메뉴 건너뛰기




Volumn 365, Issue 4, 2007, Pages 1232-1244

Influence of the Internal Disulfide Bridge on the Folding Pathway of the CL Antibody Domain

Author keywords

antibody folding; CL; disulfide bridges; folding intermediates; NMR

Indexed keywords

DISULFIDE; IMMUNOGLOBULIN; MONOMER; PROLINE; PROTEIN ANTIBODY; TYROSINE; UBIQUITIN;

EID: 33845747314     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.049     Document Type: Article
Times cited : (38)

References (64)
  • 1
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
    • Pace C.N., Grimsley G.R., Thomson J.A., and Barnett B.J. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem. 263 (Aug 1988) 11820-11825
    • (1988) J. Biol. Chem. , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Barnett, B.J.4
  • 2
    • 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. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217 (Jan 1991) 389-398
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 4
    • 0029820584 scopus 로고    scopus 로고
    • Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein
    • Hinck A.P., Truckses D.M., and Markley J.L. Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. Biochemistry 35 (Aug 1996) 10328-10338
    • (1996) Biochemistry , vol.35 , pp. 10328-10338
    • Hinck, A.P.1    Truckses, D.M.2    Markley, J.L.3
  • 5
    • 0037044333 scopus 로고    scopus 로고
    • The influence of intramolecular bridges on the dynamics of a protein folding reaction
    • Mason J.M., Gibbs N., Sessions R.B., and Clarke A.R. The influence of intramolecular bridges on the dynamics of a protein folding reaction. Biochemistry 41 (Oct 2002) 12093-12099
    • (2002) Biochemistry , vol.41 , pp. 12093-12099
    • Mason, J.M.1    Gibbs, N.2    Sessions, R.B.3    Clarke, A.R.4
  • 6
    • 0029562948 scopus 로고
    • Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat
    • Vogl T., Brengelmann R., Hinz H.J., Scharf M., Lotzbeyer M., and Engels J.W. Mechanism of protein stabilization by disulfide bridges: calorimetric unfolding studies on disulfide-deficient mutants of the alpha-amylase inhibitor tendamistat. J. Mol. Biol. 254 (Dec 1995) 481-496
    • (1995) J. Mol. Biol. , vol.254 , pp. 481-496
    • Vogl, T.1    Brengelmann, R.2    Hinz, H.J.3    Scharf, M.4    Lotzbeyer, M.5    Engels, J.W.6
  • 7
    • 0031694725 scopus 로고    scopus 로고
    • Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhibitor [C45A/C73A]tendamistat: an NMR study
    • Balbach J., Seip S., Kessler H., Scharf M., Kashani-Poor N., and Engels J.W. Structure and dynamic properties of the single disulfide-deficient alpha-amylase inhibitor [C45A/C73A]tendamistat: an NMR study. Proteins: Struct. Funct. Genet. 33 (Nov 1998) 285-294
    • (1998) Proteins: Struct. Funct. Genet. , vol.33 , pp. 285-294
    • Balbach, J.1    Seip, S.2    Kessler, H.3    Scharf, M.4    Kashani-Poor, N.5    Engels, J.W.6
  • 8
    • 29344441722 scopus 로고    scopus 로고
    • Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4
    • Vaz D.C., Rodrigues J.R., Sebald W., Dobson C.M., and Brito R.M.M. Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4. Protein Sci. 15 (Jan 2006) 33-44
    • (2006) Protein Sci. , vol.15 , pp. 33-44
    • Vaz, D.C.1    Rodrigues, J.R.2    Sebald, W.3    Dobson, C.M.4    Brito, R.M.M.5
  • 9
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • Schwalbe H., Fiebig K.M., Buck M., Jones J.A., Grimshaw S.B., Spencer A., et al. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry 36 (Jul 1997) 8977-8991
    • (1997) Biochemistry , vol.36 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5    Spencer, A.6
