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Volumn 5, Issue , 2011, Pages 395-417

Role of Disulfide Bonds in Peptide and Protein Conformation

Author keywords

Conformation stability; Cysteine framework; Disulfide bond; Disulfide connectivity; Dynamics; Folding

Indexed keywords


EID: 84870878146     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527631841.ch11     Document Type: Chapter
Times cited : (31)

References (122)
  • 1
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981) The anatomy and taxonomy of protein structure. Advances in Protein Chemistry, 34, 167-339.
    • (1981) Advances in Protein Chemistry , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 3
    • 1442356427 scopus 로고    scopus 로고
    • Role of disulfide bonds in the structure and activity of human insulin
    • Chang, S.-G., Choi, K.-D., Jang, S.-H., and Shin, H.-C. (2003) Role of disulfide bonds in the structure and activity of human insulin. Molecules and Cells, 16, 323-330.
    • (2003) Molecules and Cells , vol.16 , pp. 323-330
    • Chang, S.-G.1    Choi, K.-D.2    Jang, S.-H.3    Shin, H.-C.4
  • 4
    • 0033533380 scopus 로고    scopus 로고
    • Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nanoindentation and elasticity measurement with an AFM
    • Parbhu, A.N., Bryson, W.G., and Lal, R. (1999) Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nanoindentation and elasticity measurement with an AFM. Biochemistry, 38, 11755-11761.
    • (1999) Biochemistry , vol.38 , pp. 11755-11761
    • Parbhu, A.N.1    Bryson, W.G.2    Lal, R.3
  • 5
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt, C., Lillig, C.H., and Holmgren, A. (2008) Thioredoxins and glutaredoxins as facilitators of protein folding. Biochimica et Biophysica Acta, 1783, 641-650.
    • (2008) Biochimica et Biophysica Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 6
  • 7
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure, 3, 239-243.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 8
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford, D. (2004) The role of cysteine residues as redox-sensitive regulatory switches. Current Opinion in Structural Biology, 14, 679-686.
    • (2004) Current Opinion in Structural Biology , vol.14 , pp. 679-686
    • Barford, D.1
  • 9
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg, P.J. (2003) Disulfide bonds as switches for protein function. Trends in Biochemical Sciences, 28, 210-214.
    • (2003) Trends in Biochemical Sciences , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 14
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • Kay, L.E. (2005) NMR studies of protein structure and dynamics. Journal of Magnetic Resonance, 173, 193-207.
    • (2005) Journal of Magnetic Resonance , vol.173 , pp. 193-207
    • Kay, L.E.1
  • 15
    • 33646172143 scopus 로고    scopus 로고
    • Structural classification of small, disulfide-rich protein domains
    • Cheek, S., Krishna, S.S., and Grishin, N.V. (2006) Structural classification of small, disulfide-rich protein domains. Journal of Molecular Biology, 359, 215-237.
    • (2006) Journal of Molecular Biology , vol.359 , pp. 215-237
    • Cheek, S.1    Krishna, S.S.2    Grishin, N.V.3
  • 16
    • 58649113381 scopus 로고    scopus 로고
    • Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families
    • Thangudu, R.R., Manoharan, M., Srinivasan, N., Cadet, F., Sowdhamini, R., and Offmann, B. (2008) Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families. BMC Structural Biology, 8, 55.
    • (2008) BMC Structural Biology , vol.8 , pp. 55
    • Thangudu, R.R.1    Manoharan, M.2    Srinivasan, N.3    Cadet, F.4    Sowdhamini, R.5    Offmann, B.6
  • 17
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton, J.M. (1981) Disulphide bridges in globular proteins. Journal of Molecular Biology, 151, 261-287.
    • (1981) Journal of Molecular Biology , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 18
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A.J. and Williams, D.H. (1991) Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. Journal of Molecular Biology, 217, 389-398.
    • (1991) Journal of Molecular Biology , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 19
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • Betz, S.F. (1993) Disulfide bonds and the stability of globular proteins. Protein Science, 2, 1551-1558.
    • (1993) Protein Science , vol.2 , pp. 1551-1558
    • Betz, S.F.1
  • 20
    • 0027390460 scopus 로고
    • The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state
    • Tidor, B. and Karplus, M. (1993) The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state. Proteins, 15, 71-79.
    • (1993) Proteins , vol.15 , pp. 71-79
    • Tidor, B.1    Karplus, M.2
  • 21
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • Katz, B.A. and Kossiakoff, A. (1986) The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. Journal of Biological Chemistry, 261, 15480-15485.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 22
    • 0025307389 scopus 로고
    • Crystal structure of subtilisin BPN0 variants containing disulfide bonds and cavities: concerted structural rearrangements induced by mutagenesis
    • Katz, B. and Kossiakoff, A.A. (1990) Crystal structure of subtilisin BPN0 variants containing disulfide bonds and cavities: concerted structural rearrangements induced by mutagenesis. Proteins, 7, 343-357.
