Infrared Spectroscopy

1. Introduction As noted in a previous chapter, the light our eyes see is but a small part of a broad spectrum of electromagnetic radiation. On the immediate high energy side of the visible spectrum lies the ultraviolet, and on the low energy side is the infrared. The portion of the infrared region most useful for analysis of organic compounds is not immediately adjacent to the visible spectrum, but is that having a wavelength range from 2,500 to 16,000 nm, with a corresponding frequency range from 1.9*1013 to 1.2*1014 Hz.

Photon energies associated with this part of the infrared (from 1 to 15 kcal/mole) are not large enough to excite electrons, but may induce vibrational excitation of covalently bonded atoms and groups. The covalent bonds in molecules are not rigid sticks or rods, such as found in molecular model kits, but are more like stiff springs that can be stretched and bent. The mobile nature of organic molecules was noted in the chapter concerning conformational isomers. We must now recognize that, in addition to the facile rotation of groups about single bonds, molecules experience a wide variety of vibrational motions, characteristic of their component atoms. Consequently,
1|Page

virtually all organic compounds will absorb infrared radiation that corresponds in energy to these vibrations. Infrared spectrometers, similar in principle to the UV-Visible spectrometer described elsewhere, permit chemists to obtain absorption spectra of compounds that are a unique reflection of their molecular structure. An example of such a spectrum is that of the flavoring agent vanillin, shown below.

The complexity of this spectrum is typical of most infrared spectra, and illustrates their use in identifying substances. The gap in the spectrum between 700 & 800 cm-1 is due to solvent (CCl4) absorption. Further analysis (below) will show that this spectrum also indicates the presence of an aldehyde function, a phenolic hydroxyl and a substituted benzene ring. The inverted display of absorption, compared with UV-Visible spectra, is

2|Page

characteristic. Thus a sample that did not absorb at all would record a horizontal line at 100% transmittance (top of the chart).

Nuclear magnetic resonance Spectroscopy

Nuclear magnetic resonance (NMR) is a property that magnetic nuclei have in a magnetic field and applied electromagnetic (EM) pulse or pulses, which cause the nuclei to absorb energy from the EM pulse and radiate this energy back out. The energy radiated back out is at a specific resonance frequency which depends on the strength of the magnetic field and other factors. This allows the observation of specific quantum mechanical magnetic properties of an atomic nucleus. Many scientific techniques exploit NMR phenomena to study molecular physics, crystals and non-crystalline materials through NMR spectroscopy. NMR is also routinely used in advanced medical imaging techniques, such as in magnetic resonance imaging (MRI). All stable isotopes that contain an odd number of protons and/or of neutrons (see Isotope) have an intrinsic magnetic moment and angular momentum, in other words a nonzero spin, while all nuclides with even numbers of both have spin 0. The most commonly studied nuclei are 1H (the most NMRsensitive isotope after the radioactive 3H) and isotopes of many other elements (e.g. 2H,
29 10 13

C, although nuclei from

14

B,

11

B,

N,

15

N,

17

O,

19

F,

23

Na,

Si, 31P, 35Cl, 113Cd, 129Xe, 195Pt) are studied by high-field NMR spectroscopy

as well.
3|Page

A key feature of NMR is that the resonance frequency of a particular substance is directly proportional to the strength of the applied magnetic field. It is this feature that is exploited in imaging techniques; if a sample is placed in a non-uniform magnetic field then the resonance frequencies of the sample's nuclei depend on where in the field they are located. Since the resolution of the imaging technique depends on the magnitude of magnetic field gradient, many efforts are made to develop increased field strength, often using superconductors. The effectiveness of NMR can also be improved using hyperpolarization, and/or using two-dimensional, three-dimensional and higher-dimensional multi-frequency techniques. The principle of NMR usually involves two sequential steps: The alignment (polarization) of the magnetic nuclear spins in an applied, constant magnetic field H0. The perturbation of this alignment of the nuclear spins by employing an electro-magnetic, usually radio frequency (RF) pulse. The required perturbing frequency is dependent upon the static magnetic field (H0) and the nuclei of observation. The two fields are usually chosen to be perpendicular to each other as this maximizes the NMR signal strength. The resulting response by the total magnetization (M) of the nuclear spins is the phenomenon that is exploited in NMR spectroscopy and magnetic resonance imaging. Both use intense
4|Page

applied magnetic fields (H0) in order to achieve dispersion and very high stability to deliver spectral resolution, the details of which are described by chemical shifts, the Zeeman effect, and Knight shifts (in metals). NMR phenomena are also utilized in low-field NMR, NMR spectroscopy and MRI in the Earth's magnetic field (referred to as Earth's field NMR), and in several types of magnetometers.

Applications of NMR Medicine

Medical MRI The application of nuclear magnetic resonance best known to the general public is magnetic resonance imaging for medical diagnosis and MR Microscopy in research settings, however, it is also widely used in chemical studies, notably in NMR spectroscopy such as proton NMR, carbon-13 NMR, deuterium NMR and phosphorus-31 NMR. Biochemical information can also
5|Page

be obtained from living tissue (e.g. human brain tumors) with the technique known as in vivo magnetic resonance spectroscopy or chemical shift NMR Microscopy. These studies are possible because nuclei are surrounded by orbiting electrons, which are charged particles that generate small, local magnetic fields that add to or subtract from the external magnetic field, and so will partially shield the nuclei. The amount of shielding depends on the exact local environment. For example, a hydrogen bonded to an oxygen will be shielded differently than a hydrogen bonded to a carbon atom. In addition, two hydrogen nuclei can interact via a process known as spin-spin coupling, if they are on the same molecule, which will split the lines of the spectra in a recognizable way. As one of the two major spectroscopic techniques used in metabolomics, NMR is used to generate metabolic fingerprints from biological fluids to obtain information about disease states or toxic insults.

6|Page

Aspirin
In the Aspirin lab, we are vitally interested in predicting the IR absorptions due participate actively the carbonyl, C=O, and hydroxyl, OH, functional groups at a rate of around 1700 cm-1

7|Page

8|Page

1 H NMR spectra in behalf of aspirin are shown in figures 3 and 4, respectively. Aspirin, w. nine profoundly different carbons produces fundamentally different 13 C NMR spectrum w. nine deeply personal

9|Page

Intro Aspirin is among the the vast majority versatile hard drugs well-known participate actively strong medicine, and is among Aspirin is found in any more than 100 common medications (Anacin,

1H NMR Spectroscopy in behalf of CHM 222L Professor: S. Bruce King | Programming** Select one:**, Aspirin, 1-Bromopentane, 2-Chlorobutane, Ethyl Acetate

10 | P a g e

The 5 peaks produce have the planned chemical sh The 5 peaks produce have the the subsequent chemical profound shifts in ppm: 11, 8.125, 7.624, 7.356, 7.142 and 2.352. TRIZIVIR contains 3 nucleoside Acetaminophen Nmr aspirin spectrum of Caffeine complete information caplet 2 caplets may weighty quite alive.

11 | P a g e

Altace

Capsules

are

present

12 | P a g e

References
www.wikipedia.org www.pubmed.net www.drug.com www.tutorvista.com

13 | P a g e