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Determination of Structures of Proteins in Solution using Nuclear Magnetic Resonance

Sarma, Siddhartha P (2003) Determination of Structures of Proteins in Solution using Nuclear Magnetic Resonance. In: Resonance: Journal of Science Education, 8 (8). pp. 86-99.

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Abstract

Nuclear magnetic resonance (NMR) is a manifestation of an intrinsic property of the nucleus, i.e. nuclear spin angular momentum. Spin angular momentum gives rise to magnetic moments. Thus, nuclei that possess net magnetic moments behave like very small bar magnets. NMR spectroscopy involves the study of the behaviour of these nuclei under suitable conditions. Analogous to other forms of spectroscopy, nuclear magnetic resonance (NMR) results from absorption of electromagnetic radiation that causes transitions between nuclear spin energy states. Absorption of radiation occurs in the radio frequency region of the electromagnetic spectrum. Not all isotopes of the elements in the periodic table possess nuclei that are ‘NMR active’. What this means is that several nuclei possess zero nuclear magnetic moments in the ground state. This is a property that is difficult to predict. Certain empirical rules exist by which one can predict which elements possess net nuclear magnetic moments and which do not. For the present we will restrict ourselves to commonly occuring nuclei that possess a nuclear spin quantum number of ½, viz., $^1H$, $^{13}C$, $^{15}N$, $^{19}F$ and $^{31}P$.

Item Type: Journal Article
Additional Information: The Copyright belongs to Indian Academy of Sciences.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 16 May 2006
Last Modified: 19 Sep 2010 04:26
URI: http://eprints.iisc.ernet.in/id/eprint/6691

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