    • (1990) Proteins , vol.7 , pp. 343-357
    • Katz, B.1    Kossiakoff, A.A.2
  • 23
    • 0032493315 scopus 로고    scopus 로고
    • Roles of individual disulfide bonds in the stability and folding of an v-conotoxin
    • Price-Carter, M., Hull, M.S., and Goldenberg, D.P. (1998) Roles of individual disulfide bonds in the stability and folding of an v-conotoxin. Biochemistry, 37, 9851-9861.
    • (1998) Biochemistry , vol.37 , pp. 9851-9861
    • Price-carter, M.1    Hull, M.S.2    Goldenberg, D.P.3
  • 25
    • 24044433278 scopus 로고    scopus 로고
    • Stability constraints and protein evolution: the role of chain length, composition and disulfide bonds
    • Bastolla, U. and Demetrius, L. (2005) Stability constraints and protein evolution: the role of chain length, composition and disulfide bonds. Protein Engineering, Design and Selection, 18, 405-415.
    • (2005) Protein Engineering, Design and Selection , vol.18 , pp. 405-415
    • Bastolla, U.1    Demetrius, L.2
  • 26
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 30
    • 0030797806 scopus 로고    scopus 로고
    • Protein folding coupled to disulfide bond formation
    • Creighton, T.E. (1997) Protein folding coupled to disulfide bond formation. Biological Chemistry, 378, 731-744.
    • (1997) Biological Chemistry , vol.378 , pp. 731-744
    • Creighton, T.E.1
  • 31
    • 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 Science, 3, 1822-1832.
    • (1994) Protein Science , vol.3 , pp. 1822-1832
    • Staley, J.P.1    Kim, P.S.2
  • 32
    • 0028180377 scopus 로고
    • 1H-NMRanalysis of the partlyfolded 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, C.P.M., Kemmink, J., Neuhaus, D., Darby, N.J., and Creighton, T.E. (1994) 1H-NMRanalysis of the partlyfolded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology, 235, 1044-1061.
    • (1994) Journal of Molecular Biology , vol.235 , pp. 1044-1061
    • Van Mierlo, C.P.M.1    Kemmink, J.2    Neuhaus, D.3    Darby, N.J.4    Creighton, T.E.5
  • 33
    • 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 Journal, 10, 110-118.
    • (1996) FASEB Journal , vol.10 , pp. 110-118
    • Creighton, T.E.1    Darby, N.J.2    Kemmink, J.3
  • 34
    • 0037066087 scopus 로고    scopus 로고
    • Initial disulfide formation steps in the folding of an v-conotoxin
    • Price-Carter, M., Bulaj, G., and Goldenberg, D.P. (2002) Initial disulfide formation steps in the folding of an v-conotoxin. Biochemistry, 41, 3507-3519.
    • (2002) Biochemistry , vol.41 , pp. 3507-3519
    • Price-carter, M.1    Bulaj, G.2    Goldenberg, D.P.3
  • 35
    • 0017397751 scopus 로고
    • Kinetics of refolding of reduced ribonuclease
    • Creighton, T.E. (1977) Kinetics of refolding of reduced ribonuclease. Journal of Molecular Biology, 113, 329-341.
    • (1977) Journal of Molecular Biology , vol.113 , pp. 329-341
    • Creighton, T.E.1
  • 36
    • 0018791296 scopus 로고
    • Intermediates in the refolding of reduced ribonuclease A
    • Creighton, T.E. (1979) Intermediates in the refolding of reduced ribonuclease A. Journal of Molecular Biology, 129, 411-431.
    • (1979) Journal of Molecular Biology , vol.129 , pp. 411-431
    • Creighton, T.E.1
  • 37
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton, T.E. (1986) Disulfide bonds as probes of protein folding pathways. Methods in Enzymology, 131, 83-106.
    • (1986) Methods in Enzymology , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 38
    • 0029162633 scopus 로고
    • Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1
    • Frech, C. and Schmid, F.X. (1995) Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1. Journal of Molecular Biology, 251, 135-149.
    • (1995) Journal of Molecular Biology , vol.251 , pp. 135-149
    • Frech, C.1    Schmid, F.X.2
  • 39
    • 0035822622 scopus 로고    scopus 로고
    • Coupling of conformational folding and disulfidebond reactions in oxidative folding of proteins
    • Welker, E., Wedemeyer, W.J., Narayan, M., and Scheraga, H.A. (2001) Coupling of conformational folding and disulfidebond reactions in oxidative folding of proteins. Biochemistry, 40, 9059-9064.
