Abstract
Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 43-46 |
| Number of pages | 4 |
| Journal | Proteins: Structure, Function, and Bioinformatics |
| Volume | 1 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1986 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Structural Biology
- Biochemistry
Keywords
- calorimetry
- helix‐coil
- mutant
- protein stability
Fingerprint
Dive into the research topics of 'Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver