메뉴 건너뛰기




Volumn 43, Issue 15, 2004, Pages 4522-4529

Evidence for the Underlying Cause of Diversity of the Disulfide Folding Pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CALCIUM; CHEMICAL BONDS; MOLECULAR STRUCTURE; OXIDATION; PROTEINS; PURIFICATION;

EID: 14044266878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0360354     Document Type: Article
Times cited : (28)

References (61)
  • 1
    • 0017815610 scopus 로고
    • Experimental studies of protein folding and unfolding
    • Creighton, T. E. (1978) Experimental studies of protein folding and unfolding, Prog. Biophys. Mol. Biol. 33, 231-297.
    • (1978) Prog. Biophys. Mol. Biol. , vol.33 , pp. 231-297
    • Creighton, T.E.1
  • 2
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton, T. E. (1986) Disulfide bonds as probes of protein folding pathways, Methods Enzymol. 131, 83-106.
    • (1986) Methods Enzymol. , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 3
    • 0026537987 scopus 로고
    • The disulfide folding pathway of BPTI
    • Creighton, T. E. (1992) The disulfide folding pathway of BPTI, Science 256, 111-114.
    • (1992) Science , vol.256 , pp. 111-114
    • Creighton, T.E.1
  • 4
    • 0026628991 scopus 로고
    • Native and non-native intermediates in the BPTI folding pathway
    • Goldenberg, D. P. (1992) Native and non-native intermediates in the BPTI folding pathway, Trends Biochem. Sci. 17, 257-261.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 257-261
    • Goldenberg, D.P.1
  • 5
    • 0021659707 scopus 로고
    • Kinetic role of a metastable native-like two-disulfide species in the folding transition of bovine pancreatic trypsin inhibitor
    • Creighton, T. E., and Goldenberg, D. P. (1984) Kinetic role of a metastable native-like two-disulfide species in the folding transition of bovine pancreatic trypsin inhibitor, J. Mol. Biol. 179, 497-526.
    • (1984) J. Mol. Biol. , vol.179 , pp. 497-526
    • Creighton, T.E.1    Goldenberg, D.P.2
  • 6
    • 0025949415 scopus 로고
    • Re-examination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J. S., and Kim, P. S. (1991) Re-examination of the folding of BPTI: predominance of native intermediates, Science 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 7
    • 0030468993 scopus 로고    scopus 로고
    • Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding
    • Dadlez, M., and Kim, P. S. (1996) Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding, Biochemistry 35, 16153-16164.
    • (1996) Biochemistry , vol.35 , pp. 16153-16164
    • Dadlez, M.1    Kim, P.S.2
  • 8
    • 0019874712 scopus 로고
    • Regeneration of ribonuclease A from the reduced protein, isolation and identification of intermediates, and equilibrium treatment
    • Konishi, Y., Ooi, T., and Scheraga, H. A. (1981) Regeneration of ribonuclease A from the reduced protein, isolation and identification of intermediates, and equilibrium treatment, Biochemistry 20, 3945-3955.
    • (1981) Biochemistry , vol.20 , pp. 3945-3955
    • Konishi, Y.1    Ooi, T.2    Scheraga, H.A.3
  • 9
    • 0032539956 scopus 로고    scopus 로고
    • Regeneration of Bovine Pancreatic Ribonuclease A: Detailed Kinetic Analysis of Two Independent Folding Pathways
    • Rothwarf, D. M., Li, Y. J., and Scheraga, H. A. (1998) Regeneration of Bovine Pancreatic Ribonuclease A: Detailed Kinetic Analysis of Two Independent Folding Pathways, Biochemistry 37, 3767-3776.
    • (1998) Biochemistry , vol.37 , pp. 3767-3776
    • Rothwarf, D.M.1    Li, Y.J.2    Scheraga, H.A.3
  • 10
    • 0034809784 scopus 로고    scopus 로고
    • Bovine pancreatic ribonuclease A: Oxidative and conformational folding studies
    • Scheraga, H. A., Wedemeyer, W. J., and Welker, E. (2001) Bovine pancreatic ribonuclease A: oxidative and conformational folding studies, Methods Enzymol. 341, 189-221.
