pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding

Journal of Molecular Biology

Volumn 299, Issue 4, 2000, Pages 1091-1100

  Luisi, Donna L ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

Electrostatics; L9; Protein folding; Protein stability

Indexed keywords

PROTEIN L9; RIBOSOME PROTEIN; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; FLUORESCENCE; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 0034674156     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3752     Document Type: Article

References (41)

1. Ion-pairs in proteins
2. pKa's of ionizable groups in proteins: Atomic detail from continuum electrostatic model
3. Electrostatic interactions across a β-sheet
4. Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxin
5. On the calculation of electrostatic interactions in proteins
6. Do salt bridges stabilize protems? A continuum electrostatic analysis
7. Effect on protein stability of reversing the charge on amino-groups
8. Classical electrostatics in biology and chemistry
9. Strength and co-operativity of contributions of surface salt bridges to protein stability
10. Folding of chymotrypsin inhibitor 2. Evidence for a two state folding transition
11. Salt effects on protein stability: Two-stranded α-helical coiled-coils containing inter- or intrahelical ion pairs
12. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
13. Structure and stability of the N-terminal domain of the ribosomal protein L9: Evidence for the rapid two-state folding
14. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
15. pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
16. 2O. Determination of the thermodynamic parameters, ΔH°, ΔS°, and ΔC(p/o), and evaluation of solvent isotope effects
17. Salt bridge stability in monomeric proteins
18. The ionization of proteins
19. Estimating the degree of expansion in the transition state for protein unfolding: Analysis of the pH dependence of the rate constant for caricain denaturation
20. Effects of varying the local propensity to form secondary structure on the stability and the folding kinetics of a rapid folding mixed α/β protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9
21. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
22. Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
23. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
24. Formation of electrostatic interactions on the protein-folding pathway
25. pH dependence of urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
26. Measuring the conformational stability of a protein
27. Electrostatic effects in proteins
28. Surface electrostatic interactions contribute little to the stability of barnase
29. Protein engineering and the dissection of protein folding pathways
30. pH, ionic strength, and temperature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid third domain
31. pH dependence of the activation parameters for chymopapain unfolding: Influence of ion pairs on the kinetic stability of proteins
32. Rational modification of protein stability by the mutation of charged surface residues
33. Contribution of surface salt bridges to protein stability
34. Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
35. Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
36. Importance of two buried salt bridges in the stability and folding pathway of Barnase
37. Are buried salt bridges important for protein stability and conformational specificity?
38. Electrostatic energy and macromolecular function
39. Linked functions and reciprocal effects in hemoglobin: A second look
40. On the pH dependence of protein stability