메뉴 건너뛰기




Volumn 8, Issue 8, 1999, Pages 1605-1613

The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogs and intermediates

Author keywords

Apamin; Disulfide bridges; Folding; Secondary structure; Selenocysteine

Indexed keywords

APAMIN; DISULFIDE; PEPTIDE; PROTEIN; SELENOCYSTEINE;

EID: 0032787875     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.8.1605     Document Type: Article
Times cited : (64)

References (44)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0031265707 scopus 로고    scopus 로고
    • Synthesis of selenocysteine-peptides and their oxidation to diselenide-bridged compounds
    • Besse D, Moroder L. 1997. Synthesis of selenocysteine-peptides and their oxidation to diselenide-bridged compounds. J Peptide Sci 3:442-453.
    • (1997) J Peptide Sci , vol.3 , pp. 442-453
    • Besse, D.1    Moroder, L.2
  • 5
    • 0026018103 scopus 로고
    • Selenoprotein synthesis: An expansion of the genetic code
    • Böck A, Forchhammer K, Heider J, Baron C. 1991. Selenoprotein synthesis: An expansion of the genetic code. TIBS 16:463-467.
    • (1991) TIBS , vol.16 , pp. 463-467
    • Böck, A.1    Forchhammer, K.2    Heider, J.3    Baron, C.4
  • 6
    • 0013583796 scopus 로고
    • NMR spectroscopy of large peptides and small proteins
    • Bystrov VF, Arseniev AS, Gavrilov YD. 1978. NMR spectroscopy of large peptides and small proteins. J Magn Res 30:151-184.
    • (1978) J Magn Res , vol.30 , pp. 151-184
    • Bystrov, V.F.1    Arseniev, A.S.2    Gavrilov, Y.D.3
  • 9
    • 0026647690 scopus 로고
    • Cooperative disulfide bond formation in apamin
    • Chau MH, Nelson JW. 1992. Cooperative disulfide bond formation in apamin. Biochemistry 31:4445-4450.
    • (1992) Biochemistry , vol.31 , pp. 4445-4450
    • Chau, M.H.1    Nelson, J.W.2
  • 10
    • 0020647834 scopus 로고
    • An empirical approach to protein conformation stability and flexibility
    • Creighton TE. 1983. An empirical approach to protein conformation stability and flexibility. Biopolymers 22:49-58.
    • (1983) Biopolymers , vol.22 , pp. 49-58
    • Creighton, T.E.1
  • 11
    • 0022555899 scopus 로고
    • Disulphide bonds as probes of protein folding pathways
    • Creighton TE. 1986. Disulphide bonds as probes of protein folding pathways. Methods Enzymol 131:83-106.
    • (1986) Methods Enzymol , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 12
    • 0030797806 scopus 로고    scopus 로고
    • Protein folding coupled to disulphide bond formation
    • Creighton TE. 1997. Protein folding coupled to disulphide bond formation. Biol Chem 378:731-744.
    • (1997) Biol Chem , vol.378 , pp. 731-744
    • Creighton, T.E.1
  • 13
    • 0030023486 scopus 로고    scopus 로고
    • The roles of partly folded intermediates in protein folding
    • Creighton T, Darby NJ, 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.1    Darby, N.J.2    Kemmink, J.3
  • 14
    • 0026589880 scopus 로고
    • Stabilities of disulfide bond intermediates in the folding of apamin
    • Huyghues-Despointes BM, Nelson JW. 1992. Stabilities of disulfide bond intermediates in the folding of apamin. Biochemistry 31:1476-1483.
    • (1992) Biochemistry , vol.31 , pp. 1476-1483
    • Huyghues-Despointes, B.M.1    Nelson, J.W.2
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graphics 14:51-55.
    • (1996) J Mol Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 18
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin TY, Kim PS. 1989. Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 28:5282-5287.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.Y.1    Kim, P.S.2
  • 19
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A. 1989. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399.
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 20
    • 0042577216 scopus 로고
    • A study of the physicochemical characteristics of the neurotoxin apamin from the venom of the honeybee Apis mellifica
    • Miroshnikov AI, Elyakova EG, Kudelin AB, Senyavina LB. 1978. A study of the physicochemical characteristics of the neurotoxin apamin from the venom of the honeybee Apis mellifica. Sov J Bioorg Chem (engl transl) 4:746-752.
    • (1978) Sov J Bioorg Chem (Engl Transl) , vol.4 , pp. 746-752
    • Miroshnikov, A.I.1    Elyakova, E.G.2    Kudelin, A.B.3    Senyavina, L.B.4
  • 21
    • 0023692599 scopus 로고
    • A peptide model of a protein folding intermediate
    • Oas TG, Kim PS. 1988. A peptide model of a protein folding intermediate. Nature 336:42-48.
    • (1988) Nature , vol.336 , pp. 42-48
    • Oas, T.G.1    Kim, P.S.2
  • 22
    • 0025331245 scopus 로고
    • Folding and activity of hybrid sequence, disulfide-stabilized peptides
    • Pease JH, Storrs RW, Wemmer DE. 1990. Folding and activity of hybrid sequence, disulfide-stabilized peptides. Proc Natl Acad Sci USA 87:5643-5647.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5643-5647
    • Pease, J.H.1    Storrs, R.W.2    Wemmer, D.E.3
  • 23
    • 0023685312 scopus 로고
    • Solution structure of apamin determined by nuclear magnetic resonance and distance geometry
    • Pease JH, Wemmer DE. 1988. Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry 27:8491-8498.
    • (1988) Biochemistry , vol.27 , pp. 8491-8498
    • Pease, J.H.1    Wemmer, D.E.2