    • (2001) Methods Enzymol. , vol.341 , pp. 189-221
    • Scheraga, H.A.1    Wedemeyer, W.J.2    Welker, E.3
  • 11
    • 0026736195 scopus 로고
    • The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor
    • van Mierlo, C. P., Darby, N. J., and Creighton, T. E. (1992) The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor, Proc. Natl. Acad. Sci. U.S.A. 89, 6775-6779.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6775-6779
    • Van Mierlo, C.P.1    Darby, N.J.2    Creighton, T.E.3
  • 12
    • 0032731392 scopus 로고    scopus 로고
    • Two new structured intermediates in the oxidative folding of RNase A
    • Welker, E., Narayan, M., Volles, M. J., and Scheraga, H. A. (1999) Two new structured intermediates in the oxidative folding of RNase A, FEBS Lett. 460, 477-479.
    • (1999) FEBS Lett. , vol.460 , pp. 477-479
    • Welker, E.1    Narayan, M.2    Volles, M.J.3    Scheraga, H.A.4
  • 13
    • 0027434035 scopus 로고
    • The disulfide folding pathway of hirudin elucidated by stop/go folding experiments
    • Chatrenet, B., and Chang, J.-Y. (1993) The disulfide folding pathway of hirudin elucidated by stop/go folding experiments, J. Biol. Chem. 268, 20988-20996.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20988-20996
    • Chatrenet, B.1    Chang, J.-Y.2
  • 14
    • 0028303047 scopus 로고
    • Controlling the speed of hirudin folding
    • Chang, J.-Y. (1994) Controlling the speed of hirudin folding, Biochem. J. 300, 643-650.
    • (1994) Biochem. J. , vol.300 , pp. 643-650
    • Chang, J.-Y.1
  • 15
    • 0029840319 scopus 로고    scopus 로고
    • The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI
    • Chang, J.-Y. (1996) The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI, Biochemistry 35, 11702-11709.
    • (1996) Biochemistry , vol.35 , pp. 11702-11709
    • Chang, J.-Y.1
  • 16
    • 0035895917 scopus 로고    scopus 로고
    • A major kinetic trap for the oxidative folding of human epidermal growth factor
    • Chang, J.-Y., Li, L., and Lai, P. H. (2001) A major kinetic trap for the oxidative folding of human epidermal growth factor, J. Biol. Chem. 276, 4845-4852.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4845-4852
    • Chang, J.-Y.1    Li, L.2    Lai, P.H.3
  • 17
    • 0028121986 scopus 로고
    • The disulfide folding pathway of potato carboxypeptidase inhibitor
    • Chang, J.-Y., Cannals, F., Schindler, P., Querol, E., and Aviles, F. X. (1994) The disulfide folding pathway of potato carboxypeptidase inhibitor, J. Biol. Chem. 269, 22087-22094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22087-22094
    • Chang, J.-Y.1    Cannals, F.2    Schindler, P.3    Querol, E.4    Aviles, F.X.5
  • 18
    • 0037646964 scopus 로고    scopus 로고
    • Major kinetic traps for the oxidative folding of leech carboxypeptidase inhibitor
    • Salamanca, S., Li, L., Vendrell, J., Aviles, F. X., and Chang, J.-Y. (2003) Major kinetic traps for the oxidative folding of leech carboxypeptidase inhibitor, Biochemistry 42, 6754-6761.
    • (2003) Biochemistry , vol.42 , pp. 6754-6761
    • Salamanca, S.1    Li, L.2    Vendrell, J.3    Aviles, F.X.4    Chang, J.-Y.5
  • 19
    • 0037008013 scopus 로고    scopus 로고
    • Pathway of oxidative folding of α-lactalbumin: A model for illustrating the diversity of disulfide folding pathway
    • Chang, J.-Y., and Li, L. (2002) Pathway of oxidative folding of α-lactalbumin: A model for illustrating the diversity of disulfide folding pathway, Biochemistry 41, 8405-8413.
    • (2002) Biochemistry , vol.41 , pp. 8405-8413
    • Chang, J.-Y.1    Li, L.2
  • 20
    • 0027269511 scopus 로고
    • Pathway of disulfide-coupled unfolding and refolding of bovine α-lactalbumin
    • Ewbank, J. J., and Creighton, T. E. (1993) Pathway of disulfide-coupled unfolding and refolding of bovine α-lactalbumin, Biochemistry 32, 3677-3693.
