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| Reaction Details | |||
|---|---|---|---|
 | Report a problem with these data | ||
| Cell Reactant: | HyHEL-5 Fab | ||
| Syringe Reactant: | Lysozyme (bobwhite quail) | ||
| Meas. Tech.: | ITC and sedimentation equilibrium | ||
| Entry Date: | 12/13/00 | ||
| ΔG°: | -9.34±0.100 (kcal/mole) | ||
| pH: | 8±n/a | ||
| Log10Kb: | 6.82± n/a | ||
| Temperature: | 298.15±n/a (K) | ||
| ΔH° : | -18.4±0.800 (kcal/mole) | ||
| ΔHobs : | -18.4± (kcal/mole) | ||
| Ionic Strength: | n/a | ||
| not known | |||
| Protons Released: | n/a | ||
| ΔCp : | -0.26±0.01 (kcal/mole) | ||
| Stoich. Param.: | n/a | ||
| ΔS° : | -0.0300±0 (kcal/mole-K) | ||
| Comments: | data from Wibbenmeyer, J. A., Xavier, K. A., Smith-Gill, S. J., and Willson, R. C. (1999) Biochim. Biophys. Acta 1430, 191-202 | ||
| Citation |  Wibbenmeyer, JA; Schuck, P; Smith-Gill, SJ; Willson, RC Salt links dominate affinity of antibody HyHEL-5 for lysozyme through enthalpic contributions. J Biol Chem274:26838-42 (1999) [PubMed] Article | ||
| More Info.: | Get all data from this article , ITC RUN data , Solution Info , Data Fit Method , Instrument Info | ||
| HyHEL-5 Fab | |||
| Source: | Recombinant HyHEL-5 Fab was expressed in E. coli. | ||
| Purity: | 95% | ||
| Prep. Method: | Refolded protein was purified by Q Sepharose and nickel-charged chelating Sepharose Fast Flow Chromatography | ||
| Name: | HyHEL-5 Fab | ||
| Synonyms: | n/a | ||
| Type: | Antibody | ||
| Mol. Mass.: | 23011.84 | ||
| Organism: | Mus musculus (mouse) | ||
| Description: | Monoclonal antibody to hen egg lysozyme | ||
| Residue: | 215 | ||
| Sequence: |
| ||
| Lysozyme (bobwhite quail) | |||
| Source: | Prepared from eggs purchased from Stevenson's Game Bird Farm (Riverside, TX) | ||
| Purity: | n/a | ||
| Prep. Method: | n/a | ||
| Name: | Lysozyme (bobwhite quail) | ||
| Synonyms: | LYSC_COLVI | LYZ | bobwhite quail lysozyme(BQL) | ||
| Type: | Enzyme | ||
| Mol. Mass.: | 14279.53 | ||
| Organism: | Colinus virginianus | ||
| Description: | hydrolase | ||
| Residue: | 129 | ||
| Sequence: |
| ||
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