3D HSQC-TOCSY-NOESY-HSQC NMR Experiment

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Experiment correlates 1H δ3, 15N δ2chemical shifts of amide group of one aminoacid residue (residue A) with 15N shift Failed to parse (lexing error): \delta_1</mat> of another amide group (B) that is close in space to the side-chain of first residue <pulse test=true> anchors: @a,a1,a2,a3 @b @C,C1,C2,C3,C4 @D @E,E1--E2----E3,E4 @F disp: 3@a +3@b +3@C1 +8@D +4@E +8@F time: rlx @a2 ta @b ta @C1--C4 t12 @D t12 @E-----------E3 ta @F ta rf H: 90@a2 180@b 90@C1 shp@C2 180@D shp@E2 90@E3 180@F rf N: 90@a 180@b 90@C4 90@E 180@F pfg z: g1@a1 g2@a3 g2@C G3@C3 G4@E1 G5@E4 anchors: @c0,c,c1 @d1,d2 @e,e1,e2 @f @g,g1,g2,g3,g4 @h @i @j @k,k1,k2 @l @m,m1,m2 @n @o,o1 @p,p1 @q @r disp: +3@c +4@d1 +4@e1 +3@f +3@g1 +8@h +4@i +4@j +4@k1 +3@l +3@m1 +3@n +3@o1 +3@p +3@q +6@r time: @c dipsi @d2 tm @e1 ta @f ta @g1------g4 t22 @h t22 @i tb @j tb @k1 ta @l ta @m1 ta @n ta @o1 tc @p tc @q aq @r rf H: 90@c cpd@c1-d1=dipsi 90@e1 180@f 90@g1 shp@g2 180@h 90@k1 180@l 90@m1 180@n 90@o1 180@p acq@q----r rf N: 180@f 90@g4 180@j 90@k1 180@l 90@m1 180@n cpd@q----r pfg z: G5@c0 g3@e g4@e2 g4@g g5@g3 g6@k g7@k2 g7@m g8@m2 g8@o g9@p1 delay t12: show_at=N label=\frac{t_1}{2} delay rlx: hide=true delay tm: show_at=H label=\tau_m delay ta: label=\tau_a delay t22: show_at=N label=\frac{t_2}{2} delay tb: show_at=N label=\tau_b delay tc: label=\tau_c delay dipsi: hide=true gradient g5: strength=-100 cpd dipsi: label=dipsi </pulse> ===References=== <biblio> #zhang94 bibtex=@article{zhang1994bha, title={{Backbone 1 H and 15 N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques}}, author={Zhang, O. and Kay, L.E. and Olivier, J.P. and Forman-Kay, J.D.}, journal={Journal of Biomolecular NMR}, volume={4}, number={6}, pages={845--858}, year={1994}, publisher={Springer} } </biblio> [[Category:NOESY Experiments]]

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