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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/117/01/0003-0021

    • Keywords

       

      Unfolded proteins; NMR; high throughput procedures

    • Abstract

       

      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.

    • Author Affiliations

       

      Amarnath Chatterjee1 Ashutosh Kumar1 Jeetender Chugh1 Sudha Srivastava1 Neel S Bhavesh1 Ramakrishna V Hosur1

      1. Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai - 400 005, India
    • Dates

       
  • Journal of Chemical Sciences | News

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