✦ LIBER ✦

High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96 .fwdarw. His

✍ Scribed by Weaver, L. H.; Gray, T. M.; Gruetter, M. G.; Anderson, D. E.; Wozniak, J. A.; Dahlquist, F. W.; Matthews, B. W.

Book ID: 127094706
Publisher: American Chemical Society
Year: 1989
Tongue: English
Weight: 615 KB
Volume: 28
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi00435a025

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Evaluation at atomic resolution of the r

Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 → His

✍ Blaine H. M. Mooers; Dale E. Tronrud; Brian W. Matthews 📂 Article 📅 2009 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 601 KB

## Abstract Mutant R96H is a classic temperature‐sensitive mutant of bacteriophage T4 lysozyme. It was in fact the first variant of the protein to be characterized structurally. Subsequently, it has been studied extensively by a variety of experimental and computational techniques, but the reasons

A scanning calorimetric study of the the

A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96 .fwdarw. His mutant form thereof

✍ Kitamura, Shinichi; Sturtevant, Julian M. 📂 Article 📅 1989 🏛 American Chemical Society 🌐 English ⚖ 548 KB

A scanning calorimetric study of the the

A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg 96 .fwdarw. His mutant form thereof. [Erratum to document cited in CA110(21):188428n]

✍ Kitamura, Shinichi; Sturtevant, Julian M. 📂 Article 📅 1992 🏛 American Chemical Society 🌐 English ⚖ 53 KB