메뉴 건너뛰기




Volumn 14, Issue 1, 2011, Pages 127-135

Distinct folding pathways of two homologous disulfide proteins: Bovine pancreatic trypsin inhibitor and tick anticoagulant peptide

Author keywords

[No Author keywords available]

Indexed keywords

ANTICOAGULANT AGENT; APROTININ; CYSTINE; DISULFIDE;

EID: 78649475658     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2010.3634     Document Type: Review
Times cited : (10)

References (64)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 18: 223-230, 1973.
    • (1973) Science , vol.18 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0027933180 scopus 로고
    • NMR solution structure of re-combinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata
    • Antuch W, Güntert P, Billeter M, Hawthorne T, Grossen-bacher H, and Wüthrich K. NMR solution structure of re-combinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata. FEBS Lett 352: 251-257, 1994.
    • (1994) FEBS Lett , vol.352 , pp. 251-257
    • Antuch, W.1    Güntert, P.2    Billeter, M.3    Hawthorne, T.4    Grossen-Bacher, H.5    Wüthrich, K.6
  • 3
    • 78649488803 scopus 로고    scopus 로고
    • Protease inhibitors as models for the study of oxidative folding
    • Arolas JL and Ventura S. Protease inhibitors as models for the study of oxidative folding. Antioxid Redox Signal 14: 97- 112, 2011.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 97-112
    • Arolas, J.L.1    Ventura, S.2
  • 4
    • 33646350007 scopus 로고    scopus 로고
    • Folding of small disulfide-rich proteins: Clarifying the puzzle
    • Arolas JL, Aviles FX, Chang JY, and Ventura, S. Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci 31: 292-301, 2006.
    • (2006) Trends Biochem Sci , vol.31 , pp. 292-301
    • Arolas, J.L.1    Aviles, F.X.2    Chang, J.Y.3    Ventura, S.4
  • 5
    • 23444442371 scopus 로고    scopus 로고
    • NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor
    • Arolas JL, D'silva L, Popowicz GM, Aviles FX, Holak TA, and Ventura S. NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor. Structure 13: 1193-1202, 2005.
    • (2005) Structure , vol.13 , pp. 1193-1202
    • Arolas, J.L.1    D'Silva, L.2    Popowicz, G.M.3    Aviles, F.X.4    Holak, T.A.5    Ventura, S.6
  • 6
    • 55249100771 scopus 로고    scopus 로고
    • The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways
    • Arolas JL, Pantoja-Uceda D, Ventura S, Blanco FJ, and Aviles FX. The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways. J Biol Chem 283: 27110-27120, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 27110-27120
    • Arolas, J.L.1    Pantoja-Uceda, D.2    Ventura, S.3    Blanco, F.J.4    Aviles, F.X.5
  • 7
    • 0024391879 scopus 로고
    • How does protein folding get started?
    • Baldwin RL. How does protein folding get started? Trends Biochem Sci 14: 291-294, 1989.
    • (1989) Trends Biochem Sci , vol.14 , pp. 291-294
    • Baldwin, R.L.1
  • 8
    • 48249156678 scopus 로고    scopus 로고
    • The search for folding intermediates and the mechanism of protein folding
    • Baldwin RL. The search for folding intermediates and the mechanism of protein folding. Annu Rev Biochem. 37: 1-21, 2008.
