✦ LIBER ✦

Folding studies on ribonuclease A, a model protein

✍ Scribed by José Luis Neira; Manuel Rico

Book ID: 114382602
Publisher: Elsevier Science
Year: 1997
Tongue: English
Weight: 255 KB
Volume: 2
Category: Article
ISSN: 1359-0278
DOI: 10.1016/s1359-0278(97)00001-1

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Folding Studies on a Knotted Protein

✍ Anna L. Mallam; Sophie E. Jackson 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 575 KB

Temperature-jump NMR study of protein fo

Temperature-jump NMR study of protein folding: Ribonuclease A at low pH

✍ Kazuyuki Akasaka; Akira Naito; Hiroshi Nakatani 📂 Article 📅 1991 🏛 Springer Netherlands 🌐 English ⚖ 277 KB

Studies of the intermediates in the fold

Studies of the intermediates in the folding of ribonuclease A

✍ Kim, Peter S.; Cook, Kem H.; Baldwin, Robert L. 📂 Article 📅 1980 🏛 Biophysical Society 🌐 English ⚖ 163 KB

A testable model for protein folding

✍ George D. Rose; Ronald H. Winters; Donald B. Wetlaufer 📂 Article 📅 1976 🏛 Elsevier Science 🌐 English ⚖ 562 KB

Genetic screen to dissect protein–protei

Genetic screen to dissect protein–protein interactions: ribonuclease inhibitor–ribonuclease A as a model system

✍ Sang-Hyun Park; Ronald T Raines 📂 Article 📅 2002 🏛 Elsevier Science 🌐 English ⚖ 290 KB

Further experimental studies of the disu

Further experimental studies of the disulfide folding transition of ribonuclease A

✍ Steven J. Wearne; Thomas E. Creighton 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 932 KB

Two very different mechanisms of folding have been proposed from experimental studies of disulfide formation in reduced ribonuclease A. (1) A pathway in which the rate-limiting step separates fully folded protein from all other disulfide intermediates and occurs solely in three-disulfide intermediat