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Solvation of β-lactoglobulin in alkylurea solutions

✍ Scribed by Nataša Poklar; Savo Lapanje

Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
626 KB
Volume
42
Category
Article
ISSN
0301-4622

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📜 SIMILAR VOLUMES

Calculation of the thermodynamic quantit
Calculation of the thermodynamic quantities of solvation for lysozyme and β-lactoglobulin a in guanidinium chloride
✍ Savo Lapanje 📂 Article 📅 1984 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 430 KB 👁 1 views

The thermodynamic quantities of solvation, that is, Gibbs free energy, enthalpy, and entropy for the transfer of lysozyme and 0-lactoglobulin A from water to 6M guanidinium chloride solution, were calculated from the respective contributions of constituent groups. Comparison of the calculated values

Self-association of β-lactoglobulin A in
Self-association of β-lactoglobulin A in acid solution. I. Translational diffusion coefficients
✍ B. Chu; A. Yeh; F. C. Chen; B. Weiner 📂 Article 📅 1975 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 848 KB

## Abstract We report measurements of the diffusion coefficient of β‐lactoglobulin A (βLG‐A) at pH = 5.60 and 4.58 in 0.10 ionic strength acetate buffer by the techniques of analog photocurrent signal correlation and digital single‐clipped photon correlation. At a concentration of 21 mg/ml and a pH

Raman studies of the crystalline, soluti
Raman studies of the crystalline, solution, and alkaline-denatured states of β-lactoglobulin
✍ B. G. Frushour; J. L. Koenig 📂 Article 📅 1975 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 752 KB

## Abstract The Raman spectra of β‐lactoglobulin in the crystalline, freeze‐dried, and solution states are compared. The spectra of the freeze‐dried and crystalline proteins were practically identical. The conformationally sensitive amide III line appearing at 1242 cm^−1^ increased in intensity 30%