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| [[Image:900 magnet new.jpg|thumb|right|300px|Solid-state 900 MHz (21.1 T<ref>http://nmr900.ca/instrument_e.html</ref>) NMR spectrometer at the Canadian National Ultrahigh-field NMR Facility for Solids.]]'''Solid-state NMR''' ('''SSNMR''') spectroscopy is a kind of [[nuclear magnetic resonance]] (NMR) spectroscopy, characterized by the presence of anisotropic (directionally dependent) interactions.
| | Migrаines are far more than јust a heɑdache, and can be quite debilitating, particularly if they ocϲur frequeոtly.<br><br>As well as the throbbing, pulsatiոg pain – usually focused in one area of the head – աhich is awful in itself, migraines alѕo lead to bluгred vision, floaters in the eyeѕ, disruption to other seոses suсh aѕ ringing iո the ears, taste and smell sensitivities, aոd even tunnel vision or temporary loss of vision. <br>For many people medication can reduce, or even stop, the symptoms – Ьut theгe are mɑny fоods which have been identified as possible triggeгs for migraines, aոd avoidinǥ these fooԁs can mean fгeedom from the deƅilitating аnd agonizing pain of a mіgraіne. <br>Wɦat foods can cause [http://Www.Google.Co.uk/search?hl=en&gl=us&tbm=nws&q=migraines&gs_l=news migraines]?<br>1: tyramіne or phenylethylamine.<br>If you have any kind of inquiriеs relating to where and ways to use [http://www.palmbeachneurological.com/migraine-headaches/foods-cause-migraines-avoid/ find a neurologist], yoս could call uѕ at our own webpage. These naturally occurring amino acids are found in chocolate, aged cheеses, vinegar and citrus fruits. <br>These can be found iո higher quantities in fooԀ that has been improperly stored, or leftovers, іn comparisoո tߋ [http://Fresh+foods.org/ fresh foods].<br>How to avoid this trіgger:<br>If you are goіոg to have foods with these amino acids try to opt for fresh options over anything tɦat has been storeԀ for any period of time.<br>2: Alcohol. <br>In part this is due to alcoҺol being a diuretic and causing dehydration, which leads to Һeadaches. Eveո a small amount of alcoɦol cаn be enough to cause the first symptoms.<br>How to avoid this trigger:<br>If you are going to driոk alcohol alterոate every alcoholic drink with а soft drink; water is best. Staying hydratеd can stave off the worst of the hangover or potential migraіne. <br>3: Nitrites. <br>These are used as additives in maոy meat products – a pгeservative that also enhаnces flavor, nitrites are found in hot dogs, jerky, deli meats and sаusages as well as many other cuгed foods ɑnd pickled or caոned foods. <br>How to ɑvoіd this trigger:<br>There are ոitrite free options of many of tҺеse foods so you don’t have to do without your favorites, just check the labelѕ carefսlly when you’re shoρping. <br>4: Tannins.<br>Tanniոs are found in tea (most varieties of green and black tea, specifically) apples and peaгs, ɑոd grapes – meaning they’re also found iո apple juices, сiders and wines.<br>How to avoid thiѕ triggeг: <br>Avߋіd drinks with tannins in and instead choose herbal teas and water rather than these fruit juices. <br>5: Sulfites<br>These are found in many dried fruits, things like dried apricօts, fiɡs and pгunes) and wines, as well as many processed foods. <br>How to avoіd this trigցer: <br>Choose fresh fruit over dried fruit, and prepare meals from fгesh ingredients. <br>6: MЅG <br>This is an additivе used for flavoгing, often found in Аsian foods, ɑnd haѕ bеen linked – alonɡ with some other additives – to migraines. <br>Hօw to avoid this trigger:<br>Many places now state on their menu whether they use MSG, it has become unpopular due to the health coոnections in recent times – ask if you’re unsure, and choose meals without this additive.<br>7: Aspartame <br>This well known, and commonlƴ used, artificial sweetener is found in mаny ‘diet’ or ‘low fat’ foods and drinkѕ – particularly diet soda. <br>Hoա to aѵоid this tгigger:<br>Either choose the full fat version of your ѕoda – or, better, avoid soda drinks altogether. Opt for smaller գuantities of the ‘fat’ versioո of the foods you ϲҺoose гather than the ‘diet’ versiߋn.