1. PROTEIN NMR SPECTROSCOPY
Roll no 11011514-031
Afifa hameed
Sec “G”

2. INTRODUCTION
 most commonly known as NMR spectroscopy, is a research
technique that exploits the magnetic properties of certain
atomic nuclei.
 It 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 provide detailed information about the structure,
dynamics, reaction state, and chemical environment of
molecules.
 A spectroscopic technique that gives us information about the
number and types of atoms in a molecule.
 Nuclear magnetic resonance spectroscopy is a powerful
analytical technique used to characterize organic molecules by
identifying carbon-hydrogen frameworks within molecules.

3. Nuclear Magnetic Resonance
In the
Nucleus

4.  Most frequently, NMR spectroscopy is used by
chemists and biochemists to investigate the
properties of organic molecules.
history
 experimentally observed in late 1945
 simultaneously by the research groups of Felix
Bloch, at Stanford University and Edward Purcell at
Harvard University.
 Bloch and Purcell were jointly awarded the Nobel
Prize in Physics in 1952 for their discovery of
Nuclear Magnetic Resonance.

6. COMPONENTS.
 A magnet
 Sample and sample holder
 Radiofrequency generator
 Detector
 Recorder

7.  Types
 Two common types of NMR spectroscopy are used
to characterize organic structure.
 1) 1H NMR: is used to determine the type and
number of H atoms in a molecule.
 2) 13C NMR is used to determine the type of carbon
atoms in the molecule.

8. PROCEDURE
 The sample is dissolved in a solvent (CCl4, CDCl3 )
 The sample is in a small cylindrical glass tube b/w two poles of
magnet.
 sample is spun around the axis .
 Between gaps of poles a coil that attach Rf generator that
provide electromagnetic energy and change spin orientation.
 Perpendicular to the RF oscillator coil is a detector coil.
 When sample absorbs energy, however, the reorientation of the
nuclear spins induces a radiofrequency signal in the plane of the
detector coil.
 the typical NMR spectrometer uses a constant frequency RF-
signal and varies the magnetic field strength.
 magnetic field strength is increased, the processional frequency
of all the protons increase.
 As the field strength is increased linearly, a pen travels across a
recording chart.

10. APPLICATIONS
 In chemistry:
 study chemical bonds.
 two dimensional approaches used to study complex molecules.
 used to study chemical bonds.
 In medical
 I n BRAIN Distinguishing gray matter & white matter and detect tumors.
 In ABDOMEN Metabolic liver disease detect by NMR.
 Measures liver iron over load in hemochrtosisoma
 In KIDNEYS Distinguishing renal cortex & medulla To evaluate transplanted
kidney.
 In HEART Tomographic images of heart muscle, chambers, valvular
structures.
 In BREAST 3D-NMR & single-slice planar imaging in detecting breast
abnormalities.
 In MUSCULO SKELETAL SYSTEM
 Demonstrates Osteomyelitis, tumor metastasis in vertebral bodies & pelvic
bones.
 Provide Images of muscles, tendons, ligaments

11.  NMR IN PHARMACEUTICAL RESEARCH
 Leading technology for 3-D structure determination of bio-
macromolecules
 Studying protein structure
 SAR by NMR – Novel lead compounds
 Chemical shift mapping – Structural information on the
binding modes and site positions
 Molecular dynamics, conformational analysis
 Benefits

 Eliminates risk of x-radiation
 Excellent spatial & contrast resolution
 Detecting diseases at earlier stages