Nuclear magnetic resonance spectroscopy

NMR spectra are unique, well-resolved, analytically

A 900MHz NMR instrument with a 21.1 T magnet at HWB-NMR,
Birmingham, UK
Nuclear magnetic resonance spectroscopy, most com-
monly known as NMR spectroscopy, is a research tech-
nique that exploits the magnetic properties of certain
atomic nuclei. This type of spectroscopy determines
the physical and chemical properties of atoms or the
molecules in which they are contained. It relies on the
phenomenon of nuclear magnetic resonance and can pro-
vide detailed information about the structure, dynamics,
reaction state, and chemical environment of molecules.
The intramolecular magnetic eld around an atom in a
molecule changes the resonance frequency, thus giving
access to details of the electronic structure of a molecule The Purcell group at Harvard University and the Bloch
and its individual functional groups.
Most frequently, NMR spectroscopy is used by chemists Edward Mills Purcell and Felix Bloch shared the 1952
and biochemists to investigate the properties of organic Nobel Prize in Physics for their discoveries.[1]
molecules, although it is applicable to any kind of sam-
ple that contains nuclei possessing spin. Suitable sam-
ples range from small compounds analyzed with 1-
dimensional proton or carbon-13 NMR spectroscopy to
large proteins or nucleic acids using 3 or 4-dimensional
techniques. The impact of NMR spectroscopy on the sci- 2.1 Resonant frequency
ences has been substantial because of the range of infor-
mation and the diversity of samples, including solutions When placed in a magnetic eld, NMR active nuclei (such
and solids.
tractable and often highly predictable for small molecules.
Thus, in organic chemistry practice, NMR analysis is
used to conrm the identity of a substance. Dier-
ent functional groups are obviously distinguishable, and
identical functional groups with diering neighboring
substituents still give distinguishable signals. NMR has
largely replaced traditional wet chemistry tests such as
color reagents or typical chromatography for identica-
tion. A disadvantage is that a relatively large amount,
250 mg, of a puried substance is required, although
it may be recovered through a workup. Preferably, the
sample should be dissolved in a solvent, because NMR
analysis of solids requires a dedicated MAS machine and
may not give equally well-resolved spectra. The timescale
of NMR is relatively long, and thus it is not suitable for
observing fast phenomena, producing only an averaged
spectrum. Although large amounts of impurities do show
on an NMR spectrum, better methods exist for detect-
ing impurities, as NMR is inherently not very sensitive -
though at higher frequencies, sensitivity narrows.
NMR spectrometers are relatively expensive; universi-
ties usually have them, but they are less common in pri-
vate companies. Modern NMR spectrometers have a
very strong, large and expensive liquid helium-cooled
superconducting magnet, because resolution directly de-
pends on magnetic eld strength. Less expensive ma-
chines using permanent magnets and lower resolution are
also available, which still give sucient performance for
certain application such as reaction monitoring and quick
checking of samples. There are even benchtop NMR
spectrometers.
1 History
group at Stanford University independently developed
NMR spectroscopy in the late 1940s and early 1950s.
2 Basic NMR techniques
as 1 H or 13 C) absorb electromagnetic radiation at a fre-

