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Volumn 326, Issue 2, 2003, Pages 569-583

The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase

Author keywords

DHFR; Folding; Isomerization; Non prolyl; Peptide bond

Indexed keywords

ALANINE; DIHYDROFOLATE REDUCTASE; GLYCINE; METHOTREXATE; MUTANT PROTEIN; PEPTIDE;

EID: 0037436336     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01444-4     Document Type: Article
Times cited : (20)

References (68)
  • 2
    • 0028935887 scopus 로고
    • Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding
    • Huang G.S., Oas T.G. Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry. 34:1995;3884-3892.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 3
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the src SH3 domain
    • Grantcharova V.P., Baker D. Folding dynamics of the src SH3 domain. Biochemistry. 36:1997;15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 4
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of beta-hairpin formation in protein G folding
    • McCallister E.L., Alm E., Baker D. Critical role of beta-hairpin formation in protein G folding. Nature Struct. Biol. 7:2000;669-673.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 5
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S.E., Dobson C.M., Evans P.A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 6
    • 0018183085 scopus 로고
    • Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin
    • Nozaka M., Kuwajima K., Nitta K., Sugai S. Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin. Biochemistry. 17:1978;3753-3758.
    • (1978) Biochemistry , vol.17 , pp. 3753-3758
    • Nozaka, M.1    Kuwajima, K.2    Nitta, K.3    Sugai, S.4
  • 7
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. Biochemistry. 24:1985;874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 8
    • 0030582679 scopus 로고    scopus 로고
    • The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
    • Kuwajima K., Yamaya H., Sugai S. The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264:1996;806-822.
    • (1996) J. Mol. Biol. , vol.264 , pp. 806-822
    • Kuwajima, K.1    Yamaya, H.2    Sugai, S.3
  • 9
    • 0032498226 scopus 로고    scopus 로고
    • Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
    • Arai M., Ikura T., Semisotnov G.V., Kihara H., Amemiya Y., Kuwajima K. Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275:1998;149-162.
    • (1998) J. Mol. Biol. , vol.275 , pp. 149-162
    • Arai, M.1    Ikura, T.2    Semisotnov, G.V.3    Kihara, H.4    Amemiya, Y.5    Kuwajima, K.6
  • 10
    • 0023055739 scopus 로고
    • Folding of dihydrofolate reductase from Escherichia coli
    • Touchette N.A., Perry K.M., Matthews C.R. Folding of dihydrofolate reductase from Escherichia coli. Biochemistry. 25:1986;5445-5452.
    • (1986) Biochemistry , vol.25 , pp. 5445-5452
    • Touchette, N.A.1    Perry, K.M.2    Matthews, C.R.3
  • 11
    • 0019883139 scopus 로고
    • Urea-induced unfolding of the α subunit of tryptophan synthase: Evidence for a multistate process
    • Matthews C.R., Crisanti M.M. Urea-induced unfolding of the α subunit of tryptophan synthase: evidence for a multistate process. Biochemistry. 20:1981;784-792.
    • (1981) Biochemistry , vol.20 , pp. 784-792
    • Matthews, C.R.1    Crisanti, M.M.2
  • 12
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
    • Walkenhorst W.F., Green S.M., Roder H. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry. 36:1997;5795-5805.
    • (1997) Biochemistry , vol.36 , pp. 5795-5805
    • Walkenhorst, W.F.1    Green, S.M.2    Roder, H.3
  • 14
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P.S., Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 15
    • 0000942752 scopus 로고
    • The formation of native disulfide bonds
    • R.H. Pain. New York: Oxford University Press
    • Gilbert H.F. The formation of native disulfide bonds. Pain R.H. Mechansims of Protein Folding. 1994;104-136 Oxford University Press, New York.
    • (1994) Mechansims of Protein Folding , pp. 104-136
    • Gilbert, H.F.1
  • 16
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerization of proline residues
    • Brandts J.F., Halvorson H.R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerization of proline residues. Biochemistry. 14:1975;4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 17
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • Schmid F.X. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22:1993;123-143.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 123-143