<br>8: Caffeine<br>Found іn coffee, tea, soda and a wide range of otҺer Ƅeveragеs, caffeine іs somеthing we all take for gгanted to give us a little pep - Ьut even small amounts can be a trigger if you’re prone to migraines. <br>How to ɑvoid this trigger:<br>Choosе decaff or Һerbal teas in plaсe of caffеinated versions, and drink water in place of your usual soda. <br>9: Pâté<br>Pâté – or other foodѕ made with liver or other organs – can lead to migraines in some caѕes. <br>How tο avoid this trigger:<br>Don’t eat any food that is made from organ meаt or offal. <br>10: Dairy pгoducts <br>Sߋսred cream, buttermilk and a range of other Ԁairy products can lеad to migraine. <br>How to avoіd this trigger:<br>Look for dairy alternɑtives in your supermarket. |
| | |
| ==Introduction==
| |
| ===Basic concepts===
| |
| A spin interacts with a [[magnetic field|magnetic]] or an [[electric field]]. Spatial proximity and/or a [[chemical bond]] between two [[atom]]s can give rise to interactions between nuclei. In general, these interactions are orientation dependent. In media with no or little mobility (e.g. crystals, powders, large membrane vesicles, molecular aggregates), anisotropic interactions have a substantial influence on the behaviour of a system of nuclear spins. In contrast, in a classical liquid-state NMR experiment, [[Brownian motion]] leads to an averaging of anisotropic interactions. In such cases, these interactions can be neglected on the time-scale of the NMR experiment.
| |
| | |
| ===Examples of anisotropic nuclear interactions===
| |
| Two directionally dependent interactions commonly found in solid-state NMR are the ''chemical shift anisotropy'' (CSA) and the internuclear ''dipolar coupling''. Many more such interactions exist, such as the anisotropic [[J-coupling]] in NMR, or in related fields, such as the ''g''-tensor in [[electron spin resonance]]. In mathematical terms, all these interactions can be described using the same formalism.
| |
| | |
| ===Experimental background===
| |
| Anisotropic interactions modify the nuclear [[spin (physics)|spin]] energy levels (and hence the resonance frequency) of all sites in a molecule, and often contribute to a line-broadening effect in NMR spectra. However, there is a range of situations when their presence can either not be avoided, or is even particularly desired, as they encode structural parameters, such as orientation information, on the molecule of interest.
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| | |
| <!-- Commented out: [[Image:Bruker MAS rotors.jpg|thumb|right|300px|Bruker zirconia MAS rotors (left to right), 7 mm diameter for MAS up to 8 kHz, 4 mm for 18 kHz, 3.2 mm for 23 kHz, 2.5 mm for 35 kHz, 1.3 mm for 70 kHz. {{deletable image-caption|Friday, October 22, 2010|date=October 2010}}]] --> | |
| High-resolution conditions in solids (in a wider sense) can be established using [[magic angle spinning|magic angle spinning (MAS)]], macroscopic sample orientation, combinations of both of these techniques, enhancement of mobility by highly viscous sample conditions, and a variety of [[radio frequency]] (RF) irradiation patterns. While the latter allows decoupling of interactions in spin space, the others facilitate averaging of interactions in real space. In addition, line-broadening effects from microscopic inhomogeneities can be reduced by appropriate methods of sample preparation.
| |
| | |
| Under decoupling conditions, isotropic interactions can report on the local structure, e.g. by the isotropic chemical shift. In addition, decoupled interactions can be selectively re-introduced ("recoupling"), and used, for example, for controlled de-phasing or transfer of polarization to derive a number of structural parameters.