1
2 2 BASIC NMR TECHNIQUES
The NMR sample is prepared in a thin-walled glass tube - an
NMR tube.
quency characteristic of the isotope.[2] The resonant fre-
quency, energy of the absorption, and the intensity of the
signal are proportional to the strength of the magnetic
eld. For example, in a 21 Tesla magnetic eld, protons
resonate at 900 MHz. It is common to refer to a 21 T
magnet as a 900 MHz magnet, although dierent nuclei
resonate at a dierent frequency at this eld strength in
proportion to their nuclear magnetic moments.
2.2 Sample handling
A NMR spectrometer typically consists of a spinning
sample-holder inside a very strong magnet, a radio-
frequency emitter and a receiver with a probe (an an-
tenna assembly) that goes inside the magnet to surround
the sample, optionally gradient coils for diusion mea-
surements and electronics to control the system. Spinning
the sample is necessary to average out diusional motion.
Whereas, measurements of diusion constants (diusion
ordered spectroscopy or DOSY)[3][4] are done the sample
stationary and spinning o, and ow cells can be used for
online analysis of process ows.
2.3 Deuterated solvents
The vast majority of nuclei in a solution would be-
long to the solvent, and most regular solvents are
hydrocarbons and would contain NMR-reactive protons.
Thus, deuterium (hydrogen-2) is substituted (99+%).
The most used deuterated solvent is deuterochloroform
(CDCl3 ), although deuterium oxide (D2 O) and deuter-
ated DMSO (DMSO-d6 ) are used for hydrophilic ana-
lytes and deuterated benzene is also common. The chem-
ical shifts are slightly dierent in dierent solvents, de-
pending on electronic solvation eects. NMR spectra are
often calibrated against the known solvent residual proton
peak instead of added tetramethylsilane.
2.4 Shim and lock
To detect the very small frequency shifts due to nuclear
magnetic resonance, the applied magnetic eld must be
constant throughout the sample volume. High resolution
NMR spectrometers use shims to adjust the homogeneity
of the magnetic eld to parts per billion (ppb) in a vol-
ume of a few cubic centimeters. In order to detect and
compensate for inhomogeneity and drift in the magnetic
eld, the spectrometer maintains a lock on the solvent
deuterium frequency with a separate lock unit. In mod-
ern NMR spectrometers shimming is adjusted automati-
cally, though in some cases the operator has to optimize
the shim parameters manually to obtain the best possible
resolution.[5][6]
2.5 Acquisition of spectra
Upon excitation of the sample with a radio frequency
(601000 MHz) pulse, a nuclear magnetic resonance re-
sponse - a free induction decay (FID) - is obtained. It is a
very weak signal, and requires sensitive radio receivers
to pick up. A Fourier transform is carried out to ex-
tract the frequency-domain spectrum from the raw time-
domain FID. A spectrum from a single FID has a low
signal-to-noise ratio, but fortunately it improves readily
with averaging of repeated acquisitions. Good 1 H NMR
spectra can be acquired with 16 repeats, which takes only
minutes. However, for elements heavier than hydrogen,
the relaxation time is rather long, e.g. around 8 seconds
for 13 C. Thus, acquisition of quantitative heavy-element
spectra can be time-consuming, taking tens of minutes to
hours.
If the second excitation pulse is sent prematurely before
the relaxation is complete, the average magnetization vec-
tor still points in a nonparallel direction, giving subopti-
mal absorption and emission of the pulse. In practice, the
peak areas are then not proportional to the stoichiome-
try; only the presence, but not the amount of functional
groups is possible to discern. An inversion recovery ex-
periment can be done to determine the relaxation time
and thus the required delay between pulses. A 180 pulse,
an adjustable delay, and a 90 pulse is transmitted. When
the 90 pulse exactly cancels out the signal, the delay cor-
responds to the time needed for 90 of relaxation.[7] In-
version recovery is worthwhile for quantitive 13 C, 2D and
other time-consuming experiments.
2.6 Chemical shift 3

