2012
DOI: 10.1007/s10969-012-9144-4
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A unified NMR strategy for high-throughput determination of backbone fold of small proteins

Abstract: An efficient semi-automated strategy called PFBD (i.e. Protein Fold from Backbone Data only) has been presented for rapid backbone fold determination of small proteins. It makes use of NMR parameters involving backbone atoms only. These include chemical shifts, amide-amide NOEs and H-bonds. The backbone chemical shifts are obtained in an automated manner from the orthogonal 2D projections of variants of HNN and HN(C)N experiments (Kumar et al., in Magn Reson Chem 50(5):357-363, 2012) using AUTOBA (Borkar et al… Show more

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Cited by 3 publications
(3 citation statements)
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“…The chemical shift assignments of backbone 13 C α and 13 C resonances were used to derive the secondary structure information about the protein. For this, the residue‐wise cumulative secondary shifts were calculated as per Equation : normalΔδCUM=normalΔδ()Cα25+normalΔδ()C'10, …”
Section: Methods and Experimentsmentioning
confidence: 99%
“…The chemical shift assignments of backbone 13 C α and 13 C resonances were used to derive the secondary structure information about the protein. For this, the residue‐wise cumulative secondary shifts were calculated as per Equation : normalΔδCUM=normalΔδ()Cα25+normalΔδ()C'10, …”
Section: Methods and Experimentsmentioning
confidence: 99%
“…Recent years have witnessed a major upsurge in this direction, first, to develop methods for rapid data acquisition; [1][2][3][4][5][6][7][8] second, to develop automated algorithms for rapid data analysis; [9][10][11][12][13][14] third, to develop strategies that require minimal experimentation without sacrificing information; [15][16][17][18][19][20][21] and, fourth, to develop new ideas of structure calculation with minimum of experimental inputs (CS-ROSETTA, [22,23] CS23D, [24] GENMR, [25] etc. ), to list some of the ongoing efforts.…”
Section: Introductionmentioning
confidence: 99%
“…Following sequence-specific backbone assignment, the 13 C  and 13 C' chemical shifts are used to obtain the secondary structural information about the protein using the routine chemical shift index (CSI) method [25][26][27]. Overall, this whole exercise including data collection and data analysis can be accomplished in 1-3 days depending upon the size, concentration, and the conformational state (folded/unfolded) of the protein in solution.…”
Section: Introductionmentioning
confidence: 99%