𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Nature of the Unfolded State of Ribonuclease A: Effect of Cis−Trans X−Pro Peptide Bond Isomerization †

✍ Scribed by Houry, Walid A.; Scheraga, Harold A.

Book ID
126120868
Publisher
American Chemical Society
Year
1996
Tongue
English
Weight
672 KB
Volume
35
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

The rate-limiting step in the folding of
The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1 β-lactamase is the trans to cis isomerization of a non-proline peptide bond
✍ Marc Vanhove; Xavier Raquet; Timothy Palzkill; Roger H. Pain; Jean-Marie Frère 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 746 KB

The stability and kinetics of unfolding and refolding of the P167T mutant of the TEM-1 p-lactamase have been investigated as a function of guanidine hydrochloride concentration. The activity of the mutant enzyme was not significantly modified, which strongly suggests that the Glu166Thr167 peptide bo