𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Helical and Expanded Conformation of Equine β-Lactoglobulin in the Cold-denatured State

✍ Scribed by Yoshiteru Yamada; Takeo Yajima; Kazuo Fujiwara; Munehito Arai; Kazuki Ito; Akio Shimizu; Hiroshi Kihara; Kunihiro Kuwajima; Yoshiyuki Amemiya; Masamichi Ikeguchi

Book ID
116662196
Publisher
Elsevier Science
Year
2005
Tongue
English
Weight
583 KB
Volume
350
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

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%

The methanol-induced transition and the
The methanol-induced transition and the expanded helical conformation in hen lysozyme
✍ Yuji O. Kamatari; Kazuyuki Akasaka; Takashi Konno; Mikio Kataoka 📂 Article 📅 1998 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 822 KB

## Abstract Methanol‐induced conformational transitions of hen egg white lysozyme were investigated with a combined use of far and near‐UV CD and NMR spectroscopies, ANS binding and small‐angle X‐ray scattering. Addition of methanol induced no global change in the native conformation itself, but in