A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper
- 1 September 1995
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 4 (9) , 1934-1938
- https://doi.org/10.1002/pro.5560040929
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Measurement of Interhelical Electrostatic Interactions in the GCN4 Leucine ZipperScience, 1995
- Subdomain Folding of the Coiled Coil Leucine Zipper from the bZIP Transcriptional Activator GCN4Biochemistry, 1994
- Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4Biochemistry, 1993
- X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled CoilScience, 1991
- Why preferential hydration does not always stabilize the native structure of globular proteinsBiochemistry, 1990
- Preferential interactions determine protein solubility in three-component solutions: the magnesium chloride systemBiochemistry, 1990
- Evidence That the Leucine Zipper Is a Coiled CoilScience, 1989
- CHEMICAL SYNTHESIS OF PEPTIDES AND PROTEINSAnnual Review of Biochemistry, 1988
- Amino Acid, Peptide, and Protein Volume in SolutionAnnual Review of Biophysics and Bioengineering, 1984
- On the Conformational Stability of Globular ProteinsJournal of Biological Chemistry, 1965