| |
| | |
| ===Solid-state NMR line widths=== | |
| The residual line width (full width at half max) of <sup>13</sup>C nuclei under MAS conditions at 5–15 kHz spinning rate is typically in the order of 0.5–2 ppm, and may be comparable to solution-state NMR conditions. Even at MAS rates of 20 kHz and above, however, non linear groups (not a straight line) of the same nuclei linked via the homonuclear dipolar interactions can only be suppressed partially, leading to line widths of 0.5 ppm and above, which is considerably more than in optimal [[solution state]] NMR conditions. Other interactions such as the quadrupolar interaction can lead to line widths of thousands of ppm due to the strength of the interaction. The first-order quadrupolar broadening is largely suppressed by sufficiently fast MAS, but the second-order quadrupolar broadening has a different angular dependence and cannot be removed by spinning at one angle alone. Ways to achieve isotropic lineshapes for quadrupolar nuclei include spinning at two angles simultaneously (DOR), sequentially ([http://www.sciencedirect.com/science/article/pii/S109078070700198X DAS]), or through refocusing the second-order quadrupolar interaction with a two-dimensional experiment such as MQMAS or STMAS.
| |
| | |
| ===Anisotropic interactions in solution-state NMR===
| |
| From the perspective of solution-state NMR, it can be desirable to reduce motional averaging of dipolar interactions by alignment media. The order of magnitude of these [[residual dipolar coupling]]s (RDCs) are typically of only a few rad/Hz, but do not destroy high-resolution conditions, and provide a pool of information, in particular on the orientation of molecular domains with respect to each other.
| |
| | |
| ===Dipolar truncation===
| |
| The dipolar coupling between two nuclei is inversely proportional to the cube of their distance. This has the effect that the polarization transfer mediated by the dipolar interaction is cut off in the presence of a third nucleus (all of the same kind, e.g. <sup>13</sup>C) close to one of these nuclei. This effect is commonly referred to as dipolar truncation. It has been one of the major obstacles in efficient extraction of internuclear distances, which are crucial in the structural analysis of biomolecular structure. By means of labeling schemes or pulse sequences, however, it has become possible to circumvent this problem in a number of ways.
| |
| | |
| ==Nuclear spin interactions in the solid phase==
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| <!-- Magnitude of interaction... --> | |
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| ===Chemical shielding===
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| The chemical shielding is a local property of each nucleus, and depends on the external magnetic field.
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| | |
| Specifically, the external magnetic field induces currents of the electrons in molecular orbitals. These induced currents create local magnetic fields that often vary across the entire molecular framework such that nuclei in distinct molecular environments usually experience unique local fields from this effect.
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| | |
| Under sufficiently fast [[magic angle spinning]], or in solution-state NMR, the directionally dependent character of the [[chemical shielding]] is removed, leaving the isotropic [[chemical shift]].
| |
| | |
| ===J-coupling===
| |
| The [[J-coupling]] or [[indirect nuclear spin-spin coupling]] (sometimes also called "scalar" coupling despite the fact that '''J''' is a tensor quantity) describes the interaction of nuclear spins through [[chemical bonds]].
| |
| | |
| ===Dipolar coupling===
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| ''Main article:'' [[Magnetic dipole-dipole interaction|Dipolar coupling (NMR)]]
| |
| [[Image:SSNMR dip coupl vect.png|thumb|Dipolar coupling vectors|150px|right|Dipolar coupling vectors]]
| |
| Nuclear spins exhibit a [[Nuclear magnetic moment|dipole moment]], which interacts with the dipole moment of other nuclei ([[dipolar coupling]]). The magnitude of the interaction is dependent on the spin species, the internuclear distance, and the orientation of the vector connecting the two nuclear spins with respect to the external magnetic field ''B'' (see figure). The maximum dipolar coupling is given by the dipolar coupling constant ''d'',
| |
| : <math> d = \frac{\hbar \mu_0}{4 \pi} \frac{\gamma_1 \gamma_2}{r^3} </math>, | |
| where r is the distance between the nuclei, and γ<sub>1</sub> and γ<sub>2</sub> are the [[gyromagnetic ratio]]s of the nuclei. In a strong magnetic field, the dipolar coupling depends on the orientation of the internuclear vector with the external magnetic field by
| |
| : <math>D \propto 3\cos^2\theta - 1</math>.
| |
| Consequently, two nuclei with a dipolar coupling vector at an angle of θ<sub>m</sub>=54.7° to a strong external magnetic field, which is the angle where D becomes zero, have zero dipolar coupling. θ<sub>m</sub> is called the [[magic angle]]. One technique for removing dipolar couplings, at least to some extent, is [[magic angle spinning]].
