𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Comparison of the structural and dynamical properties of holo and apo bovine α-lactalbumin by NMR spectroscopy

✍ Scribed by Ramani Wijesinha-Bettoni; Christopher M Dobson; Christina Redfield

Book ID
115630917
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
317 KB
Volume
307
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Study of ethanol-induced conformational
Study of ethanol-induced conformational changes of holo and apo α-lactalbumin by spectroscopy and limited proteolysis
✍ Zeina Wehbi; María-Dolores Pérez; Michèle Dalgalarrondo; Lourdes Sánchez; Migue 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 866 KB

## Abstract This study was performed to contribute to the analysis of α‐lactalbumin “molten globule” state by using spectral and proteolysis techniques. Samples of holo and apo α‐lactalbumin in the presence of different concentrations of ethanol were analyzed. Results of fluorescence spectroscopy o

Molecular dynamics simulations of human
Molecular dynamics simulations of human α-lactalbumin: Changes to the structural and dynamical properties of the protein at low pH
✍ Lorna J. Smith; Christopher M. Dobson; Wilfred F. van Gunsteren 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 187 KB 👁 1 views

Two 700-ps molecular dynamics simulations of human ␣-lactalbumin have been compared. Both were initiated from an X-ray structure determined at pH 6.5. One simulation was designed to represent native conditions and the other the protein in solution at pH 2.0 without a bound calcium ion. The low pH co