    • Schmid, F.X.1
  • 19
    • 0001849773 scopus 로고
    • Proline isomerization as a rate-limiting step
    • R.H. Pain. New York: Oxford University Press
    • Nall B.T. Proline isomerization as a rate-limiting step. Pain R.H. Mechansims of Protein Folding. 1994;80-103 Oxford University Press, New York.
    • (1994) Mechansims of Protein Folding , pp. 80-103
    • Nall, B.T.1
  • 20
    • 0036965922 scopus 로고    scopus 로고
    • A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein
    • Wu Y., Matthews C.R. A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. J. Mol. Biol. 322:2002;7-13.
    • (2002) J. Mol. Biol. , vol.322 , pp. 7-13
    • Wu, Y.1    Matthews, C.R.2
  • 21
    • 0033548058 scopus 로고    scopus 로고
    • Non-proline cis peptide bonds in proteins
    • Jabs A., Weiss M.S., Hilgenfeld R. Non-proline cis peptide bonds in proteins. J. Mol. Biol. 286:1999;291-304.
    • (1999) J. Mol. Biol. , vol.286 , pp. 291-304
    • Jabs, A.1    Weiss, M.S.2    Hilgenfeld, R.3
  • 23
    • 37049121355 scopus 로고
    • The barrier to internal rotation in monosubstituted amides
    • Drakenberg T., Forsén S. The barrier to internal rotation in monosubstituted amides. J. Chem. Soc., Chem. Commun. 1971;1404-1405.
    • (1971) J. Chem. Soc., Chem. Commun. , pp. 1404-1405
    • Drakenberg, T.1    Forsén, S.2
  • 24
    • 0015777335 scopus 로고
    • An ab initio quantum-mechanical investigation on the rotational isomerism in amides and esters
    • Perricaudet M., Pullman A. An ab initio quantum-mechanical investigation on the rotational isomerism in amides and esters. Int. J. Pept. Protein Res. 5:1973;99-107.
    • (1973) Int. J. Pept. Protein Res. , vol.5 , pp. 99-107
    • Perricaudet, M.1    Pullman, A.2
  • 25
    • 0013501645 scopus 로고
    • Proline isomerization and folding of yeast cytochrome c
    • L.M. Geirasch, & J.A. King. Washington, DC: American Association for the Advancement of Science
    • Nall B.T. Proline isomerization and folding of yeast cytochrome c. Geirasch L.M., King J.A. Protein Folding: Deciphering the Second Half of the Genetic Code. 1990;198-207 American Association for the Advancement of Science, Washington, DC.
    • (1990) Protein Folding: Deciphering the Second Half of the Genetic Code , pp. 198-207
    • Nall, B.T.1
  • 27
    • 84985715908 scopus 로고
    • NMR studies of the rates of proline cis-trans isomerization in oligopeptides
    • Grathwohl C., Wüthrich K. NMR studies of the rates of proline cis-trans isomerization in oligopeptides. Biopolymers. 20:1981;2623-2633.
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wüthrich, K.2
  • 28
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single-domain proteins
    • T.E. Creighton. New York: W.H. Freeman and Company
    • Schmid F.X. Kinetics of unfolding and refolding of single-domain proteins. Creighton T.E. Protein Folding. 1992;197-241 W.H. Freeman and Company, New York.
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 29
    • 0034682867 scopus 로고    scopus 로고
    • Multiple roles of prolyl residues in structure and folding
    • Eyles S.J., Gierasch L.M. Multiple roles of prolyl residues in structure and folding. J. Mol. Biol. 301:2000;737-747.
    • (2000) J. Mol. Biol. , vol.301 , pp. 737-747
    • Eyles, S.J.1    Gierasch, L.M.2
  • 30
    • 0024286073 scopus 로고
    • Influences of solvent water on protein folding: Free energies of solvation of cis and trans peptides are nearly identical
    • Radzicka A., Pedersen L., Wolfenden R. Influences of solvent water on protein folding: free energies of solvation of cis and trans peptides are nearly identical. Biochemistry. 27:1988;4538-4541.
    • (1988) Biochemistry , vol.27 , pp. 4538-4541
    • Radzicka, A.1    Pedersen, L.2    Wolfenden, R.3
  • 31
    • 26044455503 scopus 로고
    • Cis-trans energy difference for the peptide bond in the gas phase and in aqueous solution
    • Jorgensen W.L., Gao J. Cis-trans energy difference for the peptide bond in the gas phase and in aqueous solution. J. Am. Chem. Soc. 110:1988;4212-4216.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4212-4216
    • Jorgensen, W.L.1    Gao, J.2
  • 32
    • 0034806601 scopus 로고    scopus 로고
    • Direct measurement indicates a slow cis/trans isomerization at the secondary amide peptide bond of glycylglycine