    • (2008) Annu Rev Biochem. , vol.37 , pp. 1-21
    • Baldwin, R.L.1
  • 9
    • 33646340694 scopus 로고    scopus 로고
    • Knots in rings. The circular knotted protein Momordica cochinchinensis trypsin inhibitor-II folds via a stable two-disulfide intermediate
    • Cemazar M, Daly NL, Häggblad S, Lo KP, Yulyaningsih E, and Craik DJ. Knots in rings. The circular knotted protein Momordica cochinchinensis trypsin inhibitor-II folds via a stable two-disulfide intermediate. J Biol Chem 281: 8224-8232, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 8224-8232
    • Cemazar, M.1    Daly, N.L.2    Häggblad, S.3    Lo, K.P.4    Yulyaningsih, E.5    Craik, D.J.6
  • 10
    • 44649153789 scopus 로고    scopus 로고
    • The structure of a two-disulfide intermediate assists in elucidating the oxidative folding pathway of a cyclic cystine knot protein
    • Cemazar M, Joshi A, Daly NL, Mark AE, and Craik DJ. The structure of a two-disulfide intermediate assists in elucidating the oxidative folding pathway of a cyclic cystine knot protein. Structure 16: 842-851, 2008.
    • (2008) Structure , vol.16 , pp. 842-851
    • Cemazar, M.1    Joshi, A.2    Daly, N.L.3    Mark, A.E.4    Craik, D.J.5
  • 12
    • 0028303047 scopus 로고
    • Controlling the speed of hirudin folding
    • Chang JY. Controlling the speed of hirudin folding. Biochem J 300: 643-650, 1994.
    • (1994) Biochem J , vol.300 , pp. 643-650
    • Chang, J.Y.1
  • 13
    • 0032946292 scopus 로고    scopus 로고
    • Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers
    • Chang JY. Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers. J Biol Chem 274: 123-128, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 123-128
    • Chang, J.Y.1
  • 14
    • 0029840319 scopus 로고    scopus 로고
    • The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI
    • Chang JY. The disulfide folding pathway of tick anticoagulant peptide, a kunitz-type inhibitor structurally homologous to BPTI. Biochemistry 35: 11702-11709, 1996.
    • (1996) Biochemistry , vol.35 , pp. 11702-11709
    • Chang, J.Y.1
  • 15
    • 0037016695 scopus 로고    scopus 로고
    • The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling
    • Chang JY. The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling. J Biol Chem 277: 120-126, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 120-126
    • Chang, J.Y.1
  • 16
    • 0028818922 scopus 로고
    • The property of scrambled hirudins
    • Chang JY. The property of scrambled hirudins J Biol Chem 270, 25661-25666, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 25661-25666
    • Chang, J.Y.1
  • 17
    • 0033775975 scopus 로고    scopus 로고
    • Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide
    • Chang JY and Ballatore A. Structure and heterogeneity of the one- and two-disulfide folding intermediates of tick anticoagulant peptide. J Protein Chem 19: 299-310, 2000.
    • (2000) J Protein Chem , vol.19 , pp. 299-310
    • Chang, J.Y.1    Ballatore, A.2
  • 18
    • 0034640338 scopus 로고    scopus 로고
    • The structure of denatured bovine pancreatic trypsin inhibitor (BPTI)
    • Chang JY and Ballotore A. The structure of denatured bovine pancreatic trypsin inhibitor (BPTI). FEBS Lett 473: 183-187, 2000.
    • (2000) FEBS Lett , vol.473 , pp. 183-187
    • Chang, J.Y.1    Ballotore, A.2
  • 19
    • 16244388968 scopus 로고    scopus 로고
    • Divergent folding pathways of two homologous proteins, BPTI and tick anticoagulant peptide
    • Chang JY and Li L. Divergent folding pathways of two homologous proteins, BPTI and tick anticoagulant peptide. Arch Biochem Biophys 437: 85-95, 2005.
    • (2005) Arch Biochem Biophys , vol.437 , pp. 85-95
    • Chang, J.Y.1    Li, L.2
  • 20
    • 0037008013 scopus 로고    scopus 로고
    • Pathway of oxidative folding of a-lact-albumin: A model for illustrating the diversity of disulfide folding pathway
    • Chang JY and Li L. Pathway of oxidative folding of a-lact-albumin: a model for illustrating the diversity of disulfide folding pathway. Biochemistry 41: 8405-8413, 2002.