    • (2001) Biochemistry , vol.40 , pp. 9059-9064
    • Welker, E.1    Wedemeyer, W.J.2    Narayan, M.3    Scheraga, H.A.4
  • 41
    • 84885773220 scopus 로고    scopus 로고
    • Oxidative folding of single-stranded disulfide-rich peptides
    • in Oxidative Folding of Peptides and Proteins (eds J. Buchner and L. Moroder), Royal Society of Chemistry, London
    • Bulaj, G. and Walewska, A. (2009) Oxidative folding of single-stranded disulfide-rich peptides, in Oxidative Folding of Peptides and Proteins (eds J. Buchner and L. Moroder), Royal Society of Chemistry, London, pp. 296.
    • (2009) , pp. 296
    • Bulaj, G.1    Walewska, A.2
  • 42
    • 0037016671 scopus 로고    scopus 로고
    • Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
    • Winter, J., Klappa, P., Freedman, R.B., Lilie, H., and Rudolph, R. (2002) Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. Journal of Biological Chemistry, 277, 310-317.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 310-317
    • Winter, J.1    Klappa, P.2    Freedman, R.B.3    Lilie, H.4    Rudolph, R.5
  • 44
    • 0344198482 scopus 로고    scopus 로고
    • Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
    • Proceedings of the NationalAcademy of Sciences of the United States of America
    • Bulaj, G., Buczek, O., Goodsell, I., Jimenez, E.C., Kranski, J., Nielsen, J.S., Garrett, J.E., and Olivera, B.M. (2003) Efficient oxidative folding of conotoxins and the radiation of venomous cone snails. Proceedings of the NationalAcademy of Sciences of the United States of America, 100 (Suppl. 2), 14562-14568.
    • (2003) , vol.100 , Issue.SUPPL. 2 , pp. 14562-14568
    • Bulaj, G.1    Buczek, O.2    Goodsell, I.3    Jimenez, E.C.4    Kranski, J.5    Nielsen, J.S.6    Garrett, J.E.7    Olivera, B.M.8
  • 45
    • 0042324395 scopus 로고    scopus 로고
    • Analysis of the effect of potato carboxypeptidase inhibitor pro-sequence on the folding of the mature protein
    • Bronsoms, S., Villanueva, J., Canals, F., Querol, E., and Aviles, F.X. (2003) Analysis of the effect of potato carboxypeptidase inhibitor pro-sequence on the folding of the mature protein. European Journal of Biochemistry, 270, 3641-3650.
    • (2003) European Journal of Biochemistry , vol.270 , pp. 3641-3650
    • Bronsoms, S.1    Villanueva, J.2    Canals, F.3    Querol, E.4    Aviles, F.X.5
  • 46
    • 0942279699 scopus 로고    scopus 로고
    • Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor
    • Buczek, O., Olivera, B.M., and Bulaj, G. (2004) Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor. Biochemistry, 43, 1093-1101.
    • (2004) Biochemistry , vol.43 , pp. 1093-1101
    • Buczek, O.1    Olivera, B.M.2    Bulaj, G.3
  • 47
    • 3543112006 scopus 로고    scopus 로고
    • Role of disulfide bonds for the structure and folding of proguanylin
    • Lauber, T., Schulz, A., Rosch, P., and Marx, U.C. (2004) Role of disulfide bonds for the structure and folding of proguanylin. Biochemistry, 43, 10050-10057.
    • (2004) Biochemistry , vol.43 , pp. 10050-10057
    • Lauber, T.1    Schulz, A.2    Rosch, P.3    Marx, U.C.4
  • 48
    • 70149110001 scopus 로고    scopus 로고
    • Detecting folding intermediates of a protein as it passes through the bacterial translocation channel
    • Kadokura, H. and Beckwith, J. (2009) Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell, 138, 1164-1173.
    • (2009) Cell , vol.138 , pp. 1164-1173
    • Kadokura, H.1    Beckwith, J.2
  • 49
    • 51249121549 scopus 로고    scopus 로고
    • Functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor
    • Zakharova, E., Horvath, M.P., and Goldenberg, D.P. (2008) Functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology, 382, 998-1013.
    • (2008) Journal of Molecular Biology , vol.382 , pp. 998-1013
    • Zakharova, E.1    Horvath, M.P.2    Goldenberg, D.P.3
  • 50
    • 0032477917 scopus 로고    scopus 로고
    • Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation
    • Drakopoulou, E., Vizzavona, J., Neyton, J., Aniort, V., Bouet, F., Virelizier, H., Menez, A., and Vita, C. (1998) Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation. Biochemistry, 37, 1292-1301.
