Related Articles31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dihydrofolate reductase based on two-dimensional 1H-31P-heteronuclear and 1H-detected 1H-31P-shift-correlation experiments.
For any detailed NMR conformational study of a protein-ligand complex it is essential to have specific resonance assignments. We have now assigned the pyrophosphate 31P resonances in spectra of NADPH bound to Lactobacillus casei dihydrofolate reductase (DHFR) by using a combination of 1H-31P-heteronuclear shift-correlation (HETCOR), 1H-31P-heteronuclear multiple-quantum-coherence correlation spectroscopy (HMQC-COSY), 1H-1H COSY, homonuclear Hartmann-Hahn (HOHAHA) and NOE spectroscopy (NOESY) experiments. The nicotinamide pyrophosphate phosphorus, P(n), has been unequivocally assigned to a signal (-14.07 ppm) which shows a large 3JP-O-C-H coupling constant. Such a coupling constant when combined with the appropriate Karplus relationship provides conformational information about the P-O-C-H torsion angle. The torsion angle changes by 65 degrees +/- 10 degrees for the binary complex compared with the value in free NADPH. The observed coupling constants for the binary (DHFR--NADPH) and ternary (DHFR--NADPH--methotrexate) complexes (12.3 and 10.5 +/- 0.6 Hz, respectively) indicate that the pyrophosphate group has a similar conformation in the two complexes.
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
G. K. Surya Prakash, Fang Wang, Chuanfa Ni, Jingguo Shen, Ralf Haiges, Andrei K. Yudin, Thomas Mathew and George A. Olah
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202373d/aop/images/medium/ja-2011-02373d_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202373d
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[NMR paper] Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by
Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Related Articles Titration of E. coli transhydrogenase domain III with bound NADP+ or NADPH studied by NMR reveals no pH-dependent conformational change in the physiological pH range.
Biochim Biophys Acta. 2005 Apr-May;1707(2-3):254-8
Authors: Pedersen A, Johansson T, Rydström J, Göran Karlsson B
A pH-titration 2D NMR study of Escherichia coli transhydrogenase domain III with...
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[NMR paper] Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GM
Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21...
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[NMR paper] Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GM
Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21...
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[NMR paper] NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofola
NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogues of pyrimethamine.
Related Articles NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogues of pyrimethamine.
Biochemistry. 1990 Oct 16;29(41):9660-7
Authors: Birdsall B, Tendler SJ, Arnold JR, Feeney J, Griffin RJ, Carr MD, Thomas JA, Roberts GC, Stevens MF
1H and 19F NMR signals from bound ligands have been assigned in one- and two-dimensional NMR spectra of complexes of...
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[NMR paper] The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei
The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.
Eur J Biochem. 1990 Aug 17;191(3):659-68
Authors: Birdsall B, Arnold JR, Jimenez-Barbero J,...
31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dih
Linear Mode