    • Schiene-Fischer C., Fischer G. Direct measurement indicates a slow cis/trans isomerization at the secondary amide peptide bond of glycylglycine. J. Am. Chem. Soc. 123:2001;6227-6231.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6227-6231
    • Schiene-Fischer, C.1    Fischer, G.2
  • 34
    • 0024963670 scopus 로고
    • Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli
    • Garvey E.P., Matthews C.R. Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry. 28:1989;2083-2093.
    • (1989) Biochemistry , vol.28 , pp. 2083-2093
    • Garvey, E.P.1    Matthews, C.R.2
  • 35
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima K., Garvey E.P., Finn B.E., Matthews C.R., Sugai S. Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry. 30:1991;7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 36
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings P.A., Finn B.E., Jones B.E., Matthews C.R. A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry. 32:1993;3783-3789.
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 38
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya M.R., Kraut J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 36:1997;586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 39
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate
    • Bolin J.T., Filman D.J., Matthews D.A., Hamlin R.C., Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257:1982;13650-13662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 40
    • 0020442184 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis
    • Filman D.J., Bolin J.T., Matthews D.A., Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis. J. Biol. Chem. 257:1982;13663-13672.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13663-13672
    • Filman, D.J.1    Bolin, J.T.2    Matthews, D.A.3    Kraut, J.4
  • 41
    • 0025270551 scopus 로고
    • + ternary complex. Substrate binding and a model for the transition state
    • + ternary complex. Substrate binding and a model for the transition state. Biochemistry. 29:1990;3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 42
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff C., Kraut J. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30:1991;2227-2239.
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 43
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 44
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R.L. On-pathway versus off-pathway folding intermediates. Fold. Des. 1:1996;R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 45
    • 0023517017 scopus 로고
    • Effect of point mutations on the folding of globular proteins
    • Matthews C.R. Effect of point mutations on the folding of globular proteins. Methods Enzymol. 154:1987;498-511.
    • (1987) Methods Enzymol. , vol.154 , pp. 498-511
    • Matthews, C.R.1
  • 46
    • 0019444549 scopus 로고
    • Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase
    • Cayley P.J., Dunn S.M., King R.W. Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductase. Biochemistry. 20:1981;874-879.
    • (1981) Biochemistry , vol.20 , pp. 874-879
    • Cayley, P.J.1    Dunn, S.M.2    King, R.W.3
  • 47
    • 0017845745 scopus 로고
    • Kinetics of ligand binding to dihydrofolate reductase: Binary complex formation with NADPH and coenzyme analogues
    • Dunn S.M., Batchelor J.G., King R.W. Kinetics of ligand binding to dihydrofolate reductase: binary complex formation with NADPH and coenzyme analogues. Biochemistry. 17:1978;2356-2364.
    • (1978) Biochemistry , vol.17 , pp. 2356-2364
    • Dunn, S.M.1    Batchelor, J.G.2    King, R.W.3
  • 48
    • 0019328545 scopus 로고
    • Kinetics of ternary complex formation between dihydrofolate reductase, coenzyme, and inhibitors
    • Dunn S.M., King R.W. Kinetics of ternary complex formation between dihydrofolate reductase, coenzyme, and inhibitors. Biochemistry. 19:1980;766-773.
    • (1980) Biochemistry , vol.19 , pp. 766-773
    • Dunn, S.M.1    King, R.W.2
  • 49
    • 0026028965 scopus 로고
    • Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli
    • Falzone C., Wright P., Benkovic S. Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli. Biochemistry. 30:1991;2184-2191.
    • (1991) Biochemistry , vol.30 , pp. 2184-2191
    • Falzone, C.1    Wright, P.2    Benkovic, S.3
  • 51
    • 0036289101 scopus 로고    scopus 로고
    • Highly divergent dihydrofolate reductases conserve complex folding mechanisms
    • Wallace L.A., Matthews C.R. Highly divergent dihydrofolate reductases conserve complex folding mechanisms. J. Mol. Biol. 315:2002;193-211.
