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

Ravi Pratap Barnwal; Ashok K Rout; Kandala V R Chary; Hanudatta S Atreya

doi:10.1007/s10858-007-9200-8

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

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

Institute of Chemistry and Metabolomics

Tata Institute of Fundamental Research

29 Citations (Scopus)

Abstract

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 of G-matrix Fourier transform NMR spectroscopy and quantitative J-correlation. These experiments, which facilitate fast acquisition of three-dimensional data with high spectral/digital resolution and chemical shift dispersion, will provide renewed opportunities to utilize them for sequence specific resonance assignments, estimation/characterization of secondary structure with/without prior knowledge of resonance assignments, stereospecific assignment of prochiral groups and 3D structure determination, refinement and validation. Taken together, these experiments have a wide range of applications from structural genomics projects to studying structure and folding in polypeptides.

Original language	English
Journal	Journal of Biomolecular NMR
Volume	39
Issue number	4
Pages (from-to)	259-63
Number of pages	5
ISSN	0925-2738
DOIs	https://doi.org/10.1007/s10858-007-9200-8
Publication status	Published - 12.2007

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title = "Rapid measurement of 3J(H N-H alpha) and 3J(N-H beta) coupling constants in polypeptides",

abstract = "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 of G-matrix Fourier transform NMR spectroscopy and quantitative J-correlation. These experiments, which facilitate fast acquisition of three-dimensional data with high spectral/digital resolution and chemical shift dispersion, will provide renewed opportunities to utilize them for sequence specific resonance assignments, estimation/characterization of secondary structure with/without prior knowledge of resonance assignments, stereospecific assignment of prochiral groups and 3D structure determination, refinement and validation. Taken together, these experiments have a wide range of applications from structural genomics projects to studying structure and folding in polypeptides.",

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T1 - Rapid measurement of 3J(H N-H alpha) and 3J(N-H beta) coupling constants in polypeptides

AU - Barnwal, Ravi Pratap

AU - Rout, Ashok K

AU - Chary, Kandala V R

AU - Atreya, Hanudatta S

PY - 2007/12

Y1 - 2007/12

N2 - 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 of G-matrix Fourier transform NMR spectroscopy and quantitative J-correlation. These experiments, which facilitate fast acquisition of three-dimensional data with high spectral/digital resolution and chemical shift dispersion, will provide renewed opportunities to utilize them for sequence specific resonance assignments, estimation/characterization of secondary structure with/without prior knowledge of resonance assignments, stereospecific assignment of prochiral groups and 3D structure determination, refinement and validation. Taken together, these experiments have a wide range of applications from structural genomics projects to studying structure and folding in polypeptides.

AB - 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 of G-matrix Fourier transform NMR spectroscopy and quantitative J-correlation. These experiments, which facilitate fast acquisition of three-dimensional data with high spectral/digital resolution and chemical shift dispersion, will provide renewed opportunities to utilize them for sequence specific resonance assignments, estimation/characterization of secondary structure with/without prior knowledge of resonance assignments, stereospecific assignment of prochiral groups and 3D structure determination, refinement and validation. Taken together, these experiments have a wide range of applications from structural genomics projects to studying structure and folding in polypeptides.

U2 - 10.1007/s10858-007-9200-8

DO - 10.1007/s10858-007-9200-8

M3 - Journal articles

C2 - 17914658

SN - 0925-2738

VL - 39

SP - 259

EP - 263

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 4

ER -

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

Abstract

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