    • (2002) Biochemistry , vol.41 , pp. 8405-8413
    • Chang, J.Y.1    Li, L.2
  • 21
    • 0035971117 scopus 로고    scopus 로고
    • The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: Fractionation of conformational isomers of alpha-lactalbumin
    • Chang JY and Li L. The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin. J Biol Chem 276: 9705-9712, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 9705-9712
    • Chang, J.Y.1    Li, L.2
  • 22
    • 0034708453 scopus 로고    scopus 로고
    • The underlying mechanism for the diversity of disulfide folding pathway
    • Chang JY, Li L, and Bulychev A. The underlying mechanism for the diversity of disulfide folding pathway. J Biol Chem 275: 8287-8289, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 8287-8289
    • Chang, J.Y.1    Li, L.2    Bulychev, A.3
  • 23
    • 0035895917 scopus 로고    scopus 로고
    • A major kinetic trap for the oxidative folding of human epidermal growth factor
    • Chang JY, Li L, and Lai PH. A major kinetic trap for the oxidative folding of human epidermal growth factor. J Biol Chem 276: 4845-4852, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4845-4852
    • Chang, J.Y.1    Li, L.2    Lai, P.H.3
  • 24
    • 0029039633 scopus 로고
    • The disulfide structures of scrambled hirudins
    • Chang JY, Schindler P, and Chatrenet B. The disulfide structures of scrambled hirudins. J Biol Chem 270: 11992-11997, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 11992-11997
    • Chang, J.Y.1    Schindler, P.2    Chatrenet, B.3
  • 25
    • 0027434035 scopus 로고
    • The disulfide folding pathway of hirudin elucidated by stop=go folding experiments
    • Chatrenet B and Chang JY. The disulfide folding pathway of hirudin elucidated by stop=go folding experiments. J Biol Chem 268: 20988-20996, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 20988-20996
    • Chatrenet, B.1    Chang, J.Y.2
  • 26
    • 14844315799 scopus 로고    scopus 로고
    • Oxidative folding of the cystine knot motif in cyclotide proteins
    • Craik DJ and Daly NL. Oxidative folding of the cystine knot motif in cyclotide proteins. Protein Pept Lett 12: 147-152, 2005.
    • (2005) Protein Pept Lett , vol.12 , pp. 147-152
    • Craik, D.J.1    Daly, N.L.2
  • 27
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton TE. Disulfide bonds as probes of protein folding pathways. Methods Enzymol 131: 83-106, 1986.
    • (1986) Methods Enzymol , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 28
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton TE. Protein folding. Biochem J 270: 1-16, 1990.
    • (1990) Biochem J , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 29
    • 0026537987 scopus 로고
    • The disulfide folding pathway of BPTI
    • Creighton TE. The disulfide folding pathway of BPTI. Science 256: 111-114, 1992.
    • (1992) Science , vol.256 , pp. 111-114
    • Creighton, T.E.1
  • 30
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • DOI 10.1016/S0968-0004(02)00012-9, PII S0968000402000129
    • Daggett V and Fersht AR. Is there a unifying mechanism for protein folding? Trends Biochem Sci 28: 18-25, 2003. (Pubitemid 36051002)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 31
    • 0037458652 scopus 로고    scopus 로고
    • Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides
    • Daly NL, Clark RJ, and Craik DJ. Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem 278: 6314-6322, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 32
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 29: 7133-7155, 1990.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 34
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill KA and Shortle D. Denatured states of proteins. Annu Rev Biochem 60:795-825, 1991.
    • (1991) Annu Rev Biochem , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 35
    • 0030330918 scopus 로고    scopus 로고
    • Insights into protein folding from NMR
    • Dyson HJ and Wright PE. Insights into protein folding from NMR. Annu Rev Phys Chem 47: 369-395, 1996.
