Document Detail

Rapid measurement of 3J(H N-H alpha) and 3J(N-H beta) coupling constants in polypeptides.
MedLine Citation:
PMID:  17914658     Owner:  NLM     Status:  MEDLINE    
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.
Ravi Pratap Barnwal; Ashok K Rout; Kandala V R Chary; Hanudatta S Atreya
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-10-04
Journal Detail:
Title:  Journal of biomolecular NMR     Volume:  39     ISSN:  0925-2738     ISO Abbreviation:  J. Biomol. NMR     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-11-02     Completed Date:  2008-01-18     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9110829     Medline TA:  J Biomol NMR     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  259-63     Citation Subset:  IM    
Department of Chemical Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India.
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MeSH Terms
Hydrogen / chemistry
Hydrogen Bonding
Nitrogen / chemistry
Nuclear Magnetic Resonance, Biomolecular*
Peptides / chemistry*
Protein Folding
Reg. No./Substance:
0/Peptides; 1333-74-0/Hydrogen; 7727-37-9/Nitrogen

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