    • (1998) Biochemistry , vol.37 , pp. 1292-1301
    • Drakopoulou, E.1    Vizzavona, J.2    Neyton, J.3    Aniort, V.4    Bouet, F.5    Virelizier, H.6    Menez, A.7    Vita, C.8
  • 51
    • 64349101308 scopus 로고    scopus 로고
    • Structure of the analgesic m-conotoxin KIIIA and effects on the structure and function of disulfide deletion
    • Khoo, K.K., Feng, Z.-P., Smith, B.J., Zhang, M.-M., Yoshikami, D., Olivera, B.M., Bulaj, G., and Norton, R.S. (2009) Structure of the analgesic m-conotoxin KIIIA and effects on the structure and function of disulfide deletion. Biochemistry, 48, 1210-1219.
    • (2009) Biochemistry , vol.48 , pp. 1210-1219
    • Khoo, K.K.1    Feng, Z.-P.2    Smith, B.J.3    Zhang, M.-M.4    Yoshikami, D.5    Olivera, B.M.6    Bulaj, G.7    Norton, R.S.8
  • 53
    • 0029991679 scopus 로고    scopus 로고
    • Native and nonnative 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 nonnative structure in a protein-folding intermediate: spectroscopic studies of partially reduced IGF-I and an engineered alanine model. Journal of Molecular Biology, 259, 297-313.
    • (1996) Journal of Molecular Biology , 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
  • 55
    • 0033554391 scopus 로고    scopus 로고
    • NMR solution conformation of an antitoxic analog of a-conotoxin GI: identification of a common nicotinic acetylcholine receptor a1-subunit binding surface for small ligands and a-conotoxins
    • Mok, K.H. and Han, K.-H. (1999) NMR solution conformation of an antitoxic analog of a-conotoxin GI: identification of a common nicotinic acetylcholine receptor a1-subunit binding surface for small ligands and a-conotoxins. Biochemistry, 38, 11895-11904.
    • (1999) Biochemistry , vol.38 , pp. 11895-11904
    • Mok, K.H.1    Han, K.-H.2
  • 56
    • 0028841244 scopus 로고
    • Contribution of individual disulfide bonds to biological action of Escherichia coli heat-stable enterotoxin B
    • Arriaga, Y.L., Harville, B.A., and Dreyfus, L.A. (1995) Contribution of individual disulfide bonds to biological action of Escherichia coli heat-stable enterotoxin B. Infection and Immunity, 63, 4715-4720.
    • (1995) Infection and Immunity , vol.63 , pp. 4715-4720
    • Arriaga, Y.L.1    Harville, B.A.2    Dreyfus, L.A.3
  • 57
    • 0029417047 scopus 로고
    • Conformational changes of a-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution
    • Takeda, K., Ogawa, K., Ohara, M., Hamada, S., and Moriyama, Y. (1995) Conformational changes of a-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution. Journal of Protein Chemistry, 14, 679-684.
    • (1995) Journal of Protein Chemistry , vol.14 , pp. 679-684
    • Takeda, K.1    Ogawa, K.2    Ohara, M.3    Hamada, S.4    Moriyama, Y.5
  • 58
    • 0346374729 scopus 로고    scopus 로고
    • Cross-strand disulphides in cell entry proteins: poised to act
    • Wouters, M.A., Lau, K.K., and Hogg, P.J. (2004) Cross-strand disulphides in cell entry proteins: poised to act. Bioessays, 26, 73-79.
    • (2004) Bioessays , vol.26 , pp. 73-79
    • Wouters, M.A.1    Lau, K.K.2    Hogg, P.J.3
  • 60
    • 0032947950 scopus 로고    scopus 로고
    • Solution structure of a novel ETB receptor selective agonist ET1-21 [Cys(Acm)1,15, Aib3,11, Leu7] by nuclear magnetic resonance spectroscopy and molecular modelling
    • Hewage, C.M., Jiang, L., Parkinson, J.A., Ramage, R., and Sadler, I.H. (1999) Solution structure of a novel ETB receptor selective agonist ET1-21 [Cys(Acm)1,15, Aib3,11, Leu7] by nuclear magnetic resonance spectroscopy and molecular modelling. Journal of Peptide Research, 53, 223-233.
    • (1999) Journal of Peptide Research , vol.53 , pp. 223-233
    • Hewage, C.M.1    Jiang, L.2    Parkinson, J.A.3    Ramage, R.4    Sadler, I.H.5
  • 61
    • 0141611780 scopus 로고    scopus 로고
    • Protein dynamics from solution NMR: theory and applications
    • Kempf, J.G. and Loria, J.P. (2002) Protein dynamics from solution NMR: theory and applications. Cell Biochemistry and Biophysics, 37, 187-211.