    • (1993) Biochemistry , vol.32 , pp. 3677-3693
    • Ewbank, J.J.1    Creighton, T.E.2
  • 22
    • 0037458652 scopus 로고    scopus 로고
    • Disulfide folding pathways of cystine knot proteins
    • Daly, N. L., Clark, R. J., and Craik, D. J. (2003) Disulfide folding pathways of cystine knot proteins, J. Biol. Chem. 278, 6314-6322.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 23
    • 0037126725 scopus 로고    scopus 로고
    • A Protein Caught in a Kinetic Trap: Structures and Stabilities of Insulin Disulfide Isomers
    • Hua, Q. X., Jia, W., Frank, B. H., Phillips, N. F., and Weiss, M. A. (2002) A Protein Caught in a Kinetic Trap: Structures and Stabilities of Insulin Disulfide Isomers, Biochemistry 41, 14700-14715.
    • (2002) Biochemistry , vol.41 , pp. 14700-14715
    • Hua, Q.X.1    Jia, W.2    Frank, B.H.3    Phillips, N.F.4    Weiss, M.A.5
  • 24
    • 0029991679 scopus 로고    scopus 로고
    • Native and Non-native Structure in a Protein-folding Intermediate: Spectroscopic Studies of Partially Reduced IGF-I and an Engineered Alanine Model
    • Hua, Q. X., Narhi, L., Jia, W., Arakawa, T., Rosenfeld, R., Hawkins, N., Miller, J. A., and Weiss, M. A. (1996) Native and Non-native Structure in a Protein-folding Intermediate: Spectroscopic Studies of Partially Reduced IGF-I and an Engineered Alanine Model, J. Mol. Biol. 259, 297-313.
    • (1996) J. Mol. Biol. , vol.259 , pp. 297-313
    • Hua, Q.X.1    Narhi, L.2    Jia, W.3    Arakawa, T.4    Rosenfeld, R.5    Hawkins, N.6    Miller, J.A.7    Weiss, M.A.8
  • 25
    • 53149090544 scopus 로고    scopus 로고
    • Oxidative folding of reduced and denatured huwentoxin-I
    • Liang, S., Shu, Q., Wang, X., and Zong, X. (1999) Oxidative folding of reduced and denatured huwentoxin-I, J. Protein Chem. 18, 619-625.
    • (1999) J. Protein Chem. , vol.18 , pp. 619-625
    • Liang, S.1    Shu, Q.2    Wang, X.3    Zong, X.4
  • 26
    • 0026786749 scopus 로고
    • Folding and oxidation of recombinant human granulocyte colony stimulating factor produced in Escherichia coli. Characterization of the disulfide-reduced intermediates and cysteine-serine analogs
    • Lu, H. S., Clogston, C. L., Narhi, L. O., Merewether, L. A., Pearl, W. R., and Boone, T. C. (1992) Folding and oxidation of recombinant human granulocyte colony stimulating factor produced in Escherichia coli. Characterization of the disulfide-reduced intermediates and cysteine-serine analogs, J. Biol. Chem. 267, 8770-8777.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8770-8777
    • Lu, H.S.1    Clogston, C.L.2    Narhi, L.O.3    Merewether, L.A.4    Pearl, W.R.5    Boone, T.C.6
  • 27
    • 0031954924 scopus 로고    scopus 로고
    • Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry
    • Wu, J., Yang, Y., and Watson, J. T. (1998) Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry, Protein Sci. 7, 1017-1028.
    • (1998) Protein Sci. , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3
  • 28
    • 0033621322 scopus 로고    scopus 로고
    • Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry
    • Yang, Y., Wu, J., and Watson, J. T. (1999) Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry, J. Biol. Chem. 274, 37598-37604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37598-37604
    • Yang, Y.1    Wu, J.2    Watson, J.T.3
  • 30
    • 0033586410 scopus 로고    scopus 로고
    • Probing the disulfide folding pathway of insulin-like growth factor-I
    • Milner, S. J., Carver, J. A., Ballard, F. J., and Francis, G. L. (1999) Probing the disulfide folding pathway of insulin-like growth factor-I, Biotechnol. Bioeng. 62, 693-703.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 693-703
    • Milner, S.J.1    Carver, J.A.2    Ballard, F.J.3    Francis, G.L.4
  • 31
    • 0032402863 scopus 로고    scopus 로고
    • Refolding of native and recombinant chicken riboflavin carrier (or binding) protein: Evidence for the formation of non-native intermediates during the generation of active protein
    • Pattanaik, P., Sooryanarayana, A. P. R., and Visweswariah, S. S. (1998) Refolding of native and recombinant chicken riboflavin carrier (or binding) protein: evidence for the formation of non-native intermediates during the generation of active protein, Eur. J. Biochem. 258, 411-418.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 411-418
    • Pattanaik, P.1    Sooryanarayana, A.P.R.2    Visweswariah, S.S.3
  • 32
    • 0032787875 scopus 로고    scopus 로고
    • The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogs and intermediates
    • Pegoraro, S., Fiori, S., Cramer, J., Rudolph-Bohner, S., and Moroder, L. (1999) The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogs and intermediates, Protein Sci. 8, 1605-1613.