    • (1996) Annu Rev Phys Chem , vol.47 , pp. 369-395
    • Dyson, H.J.1    Wright, P.E.2
  • 36
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW and Mayne L. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21: 243-265, 1992.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 37
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht AR. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92: 10869-10873, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 38
    • 0029053552 scopus 로고
    • Folding of a Nascent Polypeptide Chain in vitro: Cooperative formation of structure in a protein module
    • Gay GdP, Ruiz-Sanz J, Neira JL, Itzhaki LS, and Fersh AR. Folding of a Nascent Polypeptide Chain in vitro: cooperative formation of structure in a protein module. Proc Natl Acad Sci USA 92: 3683-3686, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3683-3686
    • Gdp, G.1    Ruiz-Sanz, J.2    Neira, J.L.3    Itzhaki, L.S.4    Fersh, A.R.5
  • 39
    • 0026628991 scopus 로고
    • Native and non-native intermediates in the BPTI folding pathway
    • Goldenberg DP. Native and non-native intermediates in the BPTI folding pathway. Trends Biochem Sci 17: 257-261, 1992.
    • (1992) Trends Biochem Sci , vol.17 , pp. 257-261
    • Goldenberg, D.P.1
  • 40
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14: 1-63, 1959.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 41
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim PS and Baldwin RL. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59: 631-660, 1990.
    • (1990) Annu Rev Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 42
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim PS and Baldwin RL. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem 51: 459-489, 1982.
    • (1982) Annu Rev Biochem , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 43
    • 0018873523 scopus 로고
    • Protein inhibitors of proteases
    • Laskowski M Jr. and Kato I. Protein inhibitors of proteases. Annu Rev Biochem 49:593-626, 1980.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 44
    • 0027512113 scopus 로고
    • Characterization and 2D NMR study of the stable [9-21, 15-27] 2 disulfide intermediate in the folding of the 3 disulfide trypsin inhibitor EETI II
    • Le-Nguyen D, Heitz A, Chiche L, el Hajji M, and Castro B. Characterization and 2D NMR study of the stable [9-21, 15-27] 2 disulfide intermediate in the folding of the 3 disulfide trypsin inhibitor EETI II. Protein Sci 2: 165-174, 1993.
    • (1993) Protein Sci , vol.2 , pp. 165-174
    • Le-Nguyen, D.1    Heitz, A.2    Chiche, L.3    El Hajji, M.4    Castro, B.5
  • 48
    • 72149125850 scopus 로고    scopus 로고
    • Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor
    • Pantoja-Uceda D, Arolas JL, Aviles FX, Santoro J, Ventura S, and Sommerhoff CP. Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor. J Biol Chem 284: 35612-35620, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 35612-35620
    • Pantoja-Uceda, D.1    Arolas, J.L.2    Aviles, F.X.3    Santoro, J.4    Ventura, S.5    Sommerhoff, C.P.6
  • 49
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn OB. Protein folding: hypotheses and experiments. J Protein Chem 6: 273-293, 1987.
    • (1987) J Protein Chem , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 50
    • 0032539995 scopus 로고    scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A: Identification of two nativelike three-disulfide intermediates involved in separate pathways
    • Rothwarf D, Li YJ, and Scheraga HA. Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways. Biochemistry 37: 3760-3766, 1998.
    • (1998) Biochemistry , vol.37 , pp. 3760-3766
    • Rothwarf, D.1    Li, Y.J.2    Scheraga, H.A.3
  • 51
    • 12144285005 scopus 로고    scopus 로고
    • Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin
    • Salamanca S and Chang JY. Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin. Biochemistry 44:744-750, 2005.
    • (2005) Biochemistry , vol.44 , pp. 744-750
    • Salamanca, S.1    Chang, J.Y.2
  • 52
    • 33749234997 scopus 로고    scopus 로고
    • Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or Hirudin model
    • Salamanca S and Chang JY. Pathway of oxidative folding of a 3-disulfide alpha-lactalbumin may resemble either BPTI model or Hirudin model. Protein J 25: 275-287, 2006.
