Journal:

Article Title: Molecular Crowding Inhibits Intramolecular Breathing Motions in Proteins

doi: 10.1016/j.jmb.2007.07.075

Figure Lengend Snippet: WAXS as a function of 1/d. (a) WAXS from bovine met hemoglobin. The figure is a superposition of 21 traces from solutions prepared at concentrations of 1; 2; 8.2; 10.2; 12.8; 16; 20; 25; 30; 35; 40; 47; 55; 64; 87; 102; 119; 162; 189; 257; and 300 mg/ml. (b) WAXS from hen egg white lysozyme. The figure is a superposition of 24 traces from scattering from solutions prepared at concentrations of 1; 2; 4.1; 8.2; 10.2; 12.8; 16; 20; 25; 30; 35; 47; 55; 64; 75; 87; 102; 119; 139; 162; 189; 220; 257; and 300 mg/ml. Data from solutions of 55-300 mg/ml were nearly indistinguishable. Data from 1 and 2 mg/ml solutions are readily identified due to their increased statistical fluctuations. Scaling of patterns indicated that under the conditions used, hemoglobin had a solubility of approximately 250 mg/ml and lysozyme a solubility of approximately 150 mg/ml. Scattering from solutions prepared at concentrations greater than this were virtually identical as judged by scaling, estimated excluded volume and intensity distribution.

Article Snippet: Bovine erythrocyte hemoglobin (Calbiochem, EMD Biosciences, Inc., San Diego, CA), equine myoglobin, bovine serum albumin (Sigma, St. Louis, MO) and hen egg white avidin (Affiland S.A., Ans-liege, Belgium) were diluted in phosphate-buffered saline without calcium and magnesium (Biowhittaker, Cambrex, Rockland, ME) to a final concentrated solution as indicated in the figure legend, then serially diluted to the noted concentrations.

Techniques: Solubility