2.6 Chemical shift agnetic contribution to shielding tensor).

Main article: Chemical shift

A spinning charge generates a magnetic eld that results

in a magnetic moment proportional to the spin. In the
presence of an external magnetic eld, two spin states ex-
ist (for a spin 1/2 nucleus): one spin up and one spin down,
where one aligns with the magnetic eld and the other op-
poses it. The dierence in energy (E) between the two
spin states increases as the strength of the eld increases,
but this dierence is usually very small, leading to the re-
quirement for strong NMR magnets (1-20 T for modern
NMR instruments). Irradiation of the sample with en-
ergy corresponding to the exact spin state separation of a
specic set of nuclei will cause excitation of those set of
nuclei in the lower energy state to the higher energy state. Example of the chemical shift: NMR spectrum of hexaborane
For spin 1/2 nuclei, the energy dierence between the B6 H10 showing peaks shifted in frequency, which give clues as
two spin states at a given magnetic eld strength is pro- to the molecular structure. (click to read interpretation details)
portional to their magnetic moment. However, even if
all protons have the same magnetic moments, they do The chemical shift provides information about the struc-
not give resonant signals at the same frequency values. ture of the molecule. The conversion of the raw data
This dierence arises from the diering electronic en- to this information is called assigning the spectrum.
1
vironments of the nucleus of interest. Upon application For example, for the H-NMR spectrum for ethanol
of an external magnetic eld, these electrons move in re- (CH3 CH2 OH), one would expect signals at each of three
sponse to the eld and generate local magnetic elds that specic chemical shifts: one for the CH 3 group, one for
oppose the much stronger applied eld. This local eld the CH 2 group and one for the OH group. A typical CH3
thus shields the proton from the applied magnetic eld, group has a shift around 1 ppm, a CH2 attached to an OH
which must therefore be increased in order to achieve res- has a shift of around 4 ppm and an OH has a shift any-
onance (absorption of rf energy). Such increments are where from 26 ppm depending on the solvent used and
very small, usually in parts per million (ppm). For in- the amount of hydrogen bonding. While the O atom does
stance, the proton peak from an aldehyde is shifted ca. draw electron density away from the attached H through
10 ppm compared to a hydrocarbon peak, since as an their mutual sigma bond, the electron lone pairs on the O
electron-withdrawing group, the carbonyl deshields the bathe the H in their shielding eect.
proton by reducing the local electron density. The dier- In Paramagnetic NMR spectroscopy, measurements are
ence between 2.3487 T and 2.3488 T is therefore about conducted on paramagnetic samples. The paramagnetism
42 ppm. However a frequency scale is commonly used to gives rise to very diverse chemical shifts. In 1H NMR
designate the NMR signals, even though the spectrometer spectroscopy, the chemical shift range can span 500 ppm.
may operate by sweeping the magnetic eld, and thus the
42 ppm is 4200 Hz for a 100 MHz reference frequency Because of molecular motion at room temperature, the
three methyl protons average out during the NMR exper-
(rf).
iment (which typically requires a few ms). These protons
However given that the location of dierent NMR sig- become degenerate and form a peak at the same chemical
nals is dependent on the external magnetic eld strength shift.
and the reference frequency, the signals are usually re-
ported relative to a reference signal, usually that of TMS The shape and area of peaks are indicators of chemical
(tetramethylsilane). Additionally, since the distribution structure too. In the example abovethe proton spec-
of NMR signals is eld dependent, these frequencies trum of ethanolthe CH3 peak has three times the area
are divided by the spectrometer frequency. However, as the OH peak. Similarly the CH2 peak would be twice
since we are dividing Hz by MHz, the resulting number the area of the OH peak but only 2/3 the area of the CH3
would be too small, and thus it is multiplied by a million. peak.
This operation therefore gives a locator number called Software allows analysis of signal intensity of peaks,
the chemical shift with units of parts per million.[8] which under conditions of optimal relaxation, correlate
In general, chemical shifts for protons are highly pre- with the number of protons of that type. Analysis of
dictable since the shifts are primarily determined by sim- signal intensity is done by integrationthe mathematical
pler shielding eects (electron density), but the chemi- process that calculates the area under a curve. The an-
cal shifts for many heavier nuclei are more strongly inu- alyst must integrate the peak and not measure its height
enced by other factors including excited states (param- because the peaks also have widthand thus its size is
4 2 BASIC NMR TECHNIQUES

dependent on its area not its height. However, it should on the NMR spectra and couplings between nuclei that
be mentioned that the number of protons, or any other are distant (usually more than 3 bonds apart for protons
observed nucleus, is only proportional to the intensity, or in exible molecules) are usually too small to cause ob-
the integral, of the NMR signal in the very simplest one- servable splittings. Long-range couplings over more than
dimensional NMR experiments. In more elaborate exper- three bonds can often be observed in cyclic and aromatic
iments, for instance, experiments typically used to obtain compounds, leading to more complex splitting patterns.
carbon-13 NMR spectra, the integral of the signals de- For example, in the proton spectrum for ethanol de-
pends on the relaxation rate of the nucleus, and its scalar scribed above, the CH3 group is split into a triplet with
and dipolar coupling constants. Very often these factors
an intensity ratio of 1:2:1 by the two neighboring CH2
are poorly known - therefore, the integral of the NMR protons. Similarly, the CH2 is split into a quartet with an
signal is very dicult to interpret in more complicated
intensity ratio of 1:3:3:1 by the three neighboring CH3
NMR experiments. protons. In principle, the two CH2 protons would also be
split again into a doublet to form a doublet of quartets by
the hydroxyl proton, but intermolecular exchange of the
2.7 J-coupling acidic hydroxyl proton often results in a loss of coupling
information.
Main article: J-coupling
Some of the most useful information for structure de- Coupling to any spin nuclei such as phosphorus-31
or uorine-19 works in this fashion (although the mag-
nitudes of the coupling constants may be very dier-
ent). But the splitting patterns dier from those described
above for nuclei with spin greater than because the spin
quantum number has more than two possible values. For
instance, coupling to deuterium (a spin 1 nucleus) splits
the signal into a 1:1:1 triplet because the spin 1 has three
spin states. Similarly, a spin 3/2 nucleus splits a signal
into a 1:1:1:1 quartet and so on.
Coupling combined with the chemical shift (and the in-
tegration for protons) tells us not only about the chemical
environment of the nuclei, but also the number of neigh-
boring NMR active nuclei within the molecule. In more
complex spectra with multiple peaks at similar chemical
Example H NMR spectrum (1-dimensional) of ethanol plotted shifts or in spectra of nuclei other than hydrogen, cou-
1

