D = kt/6 a. d /2D. For sucrose/h 2O, we have D = 0.521X10
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2 M 0 M 0
3 D D = kt/6a 2 d /2D a d a For sucrose/h 2O, we have D = 0.521X10-5 cm 2-1 s, then -13 d = 1 nm -11 d = 10 nm NMR frequency ~ 10 8 Hz All spin interactions become isotropic in solution, so how it can be used for structural determination?
4
5 Chemical Shift/ppm
6 B khz 4 khz Z 2 khz X Y 0 khz (static) Chemical Shift/ppm
7 Chemical Shift/ppm
8 CSA Dipolar HI I HdI I I -I One-point sampling CSA I -I I -I I -I Dipolar I I
9 a) Insertion mechanism : C enriched 99.9% Ph Ph Rh Ph Ph Rh Ph Ph Ph b) Metathesis mechanism Ph Ph Ph Rh Rh Rh Ph Ph Ph
10 13 C dipolar powder pattern Rc- c = ± nm ref. (polyacetylene, 77K) C- C = nm C=C = nm The mechanism is the insertion mechanism!
11 CSA Dipolar HI I HdI I CSA d 0
12 Z Dipolar HdI I β X α Y Z 120 o HdI I X Y HtdtI I t=0 t = 1 rotational period dt
13 HtdtI I rf irradiation applied synchronously to modulate the spin part t t t=0 t = 1 cycle Ht t=0 t = 1 cycle Ht
14 (a) conventional CPMAS 13 C CP (b) MORE experimental 15 N (c) MORE simulation Hz [2- C, N] glycine
15
16 Decoupling by MAS
17 Uniform Labeling by 13 C / 15 N Uniform Decoupling by MAS Selective Recoupling by R2TR
18 G 180 o 180 o I I I 1 I o o o o G 165 o 170 o I I I 1 I o o o o J. Biomol. NMR, 17 (2000) 111.
19
20 1 H CP Decouple Decouple 13 C t 1 t 2
21 Amyloid-β fibrils is related to Altzheimer's disease. These depositions are composed of amyloid-β peptides of 40- and 42-residues Assignment of C signals of C-labeled aa by DARR with the mixing time of 20ms Aggrigative ability of these peptides relate to the 3D structures. Asp1-γ Asp2-γ Ala-CO Lys-CO Val1,2-CO Asp1-α Lys-α Asp2-α Val1,2-α Val2-β Val1-β Val2-γ Val1-γ Lys-β Asp1-β Asp2-β Lys-ε Ala -α Lys-γ Lys-δ Ala-β The Irie's model of amyloid- (Italian) or β-sheet β-sheet β-sheet Chemical 176 Shift/ppm Chemical 40 Shift/ppm 20
22 DARR (mixing time=1 s) Chemical Shift/ppm Chemical Shift/ppm Chemical Shift/ppm Ala Lys Asp Val If residue is β-sheet, the side chains of Lys and Asp are too far Chemical Shift/ppm 21 Ala 22 Lys 23 Asp 24 Val NH C αh CO NH C αh CO NH C αh CO NH C αh CO CH3 C βh 2 C H (b) β 2 C βh C γh 2 (C) C γooh H 3 Cγ C γh 3 Ala Val Lys Asp C δh 2 C εh 2 N ζh 2 (a)
23
24
25 UV?
26
27 4 -ln((1-m(t))/2)
28 K/s >1 s Fraction of dimer f D
29 29 Si Q3 Q T Na Na (aq) + Na + (solvated) 21.8 T H He Li Be B C N O F Ne Na Mg Al Si P S Cl Ar K Ca Sc Ti V Cr MnFe Co Ni Cu ZnGaGe As Se Br Kr RbSr Y Zr NbMoTc RuRhPdAgCd In Sn SbTe I Xe Cs Ba La Hf Ta W ReOs Ir Pt Au Hg Tl Pb Bi Po At Rn Fr Ra Ac Ku Ha La Ce Pr NdPmSmEuGdTbDyHo Er TmYbLu Ac Th Pa U NpPuAmCmBk Cf Es FmMdNo Lr Al four-coordinated 21.8 T B Chemical shift / ppm 21.8 T
30 H O B1 O O H O B2 O B2 O H O B1 O O H * MAS 2- B2 B B * /ppm e 2 qq/h (MHz) 10 B B B B B B B: Izv. Vyssh. Uchebn. Zaved. Fiz. 29, 3 (1986) 11B: J Chem. Phys., 38, 1912 (1963) B2 B1 11 B(I=3/2) 10 B Chemical shift / ppm
31 Static B2 B1 MAS * /ppm Chemical Shift/ppm MQMAS B1 B2 Either use higher magnetic field or do 2D-MQMAS! Chemical shift/ppm
32 δiso / ppm e 2 Qqh -1 / MHz η < Chemical Sift (ppm) Chemical Sift (ppm)
33 hbn cbn calc. ref. 1 calc. ref. 2 e 2 Qq / h < 0.05 (MHz) η ) Solid State NMR 12, 1-7 (1998) 2) Solid State NMR 8, (1997)
34 site2 site3 This cross peak shows site2 and site Chemical shift / ppm M.Murakami et al., Solid State NMR, 2007 (31) 193.
35
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