메뉴 건너뛰기




Volumn 381, Issue 2, 2000, Pages 127-133

Enhancing the T→R transition of insulin by helix-promoting sequence modifications at the N-terminal B-chain

Author keywords

Allosterism; Circular dichroism; Ligands; N cap; Semisynthesis; Titration

Indexed keywords

INORGANIC COMPOUND; INSULIN; ION; PHENOL DERIVATIVE; COBALT; THIOCYANIC ACID DERIVATIVE; ZINC;

EID: 0033624860     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2000.018     Document Type: Article
Times cited : (8)

References (41)
  • 2
    • 0025767755 scopus 로고
    • 2-Chlorotrityl chloride resin: Studies on anchoring of Fmoc-amino acids and peptide cleavage
    • Barlos, K., Chatzi, O., Gatos, D., and Stavropoulos, G. (1991). 2-Chlorotrityl chloride resin: studies on anchoring of Fmoc-amino acids and peptide cleavage. Int. J. Peptide Prot. Res. 37, 513-520.
    • (1991) Int. J. Peptide Prot. Res. , vol.37 , pp. 513-520
    • Barlos, K.1    Chatzi, O.2    Gatos, D.3    Stavropoulos, G.4
  • 5
    • 0029006864 scopus 로고
    • The α-helix as seen from the protein tertiary structure: A 3-D structural classification
    • Blundell, T.L., and Zhu, Z.-Y. (1995). The α-helix as seen from the protein tertiary structure: a 3-D structural classification. Biophys. Chem. 55, 167-184.
    • (1995) Biophys. Chem. , vol.55 , pp. 167-184
    • Blundell, T.L.1    Zhu, Z.-Y.2
  • 6
    • 0025744390 scopus 로고
    • Characterization of the R-state insulin hexamer and its derivatives. The hexamer is stabilized by heterotropic ligand binding interactions
    • Brader, M.L., Kaarsholm, N.C., Lee, R. W.-K., and Dunn, M.F. (1991). Characterization of the R-state insulin hexamer and its derivatives. The hexamer is stabilized by heterotropic ligand binding interactions. Biochemistry 30, 6636-6645.
    • (1991) Biochemistry , vol.30 , pp. 6636-6645
    • Brader, M.L.1    Kaarsholm, N.C.2    Lee, R.W.-K.3    Dunn, M.F.4
  • 7
    • 0028150624 scopus 로고
    • Structural asymmetry and half-site reactivity in the T to R allosteric transition of the insulin hexamer
    • Brzović, P.S., Choi, W.E., Borchardt, D., Kaarsholm, N.C., and Dunn, M.F. (1994). Structural asymmetry and half-site reactivity in the T to R allosteric transition of the insulin hexamer. Biochemistry 33, 13057-13069.
    • (1994) Biochemistry , vol.33 , pp. 13057-13069
    • Brzović, P.S.1    Choi, W.E.2    Borchardt, D.3    Kaarsholm, N.C.4    Dunn, M.F.5
  • 8
    • 0027367977 scopus 로고
    • Helix capping propensities in peptides parallel those in proteins
    • Chakrabartty, A., Doig, A.J., and Baldwin, R.L. (1993). Helix capping propensities in peptides parallel those in proteins. Proc. Natl. Acad. Sci. USA 90, 11332-11336.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11332-11336
    • Chakrabartty, A.1    Doig, A.J.2    Baldwin, R.L.3
  • 9
    • 0000367088 scopus 로고
    • Tow-point calibration of circular dichrometer with d-10-camphersulfonic acid
    • Chen, G.C., and Yang, J.T. (1977). Tow-point calibration of circular dichrometer with d-10-camphersulfonic acid. Anal. Lett. 10, 1195-1207.
    • (1977) Anal. Lett. , vol.10 , pp. 1195-1207
    • Chen, G.C.1    Yang, J.T.2
  • 10
    • 0027454260 scopus 로고
    • The allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions
    • Choi, W.E., Brader, M.L., Aguilar, V., Kaarsholm, N.C., and Dunn, M.F. (1993). The allosteric transition of the insulin hexamer is modulated by homotropic and heterotropic interactions. Biochemistry 32, 11638-11645.
    • (1993) Biochemistry , vol.32 , pp. 11638-11645
    • Choi, W.E.1    Brader, M.L.2    Aguilar, V.3    Kaarsholm, N.C.4    Dunn, M.F.5
  • 11
    • 0017868338 scopus 로고
    • Emperical predictions of protein conformation
    • Chou, P.Y., and Fasman, G.D. (1978). Emperical predictions of protein conformation. Ann. Rev. Biochem. 47, 258-276.
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 258-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 14
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N-and C-capping
    • Doig, A.J., Chakrabartty, A., Klingler, T.M., and Baldwin, R.L. (1994). Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N-and C-capping. Biochemistry 33, 3396-3403.
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 15
    • 0001394390 scopus 로고