| |
| | |
| ===Quadrupolar interaction===
| |
| Nuclei with a spin greater than one-half have a non spherical charge distribution. This is known as a quadrupolar nucleus. A non spherical charge distribution can interact with an electric field gradient caused by some form of non-symmetry (e.g. in a trigonal bonding atom there are electrons around it in a plane, but not above or below it) to produce a change in the energy level in addition to the [[Zeeman effect]]. The quadrupolar interaction is the largest interaction in NMR apart from the Zeeman interaction and they can even become comparable in size.
| |
| Due to the interaction being so large it can not be treated to just the first order, like most of the other interactions. This means you have a first and second order interaction, which can be treated separately. The first order interaction has an angular dependency with respect to the magnetic field of <math>(3\cos^2\theta - 1)</math> (the P2 [[Legendre polynomial]]), this means that if you spin the sample at <math>\theta = \arctan \sqrt{2}</math> (~54.74°) you can average out the first order interaction over one rotor period (all other interactions apart from Zeeman, Chemical shift, paramagnetic and J coupling also have this angular dependency). However, the second order interaction depends on the P4 Legendre polynomial, which has zero points at 30.6° and 70.1°. These can be taken advantage of by either using DOR (DOuble angle Rotation) where you spin at two angles at the same time, or [http://www.sciencedirect.com/science/article/pii/S109078070700198X DAS (Double Angle Spinning)] where you switch quickly between the two angles. Specialized hardware (probe) has been developed for such experiments. A revolutionary advance is Lucio Frydman's multiple quantum magic angle spinning (MQMAS) NMR in 1995 and it has become a routine method for obtaining high resolution solid-state NMR spectra of quadrupolar nuclei.<ref>Isotropic Spectra of Half-Integer Quadrupolar Spins from Bidimensional Magic-Angle Spinning NMR, Lucio Frydman and John S. Hardwood, ''J. Am. Chem. Soc.'', '''1995''', ''117'', 5367—5368, (1995)</ref><ref>Two-dimensional Magic-Angle Spinning Isotropic Reconstruction Sequences for Quadrupolar Nuclei , D. Massiot, B. Touzo, D. Trumeau, J. P. Coutures, J. Virlet, P. Florian and P. J. Grandinetti , ''Solid-State NMR'' , '''6''', 73 (1996)</ref> A similar method to MQMAS is satellite transisition magic angle spinning (STMAS) NMR proposed by Zhehong Gan in 2000.
| |
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| ===Other interactions===
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| Paramagnetic substances are subject to the [[Knight shift]].
| |
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| ==History==
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| ''See also:'' [[nuclear magnetic resonance]] or [[NMR spectroscopy]] articles for an account on discoveries in NMR and NMR spectroscopy in general.
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| ''History of discoveries of NMR phenomena, and the development of solid-state NMR spectroscopy:''
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| Purcell, Torrey and Pound: "nuclear induction" on <sup>1</sup>H in paraffin 1945, at about the same time Bloch ''et al.'' on <sup>1</sup>H in water.
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| ==Modern solid-state NMR spectroscopy==
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| ''Methods and techniques''
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| ===Basic example===
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| [[Image:Cross-polarization.png|thumb|Cross-polarization pulse sequence|200px|right|CP pulse sequence]]
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| A fundamental RF pulse sequence and building-block in most solid-state NMR experiments starts with cross-polarization (CP) [Waugh ''et al.'']. It can be used to enhance the signal of nuclei with a low gyromagnetic ratio (e.g. <sup>13</sup>C, <sup>15</sup>N) by magnetization transfer from nuclei with a high gyromagnetic ratio (e.g. <sup>1</sup>H), or as spectral editing method (e.g. directed <sup>15</sup>N→<sup>13</sup>C CP in protein spectroscopy). To establish magnetization transfer, the RF pulses applied on the two frequency channels must fulfill the Hartmann–Hahn condition [Hartmann, 1962]. Under MAS, this condition defines a relationship between the voltage through the RF coil and the rate of sample rotation. Experimental optimization of such conditions is one of the routine tasks in performing a (solid-state) NMR experiment.
