Characterization of the unfolded state of bovine -lactalbumin and comparison with unfolded states of homologous proteins

Supplemental Research Data

Files in this Data Supplement:

• Adobe PDF File (484 KB) - Table S1: Results of Gaussian fitting for BLA-SsuperscriptME and all-Ala-HLA. Fitting was performed as described previously (Wirmer et al., 2004). xsubscriptcluster=center amino acid of the cluster (residue number), Rsubscriptcluster=amplitude of the cluster in s-1, lambdasubscriptcluster=width of the cluster in units of residues. Results for HEWL-SME can be found in the literature (Wirmer et al., 2004).
  Figure S1: Strip plots of residue K58 to residue N66. A) Strip plot extracted from an HNCACB spectrum. B) Strip plots extracted from an HN(CA)CO spectrum of BLA-SME. Each strip in the HNCACB shows resonances for the Csubalpha and the Csubbeta of the respective residue and the preceding residue, while each strip in the HN(CA)CO shows resonances for the CO carbon of the respective residue and the preceding one. Horizontal lines connect strips of a certain residue between the i and the i-1 strip, while vertical lines connect the i peak and the i-1 peak within one strip.
  Figure S2: Level of assignment using 15N labeled and/or 13C,15N labeled protein. Assignment was impossible using 15N labeled protein only. Full bars indicate definite assignment, while half bars indicate tentative assignment only.
  Figure S3: 1H,15N HSQC spectrum of BLA-SME at 800 MHz. Signals arising from the protein backbone are indicated by the residue type and number. Enlargements of two regions are shown due to limited space for indicating the respective residue number.