Electronics Corporation of India Limited

About: Electronics Corporation of India Limited is a government organization based out in Hyderabad, India. It is known for research contribution in the topics: Atomic absorption spectroscopy & Encryption. The organization has 93 authors who have published 75 publications receiving 1059 citations.

Rho-dependent Transcription Termination: More Questions than Answers

Abstract: Escherichia coli protein Rho is required for the factor-dependent transcription termination by an RNA polymerase and is essential for the viability of the cell. It is a homohexameric protein that recognizes and binds preferably to C-rich sites in the transcribed RNA. Once bound to RNA, it utilizes RNA-dependent ATPase activity and subsequently ATPase-dependent helicase activity to unwind RNA-DNA hybrids and release RNA from a transcribing elongation complex. Studies over the past few decades have highlighted Rho as a molecule and have revealed much of its mechanistic properties. The recently solved crystal structure could explain many of its physiological functions in terms of its structure. Despite all these efforts, many of the fundamental questions pertaining to Rho recognition sites, differential ATPase activity in response to different RNAs, translocation of Rho along the nascent transcript, interactions with elongation complex and finally unwinding and release of RNA remain obscure. In the present review we have attempted to summarize "the knowns" and "the unknowns" of the Rho protein revealed by the recent developments in this field. An attempt has also been made to understand the physiology of Rho in the light of its phylogeny.

The utility of a W–Ir permanent chemical modifier for the determination of Ni and V in emulsified fuel oils and naphtha by transverse heated electrothermal atomic absorption spectrometer

Abstract: A ‘water in oil’ emulsification procedure has been applied to a transverse heated electrothermal atomic absorption spectrometer (TH-ETAAS) for direct determination of Ni and V in petroleum products such as naphtha, NIST SRM 1618 Residual Oil and NIST SRM 1634c Residual Fuel Oil. The utility of permanent chemical modifiers such as W, W–Rh and W–Ir, has been examined in determining these elements. The furnace with an integrated platform coated with W and Ir was found to provide 25–30% improved sensitivity than other coatings for Ni. In the case of V, a pyrocoated tube with an integrated platform was found to give the best results. The W–Ir coated tube could be used for nearly 400 firings. The limit of detection for naphtha emulsion was 0.002 and 0.006 µg g−1 for Ni and V, respectively, indicating that the method is well suited for matrices containing very low concentration of trace elements. The method can also be applied to dense matrices such as SRMs Residual Oil and Residual Fuel Oil. In this case, the limit of detection was 0.1 µg g−1 for Ni and 0.5 µg g−1 for V with a precision of less than 5%.

Exploiting 3D structural templates for detection of metal-binding sites in protein structures.

Abstract: High throughput structural genomics efforts have been making the structures of proteins available even before their function has been fully characterized. Therefore, methods that exploit the structural knowledge to provide evidence about the functions of proteins would be useful. Such methods would beneeded to complement the sequence-based function annotation approaches. The current study describes generation of 3D-structural motifs for metal-binding sites from the known metalloproteins. It then scans all the available protein structures in the PDB database for putative metal-binding sites. Our analysis predicted more than 1000 novel metal-binding sites in proteins using three-residue templates, and more than 150 novel metal-binding sites using four-residue templates. Prediction of metal-binding site in a yeast protein YDR533c led to the hypothesis that it might function as metal-dependent amidopeptidase. The structural motifs identified by our method present novel metal-binding sites that reveal newer mechanisms for a few well-known proteins. Proteins 2008. © 2007 Wiley-Liss, Inc.