Rapid measurement of 3J(H N-H alpha) and 3J(N-H beta) coupling constants in polypeptides.
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.
Barnwal
Ravi Pratap
RP
Department of Chemical Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India.
Rout
Ashok K
AK
Chary
Kandala V R
KV
Atreya
Hanudatta S
HS
D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D009584:Nitrogen / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D010455:Peptides; D006859:Hydrogen; D009584:Nitrogen