• Ramakrishna V Hosur

      Articles written in Journal of Chemical Sciences

    • NMR of unfolded proteins

      Amarnath Chatterjee Ashutosh Kumar Jeetender Chugh Sudha Srivastava Neel S Bhavesh Ramakrishna V Hosur

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      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.

    • Generation of serine/threonine check points in HN(C)N spectra

      Dinesh Kumar Jeetender Chugh Ramakrishna V Hosur

      More Details Abstract Fulltext PDF

      We describe here a simple modification of the HN(C)N experiment for the generation of serine/threonine check points in the three-dimensional experiment. The various `triplet of residue’ specific peak patterns in the spectra are documented for ease of analysis and sequential backbone resonance assignment. The performance of this experiment, referred to as HN(C)N-ST, is demonstrated using two proteins, one properly folded and the other completely denatured. It is noteworthy that, even in the denatured protein, where spectral dispersions are rather poor, about 90% of the sequential connectivities through the chain could be established from this single experiment. This would have great implications for structural genomics efforts.

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