    • (2006) Protein J , vol.25 , pp. 275-287
    • Salamanca, S.1    Chang, J.Y.2
  • 53
    • 0025913761 scopus 로고
    • Determination of disulfide bond pairs and stability in recombinant tick anticoagulant peptide
    • Sardana M, Sandana V, Rodkey J, Wood T, Ng A, Vlasuk GP, and Waxman L. Determination of disulfide bond pairs and stability in recombinant tick anticoagulant peptide. J Biol Chem 266: 13560-13563, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 13560-13563
    • Sardana, M.1    Sandana, V.2    Rodkey, J.3    Wood, T.4    Ng, A.5    Vlasuk, G.P.6    Waxman, L.7
  • 54
    • 0034809784 scopus 로고    scopus 로고
    • Bovine pancreatic ribonuclease A: Oxidative and conformational folding studies
    • Scheraga HA, Wedemeyer WJ, and Welker E. Bovine pancreatic ribonuclease A: oxidative and conformational folding studies. Methods Enzymol 341: 189-221, 2001.
    • (2001) Methods Enzymol , vol.341 , pp. 189-221
    • Scheraga, H.A.1    Wedemeyer, W.J.2    Welker, E.3
  • 55
    • 49449100900 scopus 로고    scopus 로고
    • Problem solved* (*sort of)
    • Service RF. Problem solved* (*sort of). Science 321: 784-786, 2008.
    • (2008) Science , vol.321 , pp. 784-786
    • Service, R.F.1
  • 56
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle D. Structural analysis of non-native states of proteins by NMR methods. Curr Opin Struct Biol 6: 24-30, 1996.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 24-30
    • Shortle, D.1
  • 57
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: An ensemble of conformations trapped in a locally encoded topological space
    • Shortle D. The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space. Adv Protein Chem 62: 1-23, 2002.
    • (2002) Adv Protein Chem , vol.62 , pp. 1-23
    • Shortle, D.1
  • 58
    • 0038519321 scopus 로고
    • Contribution of hydrophobic interactions to the stability of globular confirmation of proteins
    • Tanford C. Contribution of hydrophobic interactions to the stability of globular confirmation of proteins. J Am Chem Soc 84: 4240-4247, 1962.
    • (1962) J Am Chem Soc , vol.84 , pp. 4240-4247
    • Tanford, C.1
  • 59
    • 0037181484 scopus 로고    scopus 로고
    • The chicken-egg scenario of protein folding revisited
    • Uversky VN and Fink AL. The chicken-egg scenario of protein folding revisited. FEBS Lett 515: 79-83, 2002.
    • (2002) FEBS Lett , vol.515 , pp. 79-83
    • Uversky, V.N.1    Fink, A.L.2
  • 60
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L, Smith DE, Arcuri KE, and Vlasuk GP. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248: 593-596, 1990.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 61
    • 0025949415 scopus 로고
    • Re-examination of the folding of BPTI: Predominance of native intermediates
    • Weissman JS and Kim PS. Re-examination of the folding of BPTI: predominance of native intermediates. Science 253: 1386-1393, 1991.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 63
    • 0031954924 scopus 로고    scopus 로고
    • Trapping intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanaylation, and subsequent structural elucidation by mass spectrmetry
    • Wu J, Yang Y, and Watson, JT. Trapping intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanaylation, and subsequent structural elucidation by mass spectrmetry. Protein Sci 7: 1017-1028, 1998.
    • (1998) Protein Sci , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3
  • 64
    • 0027723275 scopus 로고
    • Amino acid replacement that eliminates kinetic traps in the folding pathway of pancreatic trypsin inhibitor
    • Zhang JX and Goldenberg DP. Amino acid replacement that eliminates kinetic traps in the folding pathway of pancreatic trypsin inhibitor. Biochemistry 32: 14075-14081, 1993.
    • (1993) Biochemistry , vol.32 , pp. 14075-14081
    • Zhang, J.X.1    Goldenberg, D.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.