Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00121a009
Reference17 articles.
1. Replacements of Pro 86 in Phage T4 Lysozyme Extend an α-Helix But Do Not Alter Protein Stability
2. Empirical Predictions of Protein Conformation
3. A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme
4. Thermodynamic stability and point mutations of bacteriophage T4 lysozyme
5. Stabilization of λ repressor against thermal denaturation by site-directed Gly→Ala changes in α-helix 3
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