NMR of unfolded proteins

Chatterjee, Amarnath ; Kumar, Ashutosh ; Chugh, Jeetender ; Srivastava, Sudha ; Bhavesh, Neel S. ; Hosur, Ramakrishna V. (2005) NMR of unfolded proteins Journal of Chemical Sciences, 117 (1). pp. 3-21. ISSN 0253-4134

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Official URL: http://www.ias.ac.in/chemsci/Pdf-Jan2005/3.pdf

Related URL: http://dx.doi.org/10.1007/BF02704356


In the post-genomic era, as more and more genome sequences are becoming known and hectic efforts are underway to decode the information content in them, it is becoming increasingly evident that flexibility in proteins plays a crucial role in many of the biological functions. Many proteins have intrinsic disorder either wholly or in specific regions. It appears that this disorder may be important for regulatory functions of the proteins, on the one hand, and may help in directing the folding process to reach the compact native state, on the other. Nuclear magnetic resonance (NMR) has over the last two decades emerged as the sole, most powerful technique to help characterize these disordered protein systems. In this review, we first discuss the significance of disorder in proteins and then describe the recent developments in NMR methods for their characterization. A brief description of the results obtained on several disordered proteins is presented at the end.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Unfolded Proteins; NMR; High Throughput Procedures
ID Code:16640
Deposited On:15 Nov 2010 13:31
Last Modified:17 May 2016 01:22

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