    • (2002) J. Mol. Biol. , vol.315 , pp. 193-211
    • Wallace, L.A.1    Matthews, C.R.2
  • 53
    • 0036404928 scopus 로고    scopus 로고
    • Parallel channels and rate-limiting steps in complex protein folding reactions: Prolyl peptide bond isomerization and the alpha subunit of Trp synthase, a TIM barrel protein
    • Wu Y., Matthews C.R. Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl peptide bond isomerization and the alpha subunit of Trp synthase, a TIM barrel protein. J. Mol. Biol. 323:2002;309-325.
    • (2002) J. Mol. Biol. , vol.323 , pp. 309-325
    • Wu, Y.1    Matthews, C.R.2
  • 54
    • 0034622508 scopus 로고    scopus 로고
    • Multi-state equilibrium unfolding of E. coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate and unfolded ensembles
    • Ionescu R.I., Smith V.F., O'Neill J.C., Matthews C.R. Multi-state equilibrium unfolding of E. coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate and unfolded ensembles. Biochemistry. 39:2000;9540-9550.
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.I.1    Smith, V.F.2    O'Neill, J.C.3    Matthews, C.R.4
  • 55
    • 0000702636 scopus 로고
    • Part II: Techniques for the study of biological structure and function
    • W.H. Freeman and Company, New York
    • Cantor, C. R. & Schimmel, P. R. (1980). Part II: techniques for the study of biological structure and function. In Biophysical Chemistry, vol. 2, W.H. Freeman and Company, New York pp. 349-408.
    • (1980) Biophysical Chemistry , vol.2 , pp. 349-408
    • Cantor, C.R.1    Schimmel, P.R.2
  • 56
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect
    • Muñoz V., Lopez E.M., Jager M., Serrano L. Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect. Biochemistry. 36:1994;5858-5866.
    • (1994) Biochemistry , vol.36 , pp. 5858-5866
    • Muñoz, V.1    Lopez, E.M.2    Jager, M.3    Serrano, L.4
  • 59
    • 0028952263 scopus 로고
    • A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli
    • Iwakura M., Jones B.E., Luo J., Matthews C.R. A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J. Biochem. 117:1995;480-488.
    • (1995) J. Biochem. , vol.117 , pp. 480-488
    • Iwakura, M.1    Jones, B.E.2    Luo, J.3    Matthews, C.R.4
  • 60
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar G., Sommer S.S. The "megaprimer" method of site-directed mutagenesis. BioTechniques. 8:1990;404-408.
    • (1990) BioTechniques , vol.8 , pp. 404-408
    • Sarkar, G.1    Sommer, S.S.2
  • 61
    • 0013526845 scopus 로고
    • E. coli DHFR: Isolation and characterization of two isoenzymes
    • Baccanari C.B., Averitt D., Briggs C., Burchall J. E. coli DHFR: isolation and characterization of two isoenzymes. Biochemistry. 16:1977;3566-4722.
    • (1977) Biochemistry , vol.16 , pp. 3566-4722
    • Baccanari, C.B.1    Averitt, D.2    Briggs, C.3    Burchall, J.4
  • 62
    • 0014010855 scopus 로고
    • Dihydrofolate reductase of Streptococcus faecalis. I. Purification and some properties of reductase from the wild strain and from strain A
    • Hillcoat B.L., Blakley R.L. Dihydrofolate reductase of Streptococcus faecalis. I. Purification and some properties of reductase from the wild strain and from strain A. J. Biol. Chem. 241:1966;2995-3001.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2995-3001
    • Hillcoat, B.L.1    Blakley, R.L.2
  • 63
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman J.A. Solvent denaturation. Biopolymers. 17:1978;1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 64
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 65
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;122-282.
    • (1968) Advan. Protein Chem. , vol.23 , pp. 122-282
    • Tanford, C.1
  • 66
    • 0023860769 scopus 로고
    • Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase
    • Taira K., Benkovic S.J. Evaluation of the importance of hydrophobic interactions in drug binding to dihydrofolate reductase. J. Med. Chem. 1:1988;129-137.
    • (1988) J. Med. Chem. , vol.1 , pp. 129-137
    • Taira, K.1    Benkovic, S.J.2
  • 67
    • 0033579862 scopus 로고    scopus 로고
    • 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
    • Bilsel O., Zitzewitz J.A., Bowers K.E., Matthews C.R. 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. Biochemistry. 38:1999;1018-1029.
    • (1999) Biochemistry , vol.38 , pp. 1018-1029
    • Bilsel, O.1    Zitzewitz, J.A.2    Bowers, K.E.3    Matthews, C.R.4
  • 68
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.