Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: Fragment complementation and circular permutation reveal stable, alternatively folded forms

Protein Science

Volumn 10, Issue 1, 2001, Pages 116-128

  Smith, Virginia F ^a   Matthews, C Robert ^a,b  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b UNITED STATES NAVAL ACADEMY   (United States)

Author keywords

Circular dichroism spectroscopy; Fluorescence spectroscopy; Multi state unfolding; Thermal denaturation; Urea denaturation

Indexed keywords

ADENOSINE; DIHYDROFOLATE REDUCTASE; DIHYDROFOLATE REDUCTASE INHIBITOR; LIGAND; METHOTREXATE; MUTANT PROTEIN; UREA;

ARTICLE; CIRCULAR DICHROISM; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HEAT TREATMENT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; ENZYME STABILITY; ESCHERICHIA COLI; METHOTREXATE; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TETRAHYDROFOLATE DEHYDROGENASE; UREA;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0035109099     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.26601     Document Type: Article

References (63)

1. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
2. Crystal structures and properties of de novo circularly permuted 1,3-1,4-beta-glucanases
3. The folding mechanism of the α/β barrel protein, α-tryptophan synthase: Global analysis highlights the interconversion of multiple native, intermediate and unfolded forms through parallel channels
4. Thermodynamics
5. Equilibrium dissociation and unfolding of the Arc repressor dimer
6. A fully active variant of dihydrofolate reductase with a circularly permuted sequence
7. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
8. Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments
9. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
10. Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
11. Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli
12. Circular permutation of granulocyte colony-stimulating factor
13. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coil
14. Principles of protein stability. Part 1 - Reversible unfolding of proteins: Kinetic and thermodynamic analysis
15. A general approach for the design and isolation of protein fragments: The molecular dissection of dihydrofolate reductase
16. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection
17. Energetics of assembling an artificial heterodimer with an α/β motif: Cleaved versus uncleaved Escherichia coli thioredoxin
18. Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
19. Multi-state equilibrium unfolding of E. coil dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate and unfolded ensembles
20. Stability and reversibility of thermal denaturation are greatly improved by limiting terminal flexibility of Escherichia coli dihydrofolate reductase
21. Effects of the length of a glycine linker connecting the N- and C-termini of a circularly permuted dihydrofolate reductase
22. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli
23. Systematic circular permutation of an entire protein reveals essential folding elements
24. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
25. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
26. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
27. Empirical studies of protein secondary structure by vibrational circular dichroism and related techniques
28. Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase
29. Folding of barnase in parts
30. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
31. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
32. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
33. Subdomain interactions as determinants in the folding and stability of T4 lysozyme
34. Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli
35. Effect of point mutations on the folding of globular proteins
36. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
37. Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
38. Acid and thermal unfolding of Escherichia coli dihydrofolate reductase
39. Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus
40. Determination and analysis of urea and guanidine hydrochloride denaturation curves
41. Measuring the conformation stability of a protein
42. Urea denaturation of barnase: pH dependence and characterization of the unfolded state
43. Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
44. Mitochondrial protein import: Nucleoside triphosphates are involved in conferring import-competence to precursors
45. Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure
46. Molten globule and protein folding
47. Is the continuity of the domains required for the correct folding of a two-domain protein?
48. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant range
49. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
50. Solvent denaturation
51. Exons as microgenes?
52. Folding of dihydrofolate reductase from Escherichia coli
53. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
54. Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
55. Different folding transition states may result in the same native structure
56. Equilibrium and kinetic unfolding properties of dimeric human glutathione transferase A1-1
57. Eye lens betaB2-crystallin: Circular permutation does not influence the oligomerization state but enhances the conformational stability
58. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo
59. Thermodynamics of the reconstitution of tuna cytochrome c from two peptide fragments
60. Ligand binding is the principal determinant of stability for the p21 (H)-ras protein
61. Circular permutation of T4 lysozyme
62. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy