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Journal of Postgraduate Medicine
Medknow Publications and Staff Society of Seth GS Medical College and KEM Hospital, Mumbai, India
ISSN: 0022-3859
EISSN: 0022-3859
Vol. 48, No. 1, 2002, pp. 83-87
Bioline Code: jp02029
Full paper language: English
Document type: Research Article
Document available free of charge

Journal of Postgraduate Medicine, Vol. 48, No. 1, 2002, pp. 83-87

 en Technology Review - Structure Determination of Proteins in Solution by Nuclear Magnetic Resonance Spectroscopy
Chary KVR, Atreya HS

Abstract

Each cell in the human body consists of a myriad of biological macromolecules and organelles, which are required for various cellular functions and metabolism. A key component in such a system comprises of proteins, which play a crucial role in proper functioning of the cell. There are an estimated 100,000 different proteins present in the human body.1 The activity of a protein molecule inside the cell is indirectly governed by the overall fold of the individual polypeptide chains, or in other words, their three dimensional (3D) structures in space.2 Thus, the knowledge of the 3D structure of a given protein is most essential for a complete understanding of its function inside the cell. Many diseases in humans such as Alzheimers', Parkinsons', Prion disease, Cystic fibrosis, cancers etc. are attributed as the result of malfunctioning of proteins.1 Further, knowledge of the 3D structure of a protein, involved in a disease, is eventually used in designing its target drugs. Such a sphere of activity is popularly called as quantitative structure activity relationship (QSAR).3

 
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