    • (1999) Protein Sci. , vol.8 , pp. 1605-1613
    • Pegoraro, S.1    Fiori, S.2    Cramer, J.3    Rudolph-Bohner, S.4    Moroder, L.5
  • 33
    • 0035814878 scopus 로고    scopus 로고
    • Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro
    • Qiao, Z. S., Guo, Z. Y., and Feng, Y. M. (2001) Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro, Biochemistry 40, 2662-2668.
    • (2001) Biochemistry , vol.40 , pp. 2662-2668
    • Qiao, Z.S.1    Guo, Z.Y.2    Feng, Y.M.3
  • 34
    • 0038043253 scopus 로고    scopus 로고
    • In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process
    • Qiao, Z. S., Min, C. Y., Hua, Q. X., Weiss, M. A., and Feng, Y. M. (2003) In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process, J. Biol. Chem. 278, 17800-17809.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17800-17809
    • Qiao, Z.S.1    Min, C.Y.2    Hua, Q.X.3    Weiss, M.A.4    Feng, Y.M.5
  • 36
    • 0035909834 scopus 로고    scopus 로고
    • Slow folding of three-fingered toxins is associated with the accumulation of native disulfide-bonded intermediates
    • Ruoppolo, M., Talamo, F., Pucci, P., Moutiez, M., Quemeneur, E., Menez, A., and Marino, G. (2001) Slow folding of three-fingered toxins is associated with the accumulation of native disulfide-bonded intermediates, Biochemistry 40, 15257-15266.
    • (2001) Biochemistry , vol.40 , pp. 15257-15266
    • Ruoppolo, M.1    Talamo, F.2    Pucci, P.3    Moutiez, M.4    Quemeneur, E.5    Menez, A.6    Marino, G.7
  • 37
    • 0037013987 scopus 로고    scopus 로고
    • Reductive unfolding and oxidative refolding of a Bowman-Birk inhibitor from horse-gram seeds (Dolichos biflorus): Evidence for " hyperreactive" disulfide bonds and rate-limiting nature of disulfide isomerization in folding
    • Singh, R. R., and Appu Rao, A. G. (2002) Reductive unfolding and oxidative refolding of a Bowman-Birk inhibitor from horse-gram seeds (Dolichos biflorus): evidence for "hyperreactive" disulfide bonds and rate-limiting nature of disulfide isomerization in folding, Biochim. Biophys. Acta 1597, 280-291.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 280-291
    • Singh, R.R.1    Appu Rao, A.G.2
  • 38
    • 0033563126 scopus 로고    scopus 로고
    • Oxidative refolding of recombinant prochymosin
    • Wei, C., Tang, B., Zhang, Y., and Yang, K. (1999) Oxidative refolding of recombinant prochymosin, Biochem. J. 340, 345-351.
    • (1999) Biochem. J. , vol.340 , pp. 345-351
    • Wei, C.1    Tang, B.2    Zhang, Y.3    Yang, K.4
  • 39
    • 0027399212 scopus 로고
    • A study of intermediates involved in the folding pathway for recombinant human macrophage colony-stimulating factor (M-CSF): Evidence for two distinct folding pathways
    • Wilkins, J. A., Cone, J., Randhawa, Z. I., Wood, D., Warren, M. K., and Witkowska, H. E. (1993) A study of intermediates involved in the folding pathway for recombinant human macrophage colony-stimulating factor (M-CSF): evidence for two distinct folding pathways, Protein Sci. 2, 244-254.