as signal intensity vs. chemical shift. There are three dierent pling is often the only way to distinguish dierent nuclei.
types of H atoms in ethanol regarding NMR. The hydrogen (H) on
the -OH group is not coupling with the other H atoms and appears
as a singlet, but the CH3 - and the -CH2 - hydrogens are coupling
with each other, resulting in a triplet and quartet respectively.

termination in a one-dimensional NMR spectrum comes

from J-coupling or scalar coupling (a special case of
spin-spin coupling) between NMR active nuclei. This
coupling arises from the interaction of dierent spin
states through the chemical bonds of a molecule and re-
sults in the splitting of NMR signals. These splitting pat-
terns can be complex or simple and, likewise, can be
straightforwardly interpretable or deceptive. This cou-
pling provides detailed insight into the connectivity of
atoms in a molecule.
Coupling to n equivalent (spin ) nuclei splits the sig- 1
nal into a n+1 multiplet with intensity ratios following H NMR spectrum of menthol with chemical shift in ppm on
the horizontal axis. Each magnetically inequivalent proton has
Pascals triangle as described on the right. Coupling to
a characteristic shift, and couplings to other protons appear as
additional spins will lead to further splittings of each com-
splitting of the peaks into multiplets: e.g. peak a, because of the
ponent of the multiplet e.g. coupling to two dierent spin three magnetically equivalent protons in methyl group a, couple
nuclei with signicantly dierent coupling constants to one adjacent proton (e) and thus appears as a doublet.
will lead to a doublet of doublets (abbreviation: dd). Note
that coupling between nuclei that are chemically equiva-
lent (that is, have the same chemical shift) has no eect

