Testing the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli.
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Munehito Arai | K. Maki | Hisashi Takahashi | M. Arai | M. Iwakura | Hisashi Takahashi | Masahiro Iwakura | Kosuke Maki
[1] S. Walter Englander,et al. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.
[2] L Serrano,et al. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. , 1995, Journal of molecular biology.
[3] J. Onuchic,et al. Funnels, pathways, and the energy landscape of protein folding: A synthesis , 1994, Proteins.
[4] Udo Heinemann,et al. Crystal structures and properties of de novo circularly permuted 1,3‐1,4‐β‐glucanases , 1998, Proteins.
[5] J. Onuchic,et al. Theory of protein folding: the energy landscape perspective. , 1997, Annual review of physical chemistry.
[6] T. Yomo,et al. Evolutionary molecular engineering by random elongation mutagenesis , 1999, Nature Biotechnology.
[7] D A Agard,et al. Kinetics versus thermodynamics in protein folding. , 1994, Biochemistry.
[8] K. Kuwajima,et al. Role of the molten globule state in protein folding. , 2000, Advances in protein chemistry.
[9] A. Igarashi,et al. Chemo-enzymatic synthesis of optically pure l-leucovorin, an augmentor of 5-fluorouracil cytotoxicity against cancer. , 1990, Biochemical and biophysical research communications.
[10] A. Fersht,et al. Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments. , 1999, Journal of molecular biology.
[11] A. Horwich,et al. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo , 1991, The Journal of cell biology.
[12] P. V. von Hippel,et al. Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.
[13] C. Matthews,et al. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection , 1997, Protein science : a publication of the Protein Society.
[15] O. Ptitsyn,et al. Molten globule and protein folding. , 1995, Advances in protein chemistry.
[16] S. Takahashi,et al. Stepwise formation of alpha-helices during cytochrome c folding. , 2000, Nature structural biology.
[17] B. Jones,et al. Early intermediates in the folding of dihydrofolate reductase from escherichia coli detected by hydrogen exchange and NMR , 1995, Protein science : a publication of the Protein Society.
[18] P A Jennings,et al. An essential intermediate in the folding of dihydrofolate reductase. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[19] Raymond L. Blakley,et al. Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase. , 1967, Analytical biochemistry.
[20] K. Kuwajima,et al. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. , 1986, Biochemistry.
[21] William H. Press,et al. The Art of Scientific Computing Second Edition , 1998 .
[22] Tobin R. Sosnick,et al. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state , 1998, Nature Structural Biology.
[23] M. Karplus,et al. Statistical Analysis of Protein Folding Kinetics , 2002 .
[24] G. Fasman. Circular Dichroism and the Conformational Analysis of Biomolecules , 1996, Springer US.
[25] M. Iwakura,et al. Circular Permutation Analysis as a Method for Distinction of Functional Elements in the M20 Loop of Escherichia coliDihydrofolate Reductase* , 1999, The Journal of Biological Chemistry.
[26] Tsutomu Nakamura,et al. Systematic circular permutation of an entire protein reveals essential folding elements , 2000, Nature Structural Biology.
[27] A. Fersht. Structure and mechanism in protein science , 1998 .
[28] J. Beechem,et al. Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. , 1995, Biochemistry.
[29] C. Matthews,et al. 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 , 2001, Protein science : a publication of the Protein Society.
[30] M. Karplus,et al. How does a protein fold? , 1994, Nature.
[31] P. Hammarström,et al. Is the unfolded state the Rosetta Stone of the protein folding problem? , 2000, Biochemical and biophysical research communications.
[32] Carl Frieden,et al. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. , 1996, Biochemistry.
[33] K. Kuwajima. Stopped-Flow Circular Dichroism , 1996 .
[34] M. Hao,et al. Designing potential energy functions for protein folding. , 1999, Current opinion in structural biology.
[35] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.
[36] G. Rose,et al. Is protein folding hierarchic? II. Folding intermediates and transition states. , 1999, Trends in biochemical sciences.
[37] C. Robert Matthews,et al. Localized, stereochemically sensitive hydrophobic packing in an early folding intermediate of dihydrofolate reductase from Escherichia coli. , 2000, Journal of molecular biology.
[38] C. Dobson,et al. Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. , 1999, Journal of molecular biology.
[39] H. Roder,et al. Kinetic role of early intermediates in protein folding. , 1997, Current opinion in structural biology.
[40] G. Rose,et al. Is protein folding hierarchic? I. Local structure and peptide folding. , 1999, Trends in biochemical sciences.
[41] A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. , 1993, Biochemistry.
[42] R. Sauer,et al. Sequence space, folding and protein design. , 1996, Current opinion in structural biology.
[43] S. Marqusee,et al. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions , 1997, Nature Structural Biology.
[44] P E Wright,et al. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.
[45] K. Kuwajima,et al. The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. , 1996, Journal of molecular biology.
[46] Jeanette Tångrot,et al. Complete change of the protein folding transition state upon circular permutation , 2002, Nature Structural Biology.
[47] K. Kuwajima,et al. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. , 1991, Biochemistry.
[48] J. Kraut,et al. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. , 1997, Biochemistry.
[49] M. Iwakura,et al. Stability and reversibility of thermal denaturation are greatly improved by limiting terminal flexibility of Escherichia coli dihydrofolate reductase. , 1996, Journal of biochemistry.
[50] L Mayne,et al. Ultrafast signals in protein folding and the polypeptide contracted state. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[51] M. Karplus,et al. Use of quantitative structure‐property relationships to predict the folding ability of model proteins , 1998, Proteins.
[52] J G Saven,et al. Designing protein energy landscapes. , 2001, Chemical reviews.
[53] K. Dill. Dominant forces in protein folding. , 1990, Biochemistry.
[54] Matthews Cr,et al. Folding of dihydrofolate reductase from Escherichia coli , 1986 .
[55] D. Yee,et al. Principles of protein folding — A perspective from simple exact models , 1995, Protein science : a publication of the Protein Society.
[56] Carl Frieden. Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[57] V. Uversky,et al. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands , 1996, Protein science : a publication of the Protein Society.
[58] A. Murzin,et al. Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure. , 1994, Protein engineering.
[59] M Karplus,et al. The folding mechanism of larger model proteins: role of native structure. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[60] C. Pace. Determination and analysis of urea and guanidine hydrochloride denaturation curves. , 1986, Methods in enzymology.
[61] D. Shortle,et al. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea , 2001, Science.
[62] R. L. Baldwin. Pulsed H/D-exchange studies of folding intermediates , 1993 .
[63] A hydrophobic cluster forms early in the folding of dihydrofolate reductase , 1989, Proteins.
[64] J. Morrison,et al. Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate. , 1988, Biochemistry.
[65] M. Karplus,et al. Kinetics of protein folding. A lattice model study of the requirements for folding to the native state. , 1994, Journal of molecular biology.
[66] C. Matthews,et al. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. , 1991, Biochemistry.
[67] T. Nakamura,et al. Effects of the length of a glycine linker connecting the N-and C-termini of a circularly permuted dihydrofolate reductase. , 1998, Protein engineering.
[68] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[69] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.