Title: How to determine the solution structure of murine epidermal growth factor by NMR Spectroscopy Hong Liu General protocols 1 COSY, TOCSY, DQFCOSY Spin System identification; 3JNH-H 3JH-H; Dihedral angles.
2 NOESY Sequential resonance assignments; Distance between different close nuclear pairs 3 Structure constraints table 4 Calculation (Submit NMR data to a specific program) 5 Refinement Spin system identification-COSY
H-H cross peak 2DF-COSY spectrum COSY
NH-H cross-peak NH-H cross-peak 2DF-COSY spectrum Relayed-COSY spectrum H Chemical Shifts for murine epidermal growth factor at 28oC and PH 3.1
1 Sequential resonance assignmentsNOESY Containing the intra-residue NHH and sequential H NH crosspeaks Containing the
sequential NH NH cross-peaks NOESY spectrum Survey of the sequential connectivities used in the sequencespecific 1H NMR assignment
Stereospecific C H2 assignment for mEGF at 28oC and PH3.1 53 AA 41AA(C H2) 14AA(degenerate) 2prolines
10AA(not estimate) 27AA 6AA(3JH-H inconsistent with any 25AA single staggered rotamer state for 15AA 1)# 9AA(consistent)
# To assume that the protein side chains adopt one of the three staggered conformations with 1=+60o,180o,-60o Stereospecific C H2 assignment for mEGF Stereospecific assignment of sidechain amide protons
Other assignments Stereospecific assignment of Valine isopropyl Methyl groups Based on NOE: Val-34, Val19 Experimental conformational constraints 1
2 3 4 5
Survey of NOE-derived distance constraints for mEGF in a diagonal plot Structural calculation and refinement Submit the NMR data to the DISMAN program. Structures refined by restrained energy minimization.
Conclusion 1 Advantage: Test samples in solutions, not need crystals, so convenient. 2 Disadvantage: Molecular-weight can not be big.
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