    • (2002) Cell Biochemistry and Biophysics , vol.37 , pp. 187-211
    • Kempf, J.G.1    Loria, J.P.2
  • 62
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • Jarymowycz, V.A. and Stone, M.J. (2006) Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chemical Reviews, 106, 1624-1671.
    • (2006) Chemical Reviews , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 63
    • 33646931175 scopus 로고    scopus 로고
    • NMR residual dipolar couplings as probes of biomolecular dynamics
    • Tolman, J.R. and Ruan, K. (2006) NMR residual dipolar couplings as probes of biomolecular dynamics. Chemical Reviews, 106, 1720-1736.
    • (2006) Chemical Reviews , vol.106 , pp. 1720-1736
    • Tolman, J.R.1    Ruan, K.2
  • 64
    • 53749086169 scopus 로고    scopus 로고
    • Structure, dynamics, and selectivity of the sodium channel blocker m-conotoxin SIIIA
    • Yao, S., Zhang, M.-M., Yoshikami, D., Azam, L., Olivera, B.M., Bulaj, G., and Norton, R.S. (2008) Structure, dynamics, and selectivity of the sodium channel blocker m-conotoxin SIIIA. Biochemistry, 47, 10940-10949.
    • (2008) Biochemistry , vol.47 , pp. 10940-10949
    • Yao, S.1    Zhang, M.-M.2    Yoshikami, D.3    Azam, L.4    Olivera, B.M.5    Bulaj, G.6    Norton, R.S.7
  • 65
    • 0034087684 scopus 로고    scopus 로고
    • Backbone dynamics measurements on leukemia inhibitory factor, a rigid fourhelical bundle cytokine
    • Yao, S., Smith, D.K., Hinds, M.G., Zhang, J.G., Nicola, N.A., and Norton, R.S. (2000) Backbone dynamics measurements on leukemia inhibitory factor, a rigid fourhelical bundle cytokine. Protein Science, 9, 671-682.
    • (2000) Protein Science , vol.9 , pp. 671-682
    • Yao, S.1    Smith, D.K.2    Hinds, M.G.3    Zhang, J.G.4    Nicola, N.A.5    Norton, R.S.6
  • 67
    • 0033586730 scopus 로고    scopus 로고
    • Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H-NMR experiments
    • Storch, E.M., Grinstead, J.S., Campbell, A.P., Daggett, V., and Atkins, W.M. (1999) Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H-NMR experiments. Biochemistry, 38, 5065-5075.
    • (1999) Biochemistry , vol.38 , pp. 5065-5075
    • Storch, E.M.1    Grinstead, J.S.2    Campbell, A.P.3    Daggett, V.4    Atkins, W.M.5
  • 68
    • 0027393188 scopus 로고
    • Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using nitrogen-15 NMR relaxation measurements
    • Stone, M.J., Chandrasekhar, K., Holmgren, A., Wright, P.E., and Dyson, H.J. (1993) Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using nitrogen-15 NMR relaxation measurements. Biochemistry, 32, 426-435.
    • (1993) Biochemistry , vol.32 , pp. 426-435
    • Stone, M.J.1    Chandrasekhar, K.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5
  • 69
    • 0030993412 scopus 로고    scopus 로고
    • Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15NNMRrelaxation measurements
    • Kelley, J.J. 3rd, Caputo, T.M., Eaton, S.F., Laue, T.M., and Bushweller, J.H. (1997) Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15NNMRrelaxation measurements. Biochemistry, 36, 5029-5044.
    • (1997) Biochemistry , vol.36 , pp. 5029-5044
    • Kelley J.J.3rd1    Caputo, T.M.2    Eaton, S.F.3    Laue, T.M.4    Bushweller, J.H.5
  • 70
    • 0032545182 scopus 로고    scopus 로고
    • Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain
    • Beeser, S.A., Oas, T.G., and Goldenberg, D.P. (1998) Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain. Journal of Molecular Biology, 284, 1581-1596.
    • (1998) Journal of Molecular Biology , vol.284 , pp. 1581-1596
    • Beeser, S.A.1    Oas, T.G.2    Goldenberg, D.P.3
  • 71
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins. Trends in Biochemical Sciences, 27, 527-533.
    • (2002) Trends in Biochemical Sciences , vol.27 , pp. 527-533
    • Tompa, P.1
  • 72
    • 42749096469 scopus 로고    scopus 로고
    • Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2
    • Zhang, X., Perugini, M.A., Yao, S., Adda, C.G., Murphy, V.J., Low, A., Anders, R.F., and Norton, R.S. (2008) Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. Journal of Molecular Biology, 379, 105-121.
