✦ LIBER ✦

Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation

✍ Scribed by Zhenyu Gu; Xiaonan Zhu; Shaowei Ni; Zhiguo Su; Hai-Meng Zhou

Book ID: 116306637
Publisher: Elsevier Science
Year: 2004
Tongue: English
Weight: 285 KB
Volume: 36
Category: Article
ISSN: 1357-2725
DOI: 10.1016/j.biocel.2003.08.015

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Renaturation of Lysozyme - Temperature D

Renaturation of Lysozyme - Temperature Dependence of Renaturation Rate, Renaturation Yield, and Aggregation: Identification of Hydrophobic Folding Intermediates

✍ B. Fischer; I. Sumner; P. Goodenough 📂 Article 📅 1993 🏛 Elsevier Science 🌐 English ⚖ 458 KB

Artificial Chaperone-Assisted Refolding

Artificial Chaperone-Assisted Refolding of Denatured-Reduced Lysozyme: Modulation of the Competition between Renaturation and Aggregation†

✍ Rozema, David; Gellman, Samuel H. 📂 Article 📅 1996 🏛 American Chemical Society 🌐 English ⚖ 614 KB

Refolding of recombinant sulphonated pro

Refolding of recombinant sulphonated procathepsin S and of reduced chicken cystatin; implications for renaturation experiments

✍ Eva Žerovnik; Gregor Kopitar; Janko Kos; Vito Turk 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 219 KB

Integration of PEGylation and refolding

Integration of PEGylation and refolding for renaturation of recombinant proteins from insoluble aggregates produced in bacteria—Application to a single-chain Fv fragment

✍ Izumi Kumagai; Ryutaro Asano; Takeshi Nakanishi; Kentaro Hashikami; Sho Tanaka; 📂 Article 📅 2010 🏛 Elsevier Science 🌐 English ⚖ 629 KB

Isolation and Characterization of Rhodan

Isolation and Characterization of Rhodanese Intermediates during Thermal Inactivation and Their Implications for the Mechanism of Protein Aggregation †

✍ Bhattacharyya, Anusri Mitra; Horowitz, Paul M. 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 94 KB

Aggregation of recombinant human botulin

Aggregation of recombinant human botulinum protein antigen serotype c in varying solution conditions: Implications of conformational stability for aggregation kinetics

✍ Shujun Bai; Mark Cornell Manning; Theodore W. Randolph; John F. Carpenter 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 460 KB

Solution conditions greatly affect the aggregation rate of a protein. Elucidating these influences provides insight into the critical factors governing aggregation. In this study, recombinant human botulinum protein antigen serotype C [rBoNTC (H(c))] was employed as a model protein. rBoNTC (H(c)) ag