The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil

Journal of Molecular Biology

Volumn 300, Issue 5, 2000, Pages 1377-1387

  Zhu, Hai ^a   Celinski, Scott A ^a   Scholtz, J Martin ^a   Hu, James C ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Hydrogen bonds; Hydrophobic interaction; Leucine zippers; Protein stability

Indexed keywords

LEUCINE ZIPPER PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STABILITY; THERMOSTABILITY;

EID: 0034725541     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3936     Document Type: Article

References (40)

1. Structure of the leucine zipper
2. Protein stability curves
3. The packing of α-helices: Simple coiled-coils
4. Hydrophobic parameters π of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amides
5. Buried polar residues and structural specificity in the GCN4 leucine zipper
6. A switch between two, three, and four-stranded coiled coils in GCN4 leucine zipper mutants
7. Free energy balance in protein folding
8. Transcription factors 1: bZip proteins
9. An autonomous folding unit mediates the assembly of two-stranded coiled coils
10. Some factors in the interpretation of protein denaturation
11. The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
12. Computer-aided interpretation of analytical sedimentation data for protein
13. Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics
14. The interpretation of protein structures: Estimation of static accessibility
15. Energetics of protein structure
16. Molecular zippers in gene regulation
17. Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
18. Molecular basis of co-operativity in protein folding. III. Structural identification of cooperative folding units and folding intermediates
19. Reinterpretation of GCN4-p1 folding kinetics: Partial helix formation precedes dimerization in coiled coil folding
20. Hydrogen bonding stabilizes globular proteins
21. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
22. Evidence that the leucine zipper is a coiled coil
23. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
24. Contribution of the hydrophobic effect to globular protein stability
25. Urea denaturation of barnase: pH dependence and characterization of the unfolded state
26. A helix propensity scale based on experimental studies of peptides and proteins
27. How to measure and predict the molar absorption coefficient of a protein
28. Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets
29. The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
30. Synthesis and properties of the peptide corresponding to the mutant form of the leucine zipper of the transcriptional activator GCN4 from yeast
31. Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
32. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
33. Coupling of local folding to site-specific binding of proteins to DNA
34. Use of T7 RNA polymerase to direct expression of cloned genes
35. Contribution of hydrophobic interactions to the stability of the globular conformation
36. Interfacial free energy and the hydrophobic effect
37. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
38. Additivity of mutational effects in proteins
39. Buried asparagines determine the dimerization specificities of leucine zipper mutants
40. Packing and hydrophobicity effects on protein folding and stability: Effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled-coils/ leucine zippers