    • Preparation of phenyl thiohydantions from some natural amino acids
    • Edman, P. (1950). Preparation of phenyl thiohydantions from some natural amino acids. Acta. Chim. Scand. 4, 277-282.
    • (1950) Acta. Chim. Scand. , vol.4 , pp. 277-282
    • Edman, P.1
  • 16
    • 0342279052 scopus 로고
    • Der methylsulfonyläthyloxycarbonyl-rest als reversible aminoschutzgruppe für insulin
    • Geiger, R., Obermeier, R., and Tesser, G.I. (1975). Der Methylsulfonyläthyloxycarbonyl-Rest als reversible Aminoschutzgruppe für Insulin. Chem. Ber. 108, 2758-2763.
    • (1975) Chem. Ber. , vol.108 , pp. 2758-2763
    • Geiger, R.1    Obermeier, R.2    Tesser, G.I.3
  • 17
    • 0026561058 scopus 로고
    • 6 allosteric transition of the Co(II) substituted insulin hexamer
    • 6 allosteric transition of the Co(II) substituted insulin hexamer. Biochemistry 31, 1295-1301.
    • (1992) Biochemistry , vol.31 , pp. 1295-1301
    • Gross, L.1    Dunn, M.F.2
  • 19
    • 0027654704 scopus 로고
    • Distinction of structural reorganisation and ligand binding in the T→R transition of insulin on the basis of allosteric models
    • Jacoby, E., Krüger, P., Karatas, Y., and Wollmer, A. (1993). Distinction of structural reorganisation and ligand binding in the T→R transition of insulin on the basis of allosteric models. Biol. Chem. Hoppe-Seyler 374, 877-885.
    • (1993) Biol. Chem. Hoppe-seyler , vol.374 , pp. 877-885
    • Jacoby, E.1    Krüger, P.2    Karatas, Y.3    Wollmer, A.4
  • 21
    • 0024356816 scopus 로고
    • Comparison of the solution structural flexibility and zinc binding domains for insulin, proinsulin and miniproinsulin
    • Kaarsholm, N.C., Ko, H.C., and Dunn, M.F. (1989). Comparison of the solution structural flexibility and zinc binding domains for insulin, proinsulin and miniproinsulin. Biochemistry 28, 4427-4435.
    • (1989) Biochemistry , vol.28 , pp. 4427-4435
    • Kaarsholm, N.C.1    Ko, H.C.2    Dunn, M.F.3
  • 22
    • 0014820265 scopus 로고
    • A new method for the synthesis of peptides: Activation of the carboxyl group with dicyclohexyl-carbodiimide and 3-hydroxy-4-oxo-3,4-dihydro-1,2,3-benzotriazine
    • König, W., and Geiger, R. (1970). A new method for the synthesis of peptides: activation of the carboxyl group with dicyclohexyl-carbodiimide and 3-hydroxy-4-oxo-3,4-dihydro-1,2,3-benzotriazine. Chem. Ber. 103, 2034-2044.
    • (1970) Chem. Ber. , vol.103 , pp. 2034-2044
    • König, W.1    Geiger, R.2
  • 23
    • 0025125376 scopus 로고
    • Cooperativity and intermediate states in the T→R-structural transformation of insulin
    • Krüger, P., Gilge, G., Cabuk, Y., and Wollmer, A. (1990). Cooperativity and intermediate states in the T→R-structural transformation of insulin. Biol. Chem. Hoppe-Seyler 371, 669-673.
    • (1990) Biol. Chem. Hoppe-seyler , vol.371 , pp. 669-673
    • Krüger, P.1    Gilge, G.2    Cabuk, Y.3    Wollmer, A.4
  • 24
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting α-helices: Position-specific analysis of a-helices in globular proteins
    • Kumar, S., and Bansal, M. (1998). Dissecting α-helices: position-specific analysis of a-helices in globular proteins. Proteins: Structure, Function, and Genetics 31, 460-476.
    • (1998) Proteins: Structure, Function, and Genetics , vol.31 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 25
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. (1997a). A direct comparison of helix propensity in proteins and peptides. Proc. Natl. Acad. Sci. USA 94, 2833-2837.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 26
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. (1997b). Helix propensities are identical in proteins and peptides. Biochemistry 36, 10923-10929.
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 27
    • 0032562654 scopus 로고    scopus 로고
    • Position dependence of non-polar amino acid intrinsic helical propensities
    • Petukhov, M., Munoz, V., Yumoto, N., Yoshikawa, S., and Serrano, L. (1998). Position dependence of non-polar amino acid intrinsic helical propensities. J. Mol. Biol. 278, 279-289.
    • (1998) J. Mol. Biol. , vol.278 , pp. 279-289
    • Petukhov, M.1    Munoz, V.2    Yumoto, N.3    Yoshikawa, S.4    Serrano, L.5
  • 28
    • 0031010619 scopus 로고    scopus 로고
    • Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions
    • Rahuel-Clermont, S., French, C.A., Kaarsholm, N.C., and Dunn, M.F. (1997). Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions. Biochemistry 36, 5837-5845.
    • (1997) Biochemistry , vol.36 , pp. 5837-5845
    • Rahuel-Clermont, S.1    French, C.A.2    Kaarsholm, N.C.3    Dunn, M.F.4
  • 30
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson, J.S., and Richardson, D.C. (1988). Amino acid preferences for specific locations at the ends of α helices. Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 31
    • 0024807512 scopus 로고
    • Spectroscopic signatures of the T to R conformational transition in the insulin hexamer
    • Roy, M., Brader, M.L., Lee, R.W.-K., Kaarlsholm, N.C., Hansen, J.F., and Dunn, M.F. (1989). Spectroscopic signatures of the T to R conformational transition in the insulin hexamer. J. Biol. Chem. 264, 19081-19085.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19081-19085
    • Roy, M.1    Brader, M.L.2    Lee, R.W.-K.3    Kaarlsholm, N.C.4    Hansen, J.F.5    Dunn, M.F.6
  • 32
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano, L., and Fersht, A.R. (1989). Capping and α-helix stability. Nature 342, 296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 33
    • 12444283342 scopus 로고
    • A new method of forming peptide bonds
    • Sheehan, J.C., and Hess, G.P. (1955). A new method of forming peptide bonds. J. Amer. Chem. Soc. 77, 1067-1068.
    • (1955) J. Amer. Chem. Soc. , vol.77 , pp. 1067-1068
    • Sheehan, J.C.1    Hess, G.P.2
  • 34
    • 0024792755 scopus 로고
    • Cobalt probing of structural alternatives for insulin in solution
    • Thomas, B., and Wollmer, A. (1989). Cobalt probing of structural alternatives for insulin in solution. Biol. Chem. Hoppe-Seyler 370, 1235-1244.
    • (1989) Biol. Chem. Hoppe-seyler , vol.370 , pp. 1235-1244
    • Thomas, B.1    Wollmer, A.2
  • 36
    • 0028849027 scopus 로고
    • X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol
    • Whittingham, J.L., Chaudhuri, S., Dodson, E.J., Moody, P.C.E., and Dodson, G.G. (1995). X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol. Biochemistry 34, 15553-15563.
    • (1995) Biochemistry , vol.34 , pp. 15553-15563
    • Whittingham, J.L.1    Chaudhuri, S.2    Dodson, E.J.3    Moody, P.C.E.4    Dodson, G.G.5
  • 38
    • 0024466401 scopus 로고
    • Structural transition in the metal-free hexamer of protein-engineered [B13Gln]insulin
    • Wollmer, A., Rannefeld, B., Stahl, J., and Melberg, S.G. (1989). Structural transition in the metal-free hexamer of protein-engineered [B13Gln]insulin. Biol. Chem. Hoppe-Seyler 370, 1045-1053.
    • (1989) Biol. Chem. Hoppe-seyler , vol.370 , pp. 1045-1053
    • Wollmer, A.1    Rannefeld, B.2    Stahl, J.3    Melberg, S.G.4
  • 39
    • 84946648081 scopus 로고
    • Mehrfunktionelle aminosäuren und ihre einbeziehung in die chemische synthese
    • Houben-Weyl, (Stuttgart, Germany: Georg Thieme Verlag)
    • Wünsch, E. (1974). Mehrfunktionelle Aminosäuren und ihre Einbeziehung in die chemische Synthese. In: Präparative Methoden in der Organischen Chemie, Vol. 15/1, Houben-Weyl, (Stuttgart, Germany: Georg Thieme Verlag), p. 51.
    • (1974) Präparative Methoden in der Organischen Chemie , vol.15 , Issue.1 , pp. 51
    • Wünsch, E.1
  • 40
    • 0030925636 scopus 로고    scopus 로고
    • The role of context on α-helix stabilization: Host-guest analysis in a mixed background peptide model
    • Yang, J., Spek, E.J., Gong, Y., Zhou, H., and Kallenbach, N.R. (1997). The role of context on α-helix stabilization: host-guest analysis in a mixed background peptide model. Prot. Sci. 6, 1264-1272.
    • (1997) Prot. Sci. , vol.6 , pp. 1264-1272
    • Yang, J.1    Spek, E.J.2    Gong, Y.3    Zhou, H.4    Kallenbach, N.R.5
  • 41
    • 0030581145 scopus 로고    scopus 로고
    • The use of amino acid patterns of classified helices and strands in secondary structure prediction
    • Zhu, Z.-Y., and Blundell, T.L. (1996). The use of amino acid patterns of classified helices and strands in secondary structure prediction. J. Mol. Biol. 260, 261-276.
    • (1996) J. Mol. Biol. , vol.260 , pp. 261-276
    • Zhu, Z.-Y.1    Blundell, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.