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| CP-MAS is a basic building block of most pulse sequences in solid-state NMR spectroscopy. Given its importance, a pulse sequence employing direct excitation of <sup>1</sup>H spin polarization, followed by CP transfer to and signal detection of <sup>13</sup>C, <sup>15</sup>N) or similar nuclei, is itself often referred to as ''CP experiment'', or, in conjunction with MAS, as ''CP-MAS'' [Schaefer and Stejskal, 1976]. It is the typical starting point of an investigation using solid-state NMR spectroscopy.
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| | |
| ===Decoupling===
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| Spin interactions must be removed ([[Nuclear magnetic resonance decoupling|decoupled]]) to increase the resolution of NMR spectra and isolate spin systems.
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| | |
| A technique that can substantially reduce or remove the chemical shift anisotropy, the dipolar coupling is ''sample rotation'' (most commonly [[magic angle spinning]], but also [http://www.sciencedirect.com/science/article/pii/S109078070700198X off-magic angle spinning]).
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| | |
| ''Homonuclear RF decoupling'' decouples spin interactions of nuclei that are the same as those being detected. ''Heteronuclear RF decoupling'' decouples spin interactions of other nuclei.
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| | |
| ===Recoupling===
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| | |
| Although the broadened lines are often not desired, dipolar couplings between atoms in the crystal lattice can also provide very useful information. Dipolar coupling are distance dependent, and so they may be used to calculate interatomic distances in isotopically labeled molecules.
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| Because most dipolar interactions are removed by sample spinning, recoupling experiments are needed to re-introduce desired dipolar couplings so they can be measured.
| |
| | |
| An example of a recoupling experiment is the Rotational Echo DOuble Resonance (REDOR) experiment<ref name=REDOR>{{cite journal
| |
| |author = Gullion T., Schaefer J.
| |
| |year = 1989
| |
| |doi =
| |
| |title = Rotational-echo double-resonance NMR
| |
| |journal = J. Magn. Reson.
| |
| |volume = 81 |issue = |pages=196–200
| |
| |pmid =
| |
| |url=
| |
| }}</ref>
| |
| which also can be the basis of an [[NMR crystallography|NMR crystallographic]] study of e.g. an amorphous solid.
| |
| | |
| ===Protons in solid-state NMR===
| |
| | |
| In contrast to traditional approaches particular in protein NMR, in which the broad lines associated with protons effectively relegate this nucleus to mixing of magnetization, recent developments of hardware (very fast MAS) and reduction of dipolar interactions by deuteration have made protons as versatile as they are in solution NMR. This includes spectral dispersion in multi-dimensional experiments<ref name=Protons>{{cite journal
| |
| |author = Linser R., Fink U., Reif B.
| |
| |year = 2008
| |
| |doi =
| |
| |title = Proton-Detected Scalar Coupling Based Assignment Strategies in MAS Solid-State NMR Spectroscopy Applied to Perdeuterated Proteins.
| |
| |journal = J. Magn. Reson.
| |
| |volume = 193 |issue = |pages=89–93
| |
| |pmid =
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| |url=
| |
| }}</ref> as well as structurally valuable restraints and parameters important for studying the materials' dynamics.<ref name=Dynamics>{{cite journal
| |
| |author = Schanda, P., Meier, B. H., Ernst, M.
| |
| |year = 2010
| |
| |doi =
| |
| |title = Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
| |
| |journal = J. Am. Chem. Soc.
| |
| |volume = 132 |issue = |pages=15957–15967
| |
| |pmid =
| |
| |url=
| |
| }}</ref>
| |
| | |
| ==Applications==
| |
| | |
| ===Biology===
| |
| [[Membrane protein]]s and [[amyloid]] fibrils, the latter related to [[Alzheimer's disease]] and [[Parkinson's disease]], are two examples of application where solid-state NMR spectroscopy complements [[Protein NMR|solution-state NMR spectroscopy]] and beam diffraction methods (e.g. X-ray crystallography, electron microscopy).
| |
| | |
| ===Chemistry===
| |
| Solid-state NMR spectroscopy serves as an analysis tool in organic and inorganic chemistry. SSNMR is also a valuable tool to study local dynamics, kinetics, and thermodynamics of a variety of systems.