  • 25
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenár V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 26
    • 0027487236 scopus 로고
    • Selective disulfide formation in truncated apamin and sarafotoxin
    • Ramalingam K, Snyder GH. 1993. Selective disulfide formation in truncated apamin and sarafotoxin. Biochemistry 32:1155-1161.
    • (1993) Biochemistry , vol.32 , pp. 1155-1161
    • Ramalingam, K.1    Snyder, G.H.2
  • 27
    • 0032539995 scopus 로고    scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A: Identification of two nativelike three-disulfide intermediates involved in separate pathways
    • Rothwarf DM, Li Y-J, Scheraga HA. 1998. Regeneration of bovine pancreatic ribonuclease A: Identification of two nativelike three-disulfide intermediates involved in separate pathways. Biochemistry 37:3760-3766.
    • (1998) Biochemistry , vol.37 , pp. 3760-3766
    • Rothwarf, D.M.1    Li, Y.-J.2    Scheraga, H.A.3
  • 28
    • 0027413488 scopus 로고
    • Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution
    • Rothwarf DM, Scheraga HA. 1993. Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 32:2671-2679.
    • (1993) Biochemistry , vol.32 , pp. 2671-2679
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 29
    • 0027308079 scopus 로고
    • Redox potentials of active site bis-cysteinyl fragments of thiol-protein oxidoreductases
    • Siedler F, Rudolph-Böhner S, Doi M, Musiol H-J, Moroder L. 1993. Redox potentials of active site bis-cysteinyl fragments of thiol-protein oxidoreductases. Biochemistry 32:7488-7495.
    • (1993) Biochemistry , vol.32 , pp. 7488-7495
    • Siedler, F.1    Rudolph-Böhner, S.2    Doi, M.3    Musiol, H.-J.4    Moroder, L.5
  • 31
    • 0025271083 scopus 로고
    • Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor
    • Staley JP, Kim PS. 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
  • 32
    • 0026543422 scopus 로고
    • Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond
    • Staley JP, Kim PS. 1992. Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond. Proc Natl Acad Sci USA 89:1519-1523.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1519-1523
    • Staley, J.P.1    Kim, P.S.2
  • 33
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States DJ, Haberkorn RA, Ruben DJ. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 48:286-292.
    • (1982) J Magn Reson , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 34
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski RP, Whiteside GM. 1980. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J Am Chem Soc 102:2011-2026.
    • (1980) J Am Chem Soc , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whiteside, G.M.2
  • 37
    • 0026411134 scopus 로고
    • (14-38, 30-51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance study
    • van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. 1991a. (14-38, 30-51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance study. J Mol Biol 222:353-371.
    • (1991) J Mol Biol , vol.222 , pp. 353-371
    • Van Mierlo, C.P.1    Darby, N.J.2    Neuhaus, D.3    Creighton, T.E.4
  • 38
    • 0026357218 scopus 로고
    • Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor
    • van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. 1991b. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol 222:373-390.
    • (1991) J Mol Biol , vol.222 , pp. 373-390
    • Van Mierlo, C.P.1    Darby, N.J.2    Neuhaus, D.3    Creighton, T.E.4
  • 39
    • 0028180377 scopus 로고
    • 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor
    • van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1994. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol 235:1044-1061.
    • (1994) J Mol Biol , vol.235 , pp. 1044-1061
    • Van Mierlo, C.P.1    Kemmink, J.2    Neuhaus, D.3    Darby, N.J.4    Creighton, T.E.5
  • 40
    • 0020586169 scopus 로고
    • Structure of apamin in solution: A two-dimensional nuclear magnetic resonance study
    • Wemmer D, Kallenbach NR. 1983. Structure of apamin in solution: A two-dimensional nuclear magnetic resonance study. Biochemistry 22:1901-1906.
    • (1983) Biochemistry , vol.22 , pp. 1901-1906
    • Wemmer, D.1    Kallenbach, N.R.2
  • 41
    • 0028358189 scopus 로고
    • One-disulfide intermediates of apamin exhibit native-like structure
    • Xu X, Nelson JW. 1994. One-disulfide intermediates of apamin exhibit native-like structure. Biochemistry 33:5253-5261.
    • (1994) Biochemistry , vol.33 , pp. 5253-5261
    • Xu, X.1    Nelson, J.W.2
  • 42
    • 0024428106 scopus 로고
    • Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids
    • Zhang RM, Snyder GH. 1989. Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids. J Biol Chem 264:18472-18479.
    • (1989) J Biol Chem , vol.264 , pp. 18472-18479
    • Zhang, R.M.1    Snyder, G.H.2
  • 43
    • 0026348466 scopus 로고
    • Factors governing selective formation of specific disulfides in synthetic variants of α-conotoxin
    • Zhang R, Snyder GH. 1991. Factors governing selective formation of specific disulfides in synthetic variants of α-conotoxin. Biochemistry 30:11343-11348.
    • (1991) Biochemistry , vol.30 , pp. 11343-11348
    • Zhang, R.1    Snyder, G.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.