2.7.1 Second-order (or strong) coupling
The above description assumes that the coupling constant
is small in comparison with the dierence in NMR fre-
quencies between the inequivalent spins. If the shift sep-
aration decreases (or the coupling strength increases), the
multiplet intensity patterns are rst distorted, and then be-
come more complex and less easily analyzed (especially
if more than two spins are involved). Intensication of
some peaks in a multiplet is achieved at the expense of
the remainder, which sometimes almost disappear in the
background noise, although the integrated area under the
peaks remains constant. In most high-eld NMR, how-
ever, the distortions are usually modest and the charac-
teristic distortions (roong) can in fact help to identify
related peaks.
Some of these patterns can be analyzed with the method
published by John Pople,[9] though it has limited scope.
Second-order eects decrease as the frequency dier-
ence between multiplets increases, so that high-eld (i.e.
high-frequency) NMR spectra display less distortion than
lower frequency spectra. Early spectra at 60 MHz were
more prone to distortion than spectra from later machines
typically operating at frequencies at 200 MHz or above.
2.7.2 Magnetic inequivalence
For more details on this topic, see Magnetic inequiva-
lence.
More subtle eects can occur if chemically equivalent
spins (i.e., nuclei related by symmetry and so having the
same NMR frequency) have dierent coupling relation-
ships to external spins. Spins that are chemically equiva-
lent but are not indistinguishable (based on their coupling
relationships) are termed magnetically inequivalent. For
example, the 4 H sites of 1,2-dichlorobenzene divide into
two chemically equivalent pairs by symmetry, but an in-
dividual member of one of the pairs has dierent cou-
plings to the spins making up the other pair. Magnetic
inequivalence can lead to highly complex spectra which
can only be analyzed by computational modeling. Such
eects are more common in NMR spectra of aromatic
and other non-exible systems, while conformational av-
eraging about C-C bonds in exible molecules tends to
equalize the couplings between protons on adjacent car-
bons, reducing problems with magnetic inequivalence.
3 Correlation spectroscopy
For more details on this topic, see 2D-NMR.
Applications in which solid-state NMR eects occur are
Correlation spectroscopy is one of several types of two- often related to structure investigations on membrane
dimensional nuclear magnetic resonance (NMR) spec- proteins, protein brils or all kinds of polymers, and
5
troscopy or 2D-NMR. This type of NMR experiment
is best known by its acronym, COSY. Other types
of two-dimensional NMR include J-spectroscopy, ex-
change spectroscopy (EXSY), Nuclear Overhauser eect
spectroscopy (NOESY), total correlation spectroscopy
(TOCSY) and heteronuclear correlation experiments,
such as HSQC, HMQC, and HMBC. In correlation spec-
troscopy, emission is centered on the peak of an indi-
vidual nucleus; if its magnetic eld is correlated with
another nucleus by through-bond (COSY, HSQC, etc.)
or through-space (NOE) coupling, a response can also
be detected on the frequency of the correlated nucleus.
Two-dimensional NMR spectra provide more informa-
tion about a molecule than one-dimensional NMR spectra
and are especially useful in determining the structure of
a molecule, particularly for molecules that are too com-
plicated to work with using one-dimensional NMR. The
rst two-dimensional experiment, COSY, was proposed
by Jean Jeener, a professor at Universit Libre de Brux-
elles, in 1971.[10][11] This experiment was later imple-
mented by Walter P. Aue, Enrico Bartholdi and Richard
R. Ernst, who published their work in 1976.[12]
4 Solid-state nuclear magnetic res-
onance
For more details on this topic, see Solid-state NMR.
A variety of physical circumstances do not allow
molecules to be studied in solution, and at the same time
not by other spectroscopic techniques to an atomic level,
either. In solid-phase media, such as crystals, micro-
crystalline powders, gels, anisotropic solutions, etc., it
is in particular the dipolar coupling and chemical shift
anisotropy that become dominant to the behaviour of
the nuclear spin systems. In conventional solution-state
NMR spectroscopy, these additional interactions would
lead to a signicant broadening of spectral lines. A vari-
ety of techniques allows establishing high-resolution con-
ditions, that can, at least for 13 C spectra, be comparable
to solution-state NMR spectra.
Two important concepts for high-resolution solid-state
NMR spectroscopy are the limitation of possible molec-
ular orientation by sample orientation, and the reduction
of anisotropic nuclear magnetic interactions by sample
spinning. Of the latter approach, fast spinning around
the magic angle is a very prominent method, when the
system comprises spin 1/2 nuclei. Spinning rates of ca.
20 kHz are used, which demands special equipment. A
number of intermediate techniques, with samples of par-
tial alignment or reduced mobility, is currently being used
in NMR spectroscopy.
6 5 BIOMOLECULAR NMR SPECTROSCOPY

chemical analysis in inorganic chemistry, but also in- 5.2 Nucleic acids
clude exotic applications like the plant leaves and fuel
cells. For example, Rahmani et al. studied the eect of
pressure and temperature on the bicellar structures self- Main article: Nuclear magnetic resonance spectroscopy
assembly using deuterium NMR spectroscopy.[13] of nucleic acids