    • (2008) Journal of Molecular Biology , vol.379 , pp. 105-121
    • Zhang, X.1    Perugini, M.A.2    Yao, S.3    Adda, C.G.4    Murphy, V.J.5    Low, A.6    Anders, R.F.7    Norton, R.S.8
  • 74
    • 0041819762 scopus 로고    scopus 로고
    • Relationship between protein structures and disulfide-bonding patterns
    • Chuang, C.-C., Chen, C.-Y., Yang, J.-M., Lyu, P.-C., and Hwang, J.-K. (2003) Relationship between protein structures and disulfide-bonding patterns. Proteins, 53, 1-5.
    • (2003) Proteins , vol.53 , pp. 1-5
    • Chuang, C.-C.1    Chen, C.-Y.2    Yang, J.-M.3    Lyu, P.-C.4    Hwang, J.-K.5
  • 76
    • 0028222396 scopus 로고
    • Echistatin: the refined structure of a disintegrin in solution by 1H NMR and restrained molecular dynamics
    • Atkinson, R.A., Saudek, V., and Pelton, J.T. (1994) Echistatin: the refined structure of a disintegrin in solution by 1H NMR and restrained molecular dynamics. International Journal of Peptide and Protein Research, 43, 563-572.
    • (1994) International Journal of Peptide and Protein Research , vol.43 , pp. 563-572
    • Atkinson, R.A.1    Saudek, V.2    Pelton, J.T.3
  • 78
    • 0348111219 scopus 로고    scopus 로고
    • Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom
    • Shin, J., Hong, S.Y., Chung, K., Kang, I., Jang, Y., Kim, D.-s., and Lee, W. (2003) Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom. Biochemistry, 42, 14408-14415.
    • (2003) Biochemistry , vol.42 , pp. 14408-14415
    • Shin, J.1    Hong, S.Y.2    Chung, K.3    Kang, I.4    Jang, Y.5    Kim, D.-s.6    Lee, W.7
  • 79
    • 14744294145 scopus 로고    scopus 로고
    • Structure-function correlations of snake venom disintegrins
    • Calvete, J.J. (2005) Structure-function correlations of snake venom disintegrins. Current Pharmaceutical Design, 11, 829-835.
    • (2005) Current Pharmaceutical Design , vol.11 , pp. 829-835
    • Calvete, J.J.1
  • 80
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides
    • Pallaghy, P.K., Nielsen, K.J., Craik, D.J., and Norton, R.S. (1994) A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides. Protein Science, 3, 1833-1839.
    • (1994) Protein Science , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 81
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton, R.S. and Pallaghy, P.K. (1998) The cystine knot structure of ion channel toxins and related polypeptides. Toxicon, 36, 1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 82
    • 0031451746 scopus 로고    scopus 로고
    • Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus
    • Pallaghy, P.K., Alewood, D., Alewood, P.F., and Norton, R.S. (1997) Solution structure of robustoxin, the lethal neurotoxin from the funnel-web spider Atrax robustus. FEBS Letters, 419, 191-196.
    • (1997) FEBS Letters , vol.419 , pp. 191-196
    • Pallaghy, P.K.1    Alewood, D.2    Alewood, P.F.3    Norton, R.S.4
  • 83
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. Journal of Molecular Graphics, 14, 51-55.
    • (1996) Journal of Molecular Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 85
    • 33751049816 scopus 로고    scopus 로고
    • Conotoxins down under
    • Norton, R.S. and Olivera, B.M. (2006) Conotoxins down under. Toxicon, 48, 780-798.
    • (2006) Toxicon , vol.48 , pp. 780-798
    • Norton, R.S.1    Olivera, B.M.2
  • 86
    • 36148996891 scopus 로고    scopus 로고
    • Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of Conus peptides
    • Bulaj, G. and Olivera, B.M. (2008) Folding of conotoxins: formation of the native disulfide bridges during chemical synthesis and biosynthesis of Conus peptides. Antioxidants and Redox Signaling, 10, 141-156.
    • (2008) Antioxidants and Redox Signaling , vol.10 , pp. 141-156
    • Bulaj, G.1    Olivera, B.M.2
  • 87
    • 33947424873 scopus 로고    scopus 로고
    • Protein folding determinants: structural features determining alternative disulfide pairing in a- and x/l-conotoxins
    • Kang, T.S., Radic, Z., Talley, T.T., Jois, S.D.S., Taylor, P., and Kini, R.M. (2007) Protein folding determinants: structural features determining alternative disulfide pairing in a- and x/l-conotoxins. Biochemistry, 46, 3338-3355.
    • (2007) Biochemistry , vol.46 , pp. 3338-3355
    • Kang, T.S.1    Radic, Z.2    Talley, T.T.3    Jois, S.D.S.4    Taylor, P.5    Kini, R.M.6
  • 89
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (d-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel
    • Fletcher, J.I., Chapman, B.E., Mackay, J.P., Howden, M.E.H., and King, G.F. (1997) The structure of versutoxin (d-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel. Structure, 5, 1525-1535.