    • (1993) Protein Sci. , vol.2 , pp. 244-254
    • Wilkins, J.A.1    Cone, J.2    Randhawa, Z.I.3    Wood, D.4    Warren, M.K.5    Witkowska, H.E.6
  • 40
    • 0041987555 scopus 로고    scopus 로고
    • Conformational analysis of intermediates involved in the in vitro folding pathways of recombinant human macrophage colony stimulating factor β by sulfhydryl group trapping and hydrogen/deuterium pulsed labeling
    • Zhang, Y. H., Yan, X., Maier, C. S., Schimerlik, M. I., and Deinzer, M. L. (2002) Conformational analysis of intermediates involved in the in vitro folding pathways of recombinant human macrophage colony stimulating factor β by sulfhydryl group trapping and hydrogen/deuterium pulsed labeling, Biochemistry 41, 15495-15504.
    • (2002) Biochemistry , vol.41 , pp. 15495-15504
    • Zhang, Y.H.1    Yan, X.2    Maier, C.S.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 41
    • 0028818922 scopus 로고
    • The properties of scrambled hirudins
    • Chang, J.-Y. (1995) The properties of scrambled hirudins, J. Biol. Chem. 270, 25661-25666.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25661-25666
    • Chang, J.-Y.1
  • 42
    • 0029039633 scopus 로고
    • The disulfide structures of scrambled hirudins
    • Chang, J.-Y., Schindler, P., and Chatrenet, B. (1995) The disulfide structures of scrambled hirudins, J. Biol. Chem. 270, 11992-11997.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11992-11997
    • Chang, J.-Y.1    Schindler, P.2    Chatrenet, B.3
  • 43
    • 0034708453 scopus 로고    scopus 로고
    • The underlying mechanism for the diversity of disulfide folding pathways
    • Chang, J.-Y., Li, L., and Bulychev, A. (2000) The underlying mechanism for the diversity of disulfide folding pathways, J. Biol. Chem. 275, 8287-8289.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8287-8289
    • Chang, J.-Y.1    Li, L.2    Bulychev, A.3
  • 44
    • 0024343068 scopus 로고
    • Calcium regulates folding and disulfide-bond formation in α-lactalbumin
    • Rao, K. R., and Brew, K. (1989) Calcium regulates folding and disulfide-bond formation in α-lactalbumin, Biochem. Biophys. Res. Commun. 163, 1390-1396.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 1390-1396
    • Rao, K.R.1    Brew, K.2
  • 45
    • 0027298344 scopus 로고
    • Structural characterization of the disulfide folding intermediates of bovine α-lactalbumin
    • Ewbank, J. J., and Creighton, T. E. (1993) Structural characterization of the disulfide folding intermediates of bovine α-lactalbumin, Biochemistry 32, 3694-3707.
    • (1993) Biochemistry , vol.32 , pp. 3694-3707
    • Ewbank, J.J.1    Creighton, T.E.2
  • 46
    • 0034685838 scopus 로고    scopus 로고
    • α-Lactalbumin: Structure and function
    • Permyakov, E. A., and Berliner, L. J. (2000) α-Lactalbumin: Structure and function, FEBS Lett. 473, 269-274.
    • (2000) FEBS Lett. , vol.473 , pp. 269-274
    • Permyakov, E.A.1    Berliner, L.J.2
  • 47
    • 0037016695 scopus 로고    scopus 로고
    • The folding pathway of α-lactalbumin elucidated by the technique of disulfide scrambling
    • Chang, J.-Y. (2002) The folding pathway of α-lactalbumin elucidated by the technique of disulfide scrambling, J. Biol. Chem. 277, 120-126.
    • (2002) J. Biol. Chem. , vol.277 , pp. 120-126
    • Chang, J.-Y.1
  • 48
    • 0021199710 scopus 로고
    • Disulfide bonds formation in proteins
    • Creighton, T. E. (1984) Disulfide bonds formation in proteins, Methods Enzymol. 107, 305-329.
    • (1984) Methods Enzymol. , vol.107 , pp. 305-329
    • Creighton, T.E.1
  • 49
    • 0034640338 scopus 로고    scopus 로고
    • The structure of denatured bovine pancreatic trypsin inhibitor (BPTI)
    • Chang, J.-Y., and Ballatore, A. (2000) The structure of denatured bovine pancreatic trypsin inhibitor (BPTI), FEBS Lett. 473, 183-187.
    • (2000) FEBS Lett. , vol.473 , pp. 183-187
    • Chang, J.-Y.1    Ballatore, A.2
  • 50
    • 53149088268 scopus 로고    scopus 로고
    • Unfolding of hirudin characterized by the composition of denatured scrambled isomers
    • Bulychev, A., and Chang, J.-Y. (1999) Unfolding of hirudin characterized by the composition of denatured scrambled isomers, J. Protein Chem. 18, 771-778.
