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Table 1. Proton chemical shifts and vicinal coupling constants of hCC(101-117)Residue3J NH-Chemical shift [ppm]Hα[Hz] NH α - CH ε - CH β - CH δ - CH γ -CHILE1 - - 3.62 - 1.86 1.31 1.11 0.94TYR2 12.8 7.35 4.59 - 3.11 2.90 7.05 -ALA3 7.3 7.58 4.39 - 1.35 - -VAL4 8.3 7.22 4.37 - 1.60 - 0.84 0.73PRO5 - - 4.38 - 2.35 2.09 3.71 3.55 2.05TRP6 7.7 7.18 4.63 7.45 7.19 3.45 3.34 7.54 -GLN7 6.1 8.06 3.91 - 1.94 - 2.25GLY8 16.2 7.95 3.80 3.73 - - - -THR9 - 7.78 4.30 - 4.01 - 1.34MET10 5.1 8.38 4.24 - 2.23 2.13 - 2.60 2.51THR11 - 7.82 4.38 - 3.99 - 1.31LEU12 5.9 8.44 4.16 - 1.84 0.92 1.72SER13 7.6 8.06 4.39 - 4.12 4.07 - -LYS14 8.0 8.05 4.24 3.05 2.04 1.73 1.63SER15 8.4 8.26 4.21 - 4.08 - -THR16 9.6 7.63 4.42 - 4.41 - 1.35CYS17 8.2 7.76 4.57 - 3.01 - -standard Wüthrich procedure [4] using DQF-COSY, TOCSY and NOESY spectra. Thefingerprint region of the TOCSY spectrum and the diagnostic region of TOCSY andNOESY, including the sequential assignments, are given in Figure 1. There is only one setof chemical shifts, indicative of only one (time-averaged) state of hCC(101-117). Smallvalues of 3 J NHH α , typical of helix, were found for Met10 and Leu12 (Table 1). Vicinalcoupling constants typical of a β-sheet were found only for Tyr2 and Gly8. Most of theamino acid residues have3 J NHHα values near 7Hz, suggesting a statistical-coilconformation; some 3 J NHHα could not be measured. Analyzes of NOE d αN(i,i+3) intensitiespoint at helical 6-11 and 12-17 fragments of hCC(101-117). A d NN(i,i+1) connectivitiessuggesting helical conformation are present for most residues.The last 300 snapshots of MD with restraints are shown in Figure 2. RMSD value is0.71 Å for all atoms, 0.56 Å for heavy atoms and 0.35 Å for the backbone atoms. Allconformations have unordered N-termini with bends in their central part and very similarhelical structures in the (12-17) fragment. All the features of the calculated structuresobtained for the C-terminal fragment of hCC(101-117) are in very good agreement with thequalitative predictions from the NMR data.AcknowledgmentsThe work was supported by Polish Ministry of Science grant no. 1264/B/H03/2009/37 and BW8372-5-0647-0. The calculations were carried out in the Academic Computer Centre (TASK) inGdańsk, Poland.References1. Levy, E., Jaskólski, M., Grubb, A. Brain Pathol. 16, 60-70 (2006).2. Kaeser, S.A., Herzig, M.C., Coomaraswamy, J., et al. Nat. Genet. 39, 1437-1439 (2007).3. Juszczyk, P., Paraschiv, G., Szymańska, A., et al. J. Med. Chem. 52, 2420-2428 (2009).4. Wüthrich, K. NMR of Proteins and Nucleic Acids, John Wiley & Sons, New York (1986).595