"Nucleic acid NMR" is the use of NMR spectroscopy to

obtain information about the structure and dynamics of
polynucleic acids, such as DNA or RNA. As of 2003,
nearly half of all known RNA structures had been deter-
mined by NMR spectroscopy.[14]
5 Biomolecular NMR spectroscopy Nucleic acid and protein NMR spectroscopy are similar
but dierences exist. Nucleic acids have a smaller per-
centage of hydrogen atoms, which are the atoms usually
5.1 Proteins observed in NMR spectroscopy, and because nucleic acid
double helices are sti and roughly linear, they do not fold
back on themselves to give long-range correlations.[15]
Main article: Nuclear magnetic resonance spectroscopy
The types of NMR usually done with nucleic acids are 1 H
of proteins
or proton NMR, 13 C NMR, 15 N NMR, and 31 P NMR.
Two-dimensional NMR methods are almost always used,
Much of the innovation within NMR spectroscopy has such as correlation spectroscopy (COSY) and total coher-
been within the eld of protein NMR spectroscopy, an ence transfer spectroscopy (TOCSY) to detect through-
important technique in structural biology. A common bond nuclear couplings, and nuclear Overhauser eect
goal of these investigations is to obtain high resolu- spectroscopy (NOESY) to detect couplings between nu-
tion 3-dimensional structures of the protein, similar to clei that are close to each other in space.[16]
what can be achieved by X-ray crystallography. In con-
Parameters taken from the spectrum, mainly NOESY
trast to X-ray crystallography, NMR spectroscopy is usu-
cross-peaks and coupling constants, can be used to de-
ally limited to proteins smaller than 35 kDa, although
termine local structural features such as glycosidic bond
larger structures have been solved. NMR spectroscopy
angles, dihedral angles (using the Karplus equation), and
is often the only way to obtain high resolution informa-
sugar pucker conformations. For large-scale structure,
tion on partially or wholly intrinsically unstructured pro-
these local parameters must be supplemented with other
teins. It is now a common tool for the determination of
structural assumptions or models, because errors add up
Conformation Activity Relationships where the structure
as the double helix is traversed, and unlike with proteins,
before and after interaction with, for example, a drug
the double helix does not have a compact interior and
candidate is compared to its known biochemical activ-
does not fold back upon itself. NMR is also useful for in-
ity. Proteins are orders of magnitude larger than the small
vestigating nonstandard geometries such as bent helices,
organic molecules discussed earlier in this article, but
non-WatsonCrick basepairing, and coaxial stacking. It
the basic NMR techniques and some NMR theory also
has been especially useful in probing the structure of nat-
applies. Because of the much higher number of atoms
ural RNA oligonucleotides, which tend to adopt com-
present in a protein molecule in comparison with a small
plex conformations such as stem-loops and pseudoknots.
organic compound, the basic 1D spectra become crowded
NMR is also useful for probing the binding of nucleic acid
with overlapping signals to an extent where direct spec-
molecules to other molecules, such as proteins or drugs,
tral analysis becomes untenable. Therefore, multidimen-
by seeing which resonances are shifted upon binding of
sional (2, 3 or 4D) experiments have been devised to deal
the other molecule.[16]
with this problem. To facilitate these experiments, it is
desirable to isotopically label the protein with 13 C and
15
N because the predominant naturally occurring isotope
12
C is not NMR-active and the nuclear quadrupole mo-
ment of the predominant naturally occurring 14 N isotope
prevents high resolution information from being obtained
from this nitrogen isotope. The most important method 5.3 Carbohydrates
used for structure determination of proteins utilizes NOE
experiments to measure distances between pairs of atoms
within the molecule. Subsequently, the distances ob- Main article: Nuclear magnetic resonance spectroscopy
tained are used to generate a 3D structure of the molecule of carbohydrates
by solving a distance geometry problem. NMR can also
be used to obtain information on the dynamics and con- Carbohydrate NMR spectroscopy addresses questions on
formational exibility of dierent regions of a protein. the structure and conformation of carbohydrates.
 7

6 See also [6] http://www2.chemistry.msu.edu/facilities/nmr/NMR_

Artifacts.html
Distance geometry [7] http://triton.iqfr.csic.es/guide/eNMR/eNMR1D/invrec.
html
Earths eld NMR
[8] James Keeler. Chapter 2: NMR and energy levels
In vivo magnetic resonance spectroscopy (reprinted at University of Cambridge). Understanding
NMR Spectroscopy. University of California, Irvine. Re-
Functional magnetic resonance spectroscopy of the
trieved 2007-05-11.
brain
[9] Pople, J.A.; Bernstein, H. J.; Schneider, W. G. (1957).
Low eld NMR The Analysis of Nuclear Magnetic Resonanace Spectra.
Can J. Chem. 35: 6581.
Magnetic Resonance Imaging
[10] Aue, W. P. and Bartholdi, E. and Ernst, R. R.,
NMR crystallography Twodimensional spectroscopy. Application to nuclear
magnetic resonance; The Journal of Chemical Physics, 64,
NMR spectra database
2229-2246 (1976)
NMR tube - includes a section on sample prepara-
[11] Jeener, J., Jeener, Jean: Reminiscences about the Early
tion Days of 2D NMR; John Wiley & Sons, Ltd: Encyclope-
dia of Magnetic Resonance (2007)
NMR spectroscopy of stereoisomers
[12] Martin, G.E; Zekter, A.S., Two-Dimensional NMR Meth-
Nuclear magnetic resonance spectroscopy of nucleic ods for Establishing Molecular Connectivity; VCH Pub-
acids lishers, Inc: New York, 1988 (p.59)
Nuclear magnetic resonance spectroscopy of pro- [13] A. Rahmani, C. Knight , and M. R. Morrow. Response
teins to hydrostatic pressure of bicellar dispersions containing
anionic lipid: Pressure-induced interdigitation. 2013, 29
Nuclear quadrupole resonance (44), pp 1348113490, DOI: 10.1021/la4035694
Pulsed eld magnet [14] Frtig, Boris; Richter, Christian; Whnert, Jens;
Schwalbe, Harald (2003). NMR Spectroscopy
Relaxation (NMR) of RNA. ChemBioChem. 4 (10): 93662.
doi:10.1002/cbic.200300700. PMID 14523911.
Triple-resonance nuclear magnetic resonance spec-
troscopy [15] Addess, Kenneth J.; Feigon, Juli (1996). Introduction to
1
H NMR Spectroscopy of DNA. In Hecht, Sidney M.
Bioorganic Chemistry: Nucleic Acids. New York: Oxford
7 References University Press. ISBN 0-19-508467-5.

