Localized, stereochemically sensitive hydrophobic packing in an early folding intermediate of dihydrofolate reductase from Escherichia coli

Journal of Molecular Biology

Volumn 295, Issue 4, 2000, Pages 737-744

  O'Neill Jr, John C ^a   Robert Matthews, C ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

Burst phase intermediate; Hydrophobic clusters; Protein folding; Side chain packing interactions; Stopped flow circular dichroism

Indexed keywords

DIHYDROFOLATE REDUCTASE;

ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; STEREOCHEMISTRY;

ESCHERICHIA COLI;

EID: 0034723140     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3403     Document Type: Article

References (43)

1. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
2. Escherichia coli dihydrofolate reductase: Isolation and characterization of two isozymes
3. Observation of distinct nanosecond and microsecond protein folding events
4. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
5. Submillisecond protein folding kinetics by ultrafast mixing
6. Side-chain packing of the N and C-terminal helices plays a critical role in the kinetics of cytocrome c folding
7. Protein folding and stability - The pathway of folding of barnase
8. Discrete intermediates versus molten globule models for protein folding: Characterization of partially folded intermediates of apomyoglobin
9. A hydrophobic cluster forms early in the folding of dihydrofolate reductase
10. The core of apomyoglobin E-form folds at the diffusion limit
11. Effect of substrate decomposition on the spectrophoto-metric assay of dihydrofolate reductase
12. Structure and stability of monomeric lambda repressor: NMR evidence for two-state-folding
13. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
14. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
15. Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
16. Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
17. Energetics of complementary side-chain packing in a protein hydrophobic core
18. The molten globule state for understanding the folding and cooperativity of globular-protein structure
19. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
20. Structure of the transition state for folding of the 129-amino acid protein CheY resembles that of the smaller protein, CI2
21. Effects of core mutations on the folding of a β-sheet protein: Implications for backbone organization in the I-state
22. Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli
23. The folding process of hen lysozyme: A perspective from the 'new' view
24. Measuring the conformational stability of a protein
25. The development of tertiary interactions during the folding of a large protein
26. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
27. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
28. Kinetic role of early intermediates in protein folding
29. Structural characterization of folding intermediates in cytochrome c by hydrogen-exchange labeling and NMR
30. Amide protection in an early folding intermediate of cytochrome c
31. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
32. Solvent denaturation
33. Extremely rapid folding in the absence of intermediates
34. A residue-specific NMR view of the non-cooperative unfolding of a molten globule
35. Evidence for barrier-limited protein folding kinetics on the microsecond time scale
36. Contribution of individual residues to the formation of the native-like tertiary topology in the α-lactalbumin molten globule
37. Ultrafast signals in protein folding and the polypeptide contracted state
38. Folding of dihydrofolate reductase from Escherichia coli
39. Hydrophobic folding units derived from dissimilar monomer structures and their interactions
40. Protein folding via binding and vice versa
41. A specific hydrophobic core in the α-lactalbumin molten globule