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    Mackay, J.P.3    Howden, M.E.H.4    King, G.F.5
  • 92
    • 34247565154 scopus 로고    scopus 로고
    • Solution structure of an M-1 conotoxin with a novel disulfide linkage
    • Du, W.-H., Han, Y.-H., Huang, F.-j., Li, J., Chi, C.-W., and Fang, W.-H. (2007) Solution structure of an M-1 conotoxin with a novel disulfide linkage. FEBS Journal, 274, 2596-2602.
    • (2007) FEBS Journal , vol.274 , pp. 2596-2602
    • Du, W.-H.1    Han, Y.-H.2    Huang, F.-J.3    Li, J.4    Chi, C.-W.5    Fang, W.-H.6
  • 95
    • 0026348466 scopus 로고
    • Factors governing selective formation of specific disulfides in synthetic variants of a-conotoxin
    • Zhang, R.M. and Snyder, G.H. (1991) Factors governing selective formation of specific disulfides in synthetic variants of a-conotoxin. Biochemistry, 30, 11343-11348.
    • (1991) Biochemistry , vol.30 , pp. 11343-11348
    • Zhang, R.M.1    Snyder, G.H.2
  • 96
    • 0032079381 scopus 로고    scopus 로고
    • Structure determination of the three disulfide bond isomers of a-conotoxin GI: a model for the role of disulfide bonds in structural stability
    • Gehrmann, J., Alewood, P.F., and Craik, D.J. (1998) Structure determination of the three disulfide bond isomers of a-conotoxin GI: a model for the role of disulfide bonds in structural stability. Journal of Molecular Biology, 278, 401-415.
    • (1998) Journal of Molecular Biology , vol.278 , pp. 401-415
    • Gehrmann, J.1    Alewood, P.F.2    Craik, D.J.3
  • 97
    • 0037073683 scopus 로고    scopus 로고
    • A new level of conotoxin diversity, a non-native disulfide bond connectivity in a-conotoxinAuIB reduces structural definition but increases biological activity
    • Dutton, J.L., Bansal, P.S., Hogg, R.C., Adams, D.J., Alewood, P.F., and Craik, D.J. (2002) A new level of conotoxin diversity, a non-native disulfide bond connectivity in a-conotoxinAuIB reduces structural definition but increases biological activity. Journal of Biological Chemistry, 277, 48849-48857.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 48849-48857
    • Dutton, J.L.1    Bansal, P.S.2    Hogg, R.C.3    Adams, D.J.4    Alewood, P.F.5    Craik, D.J.6
  • 100
    • 4143097228 scopus 로고    scopus 로고
    • Assignment of the four disulfides in the N-terminal somatomedin B domain of native vitronectin isolated from human plasma
    • Horn, N.A., Hurst, G.B., Mayasundari, A., Whittemore, N.A., Serpersu, E.H., and Peterson, C.B. (2004) Assignment of the four disulfides in the N-terminal somatomedin B domain of native vitronectin isolated from human plasma. Journal of Biological Chemistry, 279, 35867-35878.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 35867-35878
    • Horn, N.A.1    Hurst, G.B.2    Mayasundari, A.3    Whittemore, N.A.4    Serpersu, E.H.5    Peterson, C.B.6
  • 102
    • 3142711774 scopus 로고    scopus 로고
    • The solution structure of the N-terminal domain of human vitronectin: proximal sites that regulate fibrinolysis and cell migration
    • Mayasundari, A., Whittemore, N.A., Serpersu, E.H., and Peterson, C.B. (2004) The solution structure of the N-terminal domain of human vitronectin: proximal sites that regulate fibrinolysis and cell migration. Journal of Biological Chemistry, 279, 29359-29366.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 29359-29366
    • Mayasundari, A.1    Whittemore, N.A.2    Serpersu, E.H.3    Peterson, C.B.4
  • 104
    • 41549168582 scopus 로고    scopus 로고
    • A simplified approach to disulfide connectivity prediction from protein sequences
    • Vincent, M., Passerini, A., Labbe, M., and Frasconi, P. (2008) A simplified approach to disulfide connectivity prediction from protein sequences. BMC Bioinformatics, 9, 20.
    • (2008) BMC Bioinformatics , vol.9 , pp. 20
    • Vincent, M.1    Passerini, A.2    Labbe, M.3    Frasconi, P.4
  • 106
    • 36549021546 scopus 로고    scopus 로고
    • Predicting disulfide connectivity from protein sequence using multiple sequence feature vectors and secondary structure
    • Song, J., Yuan, Z., Tan, H., Huber, T., and Burrage, K. (2007) Predicting disulfide connectivity from protein sequence using multiple sequence feature vectors and secondary structure. Bioinformatics, 23, 3147-3154.
