Scientific Commons: Hanudatta S. Atreya

CSSI-PRO: a method for secondary structure type editing, assignment and estimation in proteins using linear combination of backbone chemical shifts (2009)

Swain, Monalisa, Atreya, Hanudatta S

Estimation of secondary structure in polypeptides is important for studying their structure, folding and dynamics. In NMR spectroscopy, such information is generally obtained after sequence specific...

Chemical shift based editing of CH3 groups in fractionally $^{13}C$-labelled proteins using GFT (3,2)D CT-HCCH-COSY: stereospecific assignments of $CH_3$ groups of Val and Leu residues (2008)

Barnwal, Ravi Pratap, Atreya, Hanudatta S, Chary, Kandala VR

We propose a (3,2)D CT-HCCH-COSY experiment to rapidly collect the data and provide significant dispersion in the spectral region containing $^13$C-$1^H$ cross peaks of $CH_3$ groups belonging to...

Identification of C-terminal neighbours of amino acid residues without an aliphatic $^{13}C^\gamma$ as an aid to NMR assignments in proteins (2008)

Barnwal, Ravi Pratap, Rout, Ashok K, Atreya, Hanudatta S, Chary, Kandala VR

We propose a methodology that uses GFT (3,2)D CB(CACO)NNH experiment to rapidly collect the data and readily identify six amino acid residue types (Ala, Asn, Asp, Cys, Gly and Ser) in any given...

Rapid measurement of $^3J(H^N-H^\alpha)$ and $^3J(N-H^\beta)$ coupling constants in polypeptides (2007)

Barnwal, Ravi Pratap, Rout, Ashok K, Chary, Kandala VR, Atreya, Hanudatta S

We present two NMR experiments, (3,2)D HNHA and (3,2)D HNHB, for rapid and accurate measurement of $(^3J(H^N-H^\alpha)$ and $^3J(N-H^\beta)$ coupling constants in polypeptides based on the principle...

The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold (2004)

Herve Du Penhoat, Catherine, Atreya, Hanudatta S., Shen, Yang, Liu, Gaohua, Acton, Thomas B., Xiao, Rong, ...

The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal protein S27e. Here, we present the high-quality NMR solution structure of this archaeal protein, which comprises a C4 zinc finger...

Structural basis for sequential displacement of Ca2+ by Yb3+ in a protozoan EF-hand calcium binding protein (2003)

Atreya, Hanudatta S., Mukherjee, Sulakshana, Chary, Kandala V.R., Lee, Yong-Min, Luchinat, Claudio

We have studied the displacement of Ca2+by the trivalent lanthanide ions (Yb3+) in a protozoan (Entamoeba histolytica) Ca2+-binding protein (EhCaBP), by NMR and thermodynamics. We have demonstrated,...

G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment

Atreya, Hanudatta S., Szyperski, Thomas

A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented here rapidly affords four-, five-, or...

NMR data collection and analysis protocol for high-throughput protein structure determination

Liu, Gaohua, Shen, Yang, Atreya, Hanudatta S., Parish, David, Shao, Ying, Sukumaran, Dinesh K., ...

A standardized protocol enabling rapid NMR data collection for high-quality protein structure determination is presented that allows one to capitalize on high spectrometer sensitivity: a set of five...