    • (1999) J. Protein Chem. , vol.18 , pp. 771-778
    • Bulychev, A.1    Chang, J.-Y.2
  • 51
    • 0030023486 scopus 로고    scopus 로고
    • The roles of partly folded intermediates in protein folding
    • Creighton, T. E., Darby, N. J., and Kemmink, J. (1996) The roles of partly folded intermediates in protein folding, FASEB J. 10, 110-118.
    • (1996) FASEB J. , vol.10 , pp. 110-118
    • Creighton, T.E.1    Darby, N.J.2    Kemmink, J.3
  • 52
    • 0025271083 scopus 로고
    • Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor
    • Staley, J. P., and Kim, P. S. (1990) Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor, Nature 344, 685-688.
    • (1990) Nature , vol.344 , pp. 685-688
    • Staley, J.P.1    Kim, P.S.2
  • 53
    • 0028073893 scopus 로고
    • Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor
    • Staley, J. P., and Kim, P. S. (1994) Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor, Protein Sci. 3, 1822-1832.
    • (1994) Protein Sci. , vol.3 , pp. 1822-1832
    • Staley, J.P.1    Kim, P.S.2
  • 54
    • 0037126701 scopus 로고    scopus 로고
    • Interactions that Favor the Native over the Non-Native Disulfide Bond among Residues 58-72 in the Oxidative Folding of Bovine Pancreatic Ribonuclease A
    • Carty, R. P., Pincus, M. R., and Scheraga, H. A. (2002) Interactions that Favor the Native over the Non-Native Disulfide Bond among Residues 58-72 in the Oxidative Folding of Bovine Pancreatic Ribonuclease A, Biochemistry 41, 14815-14819.
    • (2002) Biochemistry , vol.41 , pp. 14815-14819
    • Carty, R.P.1    Pincus, M.R.2    Scheraga, H.A.3
  • 55
    • 0027311222 scopus 로고
    • Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: Genetic models of protein-folding intermediates
    • Narhi, L. O., Hua, Q. X., Arakawa, T., Fox, G. M., Tsai, L., Rosenfeld, R., Holst, P., Miller, J. A., and Weiss, M. A. (1993) Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates, Biochemistry 32, 5214-5221.
    • (1993) Biochemistry , vol.32 , pp. 5214-5221
    • Narhi, L.O.1    Hua, Q.X.2    Arakawa, T.3    Fox, G.M.4    Tsai, L.5    Rosenfeld, R.6    Holst, P.7    Miller, J.A.8    Weiss, M.A.9
  • 56
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu, L. C., Peng, Z. Y., and Kim, P. S. (1995) Bipartite structure of the α-lactalbumin molten globule, Nat. Struct. Biol. 2, 281-286.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.Y.2    Kim, P.S.3
  • 57
    • 0028916267 scopus 로고
    • Local structural preferences in the α-lactalbumin molten globule
    • Peng, Z. Y., Wu, L. C., and Kim, P. S. (1995) Local structural preferences in the α-lactalbumin molten globule, Biochemistry 34, 3248-3252.
    • (1995) Biochemistry , vol.34 , pp. 3248-3252
    • Peng, Z.Y.1    Wu, L.C.2    Kim, P.S.3
  • 58
    • 0035971117 scopus 로고    scopus 로고
    • The structure of denatured α-lactalbumin elucidated by the technique of disulfide scrambling
    • Chang, J.-Y., and Li, L. (2002) The structure of denatured α-lactalbumin elucidated by the technique of disulfide scrambling, J. Biol. Chem. 276, 9705-9712.
    • (2002) J. Biol. Chem. , vol.276 , pp. 9705-9712
    • Chang, J.-Y.1    Li, L.2
  • 59
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure, Proteins: Struct., Funct., Genet. 6, 87-103.
    • (1989) Proteins: Struct., Funct., Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 60
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. (1995) Molten globule and protein folding, Adv. Protein Chem. 47, 83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 61
    • 0034731321 scopus 로고    scopus 로고
    • A stabilized molten globule protein
    • Chang, J.-Y., Bulychev, A., and Li, L. (2000) A stabilized molten globule protein, FEBS Lett. 487, 298-300.
    • (2000) FEBS Lett. , vol.487 , pp. 298-300
    • Chang, J.-Y.1    Bulychev, A.2    Li, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.