1. by Sunghyouk Park, Michael E. Johnson, and Leslie W.-M. Fung
Nuclear magnetic resonance studies of mutations at the tetramerization region of human alpha spectrin
by Sunghyouk Park, Michael E. Johnson, and Leslie W.-M. Fung
Blood
Volume 100(1):
July 1, 2002
©2002 by American Society of Hematology

2. Gel filtration of mixtures of Spβ and SpαArg28/Arg45, Arg28Ser, Arg45Ser, or Arg45Thr at 7 μM.The top 2 chromatograms of the individual sample are shown as references; additional measurements were done at 12 and 30 μM (data not shown).
Gel filtration of mixtures of Spβ and SpαArg28/Arg45, Arg28Ser, Arg45Ser, or Arg45Thr at 7 μM.The top 2 chromatograms of the individual sample are shown as references; additional measurements were done at 12 and 30 μM (data not shown). The position of each species is indicated by an arrow on the top chromatogram. We used 5 mM phosphate buffer with 150 mM NaCl at pH 6.5 (NMR sample buffer) for sample incubation and as eluting buffer. Schematic representations of the native Spα1-156 and Spβ structures are shown as insets above the corresponding chromatograms. The positions of the Arg28 and Arg45 mutations are shown by addition of the side chains at their sequence positions in insets above the corresponding chromatograms.
Sunghyouk Park et al. Blood 2002;100:
©2002 by American Society of Hematology

3. HSQC spectra of native Arg28/Arg45, Arg45Thr, Arg45Ser, and Arg28Ser peptides.(A) Native Arg28/Arg45 peptide, with resonances corresponding to the initial unstructured sequence 1-20 and the loop regions between helices 46-52, 82-87, and shown in bla...
HSQC spectra of native Arg28/Arg45, Arg45Thr, Arg45Ser, and Arg28Ser peptides.(A) Native Arg28/Arg45 peptide, with resonances corresponding to the initial unstructured sequence 1-20 and the loop regions between helices 46-52, 82-87, and shown in black; resonances corresponding to the initial Helix C′ shown in yellow; and resonances corresponding to Helices A1, B1, and C1 of the triple helical bundle shown in red, green, and blue, respectively. Arrows denote resonances affected by the mutations, with black arrows noting the mutated residues (Arg45 and Arg28), red arrows noting resonances affected by the Arg45Thr mutation, and blue arrows noting resonances affected by the Arg45Ser mutation. (B) Arg45Thr peptide, with arrows noting resonances whose chemical shifts are affected by the mutation. (C) Arg45Ser peptide, with arrows noting resonances affected by the mutation. (D) Arg28Ser peptide, for which missing resonances can be seen by comparison with (A). All spectra were acquired for the samples in NMR sample buffer at 20°C.
Sunghyouk Park et al. Blood 2002;100:
©2002 by American Society of Hematology

4. Plot of the backbone amide chemical-shift changes (Δδ) against residue numbers in Spα1-156Arg45Ser and Arg45Thr relative to Arg28/Arg45, and missing resonances in Arg45Ser.Sample identity is indicated at the top of each plot.
Plot of the backbone amide chemical-shift changes (Δδ) against residue numbers in Spα1-156Arg45Ser and Arg45Thr relative to Arg28/Arg45, and missing resonances in Arg45Ser.Sample identity is indicated at the top of each plot. Normalized chemical-shift changes in the top 2 plots were calculated as described in “Materials and methods.” Residues that could not be identified because of changes in the mutant spectra (residues 44, 45 in Arg45Thr; and 42, 45 in Arg45Ser) are left blank. The bottom plot notes resonances missing in the Arg28Ser HSQC spectrum, as compared with that of the native peptide.
Sunghyouk Park et al. Blood 2002;100:
©2002 by American Society of Hematology