Alternative packing arrangements in the hydrophobic core of λrepresser
- 1 May 1989
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 339 (6219) , 31-36
- https://doi.org/10.1038/339031a0
Abstract
The random alteration of hydrophobic core positions in the N-terminal domain of lambda-repressor, both individually and in combination, shows that there are many ways of repacking the core of the protein. Although the number of functional sequences is limited by constraints on composition, volume and steric interactions, the simple requirement that these positions remain hydrophobic is the main determinant of whether a core sequence is compatible with the wild-type fold.Keywords
This publication has 22 references indexed in Scilit:
- Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different structural classesPublished by Elsevier ,2005
- Structure of the Lambda Complex at 2.5 Å Resolution: Details of the Repressor-Operator InteractionsScience, 1988
- Combinatorial Cassette Mutagenesis as a Probe of the Informational Content of Protein SequencesScience, 1988
- Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded proteinBiochemistry, 1987
- Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.Proceedings of the National Academy of Sciences, 1983
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTUREAnnual Review of Biophysics and Bioengineering, 1977
- Structural invariants in protein foldingNature, 1975
- Structure and function of haemoglobinJournal of Molecular Biology, 1965
- Some Factors in the Interpretation of Protein DenaturationAdvances in Protein Chemistry, 1959