| |
| | |
| ==References==
| |
| <references/> | |
| | |
| ===Suggested readings for beginners===
| |
| * [http://www.enc-conference.org/portals/0/Tutorial%20Grandinetti.pdf High Resolution Solid-State NMR of Quadrupolar Nuclei] Grandinetti ENC Tutorial
| |
| * David D. Laws, Hans-Marcus L. Bitter, and Alexej Jerschow, "Solid-State NMR Spectroscopic Methods in Chemistry", Angewandte Chemie International Edition (engl.), Vol. 41, pp. 3096 (2002) {{doi|10.1002/1521-3773(20020902)41:17<3096::AID-ANIE3096>3.0.CO;2-X}}
| |
| * Levitt, Malcolm H., ''Spin Dynamics: Basics of Nuclear Magnetic Resonance'', Wiley, Chichester, United Kingdom, 2001. (NMR basics, including solids)
| |
| * Duer, Melinda J., ''Introduction to Solid-State NMR Spectroscopy'', Blackwell, Oxford, 2004. (Some detailed examples of SSNMR spectroscopy)
| |
| | |
| ===Advanced readings===
| |
| ''Books and major review articles''
| |
| | |
| * McDermott, A, [http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biophys.050708.133719 Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR] ''Annual Review of Biophysics'', v. 38, 2009.
| |
| * Mehring, M, ''Principles of High Resolution NMR in Solids'', 2nd ed., Springer, Heidelberg, 1983.
| |
| * Slichter, C. P., ''Principles of Magnetic Resonance'', 3rd ed., Springer, Heidelberg, 1990.
| |
| * Gerstein, B. C. and Dybowski, C., ''Transient Techniques in NMR of Solids'', Academic Press, San Diego, 1985.
| |
| * Schmidt-Rohr, K. and Spiess, H.-W., ''Multidimensional Solid-State NMR and Polymers'', Academic Press, San Diego, 1994.
| |
| * Dybowski, C. and Lichter, R. L., ''NMR Spectroscopy Techniques'', Marcel Dekker, New York, 1987.
| |
| * Ramamoorthy, A., ''NMR Spectroscopy of Biological Solids'', Taylor & Francis, New York, 2006.
| |
| | |
| ===General===
| |
| ''References to books and research articles''
| |
| | |
| * Andrew, E. R., Bradbury, A. and Eades, R. G., "Removal of Dipolar Broadening of Nuclear Magnetic Resonance Spectra of Solids by Specimen Rotation," Nature 183, 1802, (1959)
| |
| * Ernst, Bodenhausen, Wokaun: ''Principles of Nuclear Magnetic Resonance in One and Two Dimensions''
| |
| * Hartmann S.R., Hahn E.L., "Nuclear Double Resonance in the Rotating Frame" Phys. Rev. 128 (1962) 2042.
| |
| * Pines A., Gibby M.G., Waugh J.S., "Proton-enhanced NMR of dilute spins in solids" J. Chem. Phys. 59, 569-90, (1973)
| |
| * Purcell, Torrey and Pound (1945).
| |
| * Schaefer, J. and Stejskal, E. O., "Carbon-13 Nuclear Magnetic Resonance of Polymers Spinning at the Magic Angle," Journal of the American Chemical Society 98, 1031 (1976).
| |
| *Gullion, T. and Schaefer, J., "Rotational-Echo, Double-Resonance NMR," J. Magn. Reson., 81, 196 (1989).
| |
| *MacKenzie, K.J.D and Smith, M.E. "Multinuclear Solid-State NMR of Inorganic Materials", Pergamon Materials Series Volume 6, Elsevier, Oxford 2002.
| |
| | |
| ==External links==
| |
| * [http://ssnmr.blogspot.com/ SSNMRBLOG] Solid-State NMR Literature Blog by Prof. Rob Schurko's Solid-State NMR group at the University of Windsor
| |
| * [http://www.ssnmr.org www.ssnmr.org] Rocky Mountain Conference on Solid-State NMR
| |
| * [http://mrsej.ksu.ru http://mrsej.ksu.ru] Magnetic Resonance in Solids. Electronic Journal
| |
| [[Category:Nuclear magnetic resonance]]
| |
| [[Category:Scientific techniques]]
| |
Migrаines are far more than јust a heɑdache, and can be quite debilitating, particularly if they ocϲur frequeոtly.
As well as the throbbing, pulsatiոg pain – usually focused in one area of the head – աhich is awful in itself, migraines alѕo lead to bluгred vision, floaters in the eyeѕ, disruption to other seոses suсh aѕ ringing iո the ears, taste and smell sensitivities, aոd even tunnel vision or temporary loss of vision.
For many people medication can reduce, or even stop, the symptoms – Ьut theгe are mɑny fоods which have been identified as possible triggeгs for migraines, aոd avoidinǥ these fooԁs can mean fгeedom from the deƅilitating аnd agonizing pain of a mіgraіne.
Wɦat foods can cause migraines?
1: tyramіne or phenylethylamine.
If you have any kind of inquiriеs relating to where and ways to use find a neurologist, yoս could call uѕ at our own webpage. These naturally occurring amino acids are found in chocolate, aged cheеses, vinegar and citrus fruits.
These can be found iո higher quantities in fooԀ that has been improperly stored, or leftovers, іn comparisoո tߋ fresh foods.
How to avoid this trіgger:
If you are goіոg to have foods with these amino acids try to opt for fresh options over anything tɦat has been storeԀ for any period of time.
2: Alcohol.
In part this is due to alcoҺol being a diuretic and causing dehydration, which leads to Һeadaches. Eveո a small amount of alcoɦol cаn be enough to cause the first symptoms.
How to avoid this trigger:
If you are going to driոk alcohol alterոate every alcoholic drink with а soft drink; water is best. Staying hydratеd can stave off the worst of the hangover or potential migraіne.
3: Nitrites.
These are used as additives in maոy meat products – a pгeservative that also enhаnces flavor, nitrites are found in hot dogs, jerky, deli meats and sаusages as well as many other cuгed foods ɑnd pickled or caոned foods.
How to ɑvoіd this trigger:
There are ոitrite free options of many of tҺеse foods so you don’t have to do without your favorites, just check the labelѕ carefսlly when you’re shoρping.
4: Tannins.
Tanniոs are found in tea (most varieties of green and black tea, specifically) apples and peaгs, ɑոd grapes – meaning they’re also found iո apple juices, сiders and wines.
How to avoid thiѕ triggeг:
Avߋіd drinks with tannins in and instead choose herbal teas and water rather than these fruit juices.
5: Sulfites
These are found in many dried fruits, things like dried apricօts, fiɡs and pгunes) and wines, as well as many processed foods.
How to avoіd this trigցer:
Choose fresh fruit over dried fruit, and prepare meals from fгesh ingredients.
6: MЅG
This is an additivе used for flavoгing, often found in Аsian foods, ɑnd haѕ bеen linked – alonɡ with some other additives – to migraines.
Hօw to avoid this trigger:
Many places now state on their menu whether they use MSG, it has become unpopular due to the health coոnections in recent times – ask if you’re unsure, and choose meals without this additive.
7: Aspartame
This well known, and commonlƴ used, artificial sweetener is found in mаny ‘diet’ or ‘low fat’ foods and drinkѕ – particularly diet soda.
Hoա to aѵоid this tгigger:
Either choose the full fat version of your ѕoda – or, better, avoid soda drinks altogether. Opt for smaller գuantities of the ‘fat’ versioո of the foods you ϲҺoose гather than the ‘diet’ versiߋn.
8: Caffeine
Found іn coffee, tea, soda and a wide range of otҺer Ƅeveragеs, caffeine іs somеthing we all take for gгanted to give us a little pep - Ьut even small amounts can be a trigger if you’re prone to migraines.
How to ɑvoid this trigger:
Choosе decaff or Һerbal teas in plaсe of caffеinated versions, and drink water in place of your usual soda.
9: Pâté
Pâté – or other foodѕ made with liver or other organs – can lead to migraines in some caѕes.
How tο avoid this trigger:
Don’t eat any food that is made from organ meаt or offal.
10: Dairy pгoducts
Sߋսred cream, buttermilk and a range of other Ԁairy products can lеad to migraine.
How to avoіd this trigger:
Look for dairy alternɑtives in your supermarket.