
frequency is equivalent to the energy difference
between the two levels
- Determines
structures of
biological
macromolecules
- Limitations
- Low sensitivity
- High complexity
- Low sensitivity
- New developments in NMR
- Progress in spectromer
technology has increased
sensitivity and resolution of
NMR
- Theoretical advances
- Better
understanding of
information from
NMR
- Better
understanding of
information from
NMR
- Advances in biochemical methods
- Simple and fast
preparation of
samples
- Simple and fast
preparation of
samples
- Heteronuclei can be
incorporated into
protein
- Progress in spectromer
technology has increased
sensitivity and resolution of
NMR
- Why NMR?
- Probe molecules are in
their natural state
- Structure
- Function
- Dynamics
- Interactions with
ligands, proteins and
membranes
- Structure
- No crystal packing effects
- No need to crystallise
- NMR is expensive and uses
large equipment but structural
and functional information can be
found out
- Probe molecules are in
their natural state
- Peptide bond
- Repeating unit
throughout the
protein
- Allows
NMR to
work
- Repeating unit
throughout the
protein
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