[16] Wemmer, David (2000). Chapter 5: Structure and Dy-

[1] Background and Theory Page of Nuclear Magnetic Res- namics by NMR. In Bloomeld, Victor A.; Crothers,
onance Facility. Mark Wainwright Analytical Centre - Donald M.; Tinoco, Ignacio. Nucleic acids: Structures,
University of Southern Wales Sydney. 9 December 2011. Properties, and Functions. Sausalito, California: Univer-
Retrieved 9 February 2014. sity Science Books. ISBN 0-935702-49-0.

[2] Shah, N; Sattar, A; Benanti, M; Hollander, S; Cheuck, L

(January 2006). Magnetic resonance spectroscopy as an
imaging tool for cancer: a review of the literature.. The 8 Further reading
Journal of the American Osteopathic Association. 106 (1):
2327. PMID 16428685. John D. Roberts (1959). Nuclear Magnetic Reso-
[3] Johnson Jr., C. S. (1999). Diusion ordered nuclear
nance : applications to organic chemistry. McGraw-
magnetic resonance spectroscopy: principles and ap- Hill Book Company. ISBN 9781258811662.
plications. Progress in Nuclear Magnetic Resonance
J.A.Pople; W.G.Schneider; H.J.Bernstein (1959).
Spectroscopy. 34: 203256. doi:10.1016/S0079-
High-resolution Nuclear Magnetic Resonance.
6565(99)00003-5.
McGraw-Hill Book Company.
[4] Neufeld, R.; Stalke, D. (2015). Accurate Molecular
Weight Determination of Small Molecules via DOSY- A. Abragam (1961). The Principles of Nuclear Mag-
NMR by Using External Calibration Curves with Normal- netism. Clarendon Press. ISBN 9780198520146.
ized Diusion Coecients. Chem. Sci. 6: 33543364.
Charles P. Slichter (1963). Principles of magnetic
doi:10.1039/C5SC00670H.
resonance: with examples from solid state physics.
[5] http://nmr.chem.wsu.edu/tutorials/basics/lock/ Harper & Row. ISBN 9783540084761.
8 9 EXTERNAL LINKS

John Emsley; James Feeney; Leslie Howard Sut-

clie (1965). High Resolution Nuclear Mag-
netic Resonance Spectroscopy. Pergamon. ISBN
9781483184081.

9 External links
James Keeler. Understanding NMR Spectroscopy
(reprinted at University of Cambridge). University
of California, Irvine. Retrieved 2007-05-11.
The Basics of NMR - A non-technical overview
of NMR theory, equipment, and techniques by Dr.
Joseph Hornak, Professor of Chemistry at RIT

GAMMA and PyGAMMA Libraries - GAMMA is

an open source C++ library written for the simula-
tion of Nuclear Magnetic Resonance Spectroscopy
experiments. PyGAMMA is a Python wrapper
around GAMMA.
relax Software for the analysis of NMR dynamics

Vespa - VeSPA (Versatile Simulation, Pulses and

Analysis) is a free software suite composed of three
Python applications. These GUI based tools are for
magnetic resonance (MR) spectral simulation, RF
pulse design, and spectral processing and analysis of
MR data.
 9

10 Text and image sources, contributors, and licenses

10.1 Text
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