    • (2007) Bioinformatics , vol.23 , pp. 3147-3154
    • Song, J.1    Yuan, Z.2    Tan, H.3    Huber, T.4    Burrage, K.5
  • 107
    • 33744801136 scopus 로고    scopus 로고
    • Disulfide connectivity prediction with 70% accuracy using twolevel models
    • Chen, B.-J., Tsai, C.-H., Chan, C.-h., and Kao, C.-Y. (2006) Disulfide connectivity prediction with 70% accuracy using twolevel models. Proteins, 64, 246-252.
    • (2006) Proteins , vol.64 , pp. 246-252
    • Chen, B.-J.1    Tsai, C.-H.2    Chan, C.-h.3    Kao, C.-Y.4
  • 108
    • 17444411155 scopus 로고    scopus 로고
    • Cysteine separations profiles on protein sequences infer disulfide connectivity
    • Zhao, E., Liu, H.-L., Tsai, C.-H., Tsai, H.-K., Chan, C.-h., and Kao, C.-Y. (2005) Cysteine separations profiles on protein sequences infer disulfide connectivity. Bioinformatics, 21, 1415-1420.
    • (2005) Bioinformatics , vol.21 , pp. 1415-1420
    • Zhao, E.1    Liu, H.-L.2    Tsai, C.-H.3    Tsai, H.-K.4    Chan, C.-h.5    Kao, C.-Y.6
  • 109
    • 0035951063 scopus 로고    scopus 로고
    • Designed peptide analogs of the potassium channel blocker ShK toxin
    • Lanigan, M.D., Pennington, M.W., Lefievre, Y., Rauer, H., and Norton, R.S. (2001) Designed peptide analogs of the potassium channel blocker ShK toxin. Biochemistry, 40, 15528-15537.
    • (2001) Biochemistry , vol.40 , pp. 15528-15537
    • Lanigan, M.D.1    Pennington, M.W.2    Lefievre, Y.3    Rauer, H.4    Norton, R.S.5
  • 111
    • 16644375793 scopus 로고    scopus 로고
    • Formation of disulfide bonds in proteins and peptides
    • Bulaj, G. (2005) Formation of disulfide bonds in proteins and peptides. Biotechnology Advances, 23, 87-92.
    • (2005) Biotechnology Advances , vol.23 , pp. 87-92
    • Bulaj, G.1
  • 114
    • 14544294044 scopus 로고    scopus 로고
    • Conformationally restricted peptides as tools in opioid receptor studies
    • Janecka, A. and Kruszynski, R. (2005) Conformationally restricted peptides as tools in opioid receptor studies. Current Medicinal Chemistry, 12, 471-481.
    • (2005) Current Medicinal Chemistry , vol.12 , pp. 471-481
    • Janecka, A.1    Kruszynski, R.2
  • 116
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D.J., Daly, N.L., and Waine, C. (2001) The cystine knot motif in toxins and implications for drug design. Toxicon, 39, 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 119
    • 77949820036 scopus 로고    scopus 로고
    • Site-specific effects of diselenide bridges on the oxidative folding of v-selenoconotoxin GVIA
    • Gowd, K.H., Yarotskyy, V., Elmslie, K.S., Skalicky, J.J., Olivera, B.M., and Bulaj, G. (2010) Site-specific effects of diselenide bridges on the oxidative folding of v-selenoconotoxin GVIA. Biochemistry, 49, 2741-2752.
    • (2010) Biochemistry , vol.49 , pp. 2741-2752
    • Gowd, K.H.1    Yarotskyy, V.2    Elmslie, K.S.3    Skalicky, J.J.4    Olivera, B.M.5    Bulaj, G.6
  • 121
    • 65449157697 scopus 로고    scopus 로고
    • Thermal domain motions of CheA kinase in solution: disulfide trapping reveals the motional constraints leading to transautophosphorylation
    • Gloor, S.L. and Falke, J.J. (2009) Thermal domain motions of CheA kinase in solution: disulfide trapping reveals the motional constraints leading to transautophosphorylation. Biochemistry, 48, 3631-3644.
    • (2009) Biochemistry , vol.48 , pp. 3631-3644
    • Gloor, S.L.1    Falke, J.J.2
  • 122
    • 34250792303 scopus 로고    scopus 로고
    • Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis
    • Bass, R.B., Butler, S.L., Chervitz, S.A., Gloor, S.L., and Falke, J.J. (2007) Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis. Methods in Enzymology, 423, 25-51.
    • (2007) Methods in Enzymology , vol.423 , pp. 25-51
    • Bass, R.B.1    Butler, S.L.2    Chervitz, S.A.3    Gloor, S.L.4    Falke, J.J.5


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