  • 10
    • 0034491013 scopus 로고    scopus 로고
    • The effects of disulfide bonds on the denatured state of barnase
    • Clarke J., Hounslow A.M., Bond C.J., Fersht A.R., and Daggett V. The effects of disulfide bonds on the denatured state of barnase. Protein Sci. 9 (Dec 2000) 2394-2404
    • (2000) Protein Sci. , vol.9 , pp. 2394-2404
    • Clarke, J.1    Hounslow, A.M.2    Bond, C.J.3    Fersht, A.R.4    Daggett, V.5
  • 11
    • 0028270993 scopus 로고
    • Intact disulfide bonds decelerate the folding of ribonuclease T1
    • Mucke M., and Schmid F.X. Intact disulfide bonds decelerate the folding of ribonuclease T1. J. Mol. Biol. 239 (Jun 1994) 713-725
    • (1994) J. Mol. Biol. , vol.239 , pp. 713-725
    • Mucke, M.1    Schmid, F.X.2
  • 12
    • 0028028126 scopus 로고
    • Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme
    • Eyles S.J., Radford S.E., Robinson C.V., and Dobson C.M. Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Biochemistry 33 (Nov 1994) 13038-13048
    • (1994) Biochemistry , vol.33 , pp. 13038-13048
    • Eyles, S.J.1    Radford, S.E.2    Robinson, C.V.3    Dobson, C.M.4
  • 13
    • 0041089466 scopus 로고    scopus 로고
    • Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for beta-sheet formation
    • Schonbrunner N., Pappenberger G., Scharf M., Engels J., and Kiefhaber T. Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for beta-sheet formation. Biochemistry 36 (Jul 1997) 9057-9065
    • (1997) Biochemistry , vol.36 , pp. 9057-9065
    • Schonbrunner, N.1    Pappenberger, G.2    Scharf, M.3    Engels, J.4    Kiefhaber, T.5
  • 14
    • 0034602924 scopus 로고    scopus 로고
    • The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge
    • Yokota A., Izutani K., Takai M., Kubo Y., Noda Y., Koumoto Y., et al. The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. J. Mol. Biol. 295 (Feb 2000) 1275-1288
    • (2000) J. Mol. Biol. , vol.295 , pp. 1275-1288
    • Yokota, A.1    Izutani, K.2    Takai, M.3    Kubo, Y.4    Noda, Y.5    Koumoto, Y.6
  • 15
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation
    • Clarke J., and Fersht A.R. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 32 (Apr 1993) 4322-4329
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 16
    • 0033462152 scopus 로고    scopus 로고
    • Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme
    • Roux P., Ruoppolo M., Chaffotte A.F., and Goldberg M.E. Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme. Protein Sci. 8 (Dec 1999) 2751-2760
    • (1999) Protein Sci. , vol.8 , pp. 2751-2760
    • Roux, P.1    Ruoppolo, M.2    Chaffotte, A.F.3    Goldberg, M.E.4
  • 17
    • 28844456360 scopus 로고    scopus 로고
    • Low energy pathways and non-native interactions: the influence of artificial disulfide bridges on the mechanism of folding
    • Mason J.M., Cliff M.J., Sessions R.B., and Clarke A.R. Low energy pathways and non-native interactions: the influence of artificial disulfide bridges on the mechanism of folding. J. Biol. Chem. 280 (Dec 2005) 40494-40499
    • (2005) J. Biol. Chem. , vol.280 , pp. 40494-40499
    • Mason, J.M.1    Cliff, M.J.2    Sessions, R.B.3    Clarke, A.R.4
  • 18
    • 0029162633 scopus 로고
    • Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1
    • Frech C., and Schmid F.X. Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1. J. Mol. Biol. 251 (Aug 1995) 135-149
    • (1995) J. Mol. Biol. , vol.251 , pp. 135-149
    • Frech, C.1    Schmid, F.X.2
  • 19
    • 0028818785 scopus 로고
    • A kinetic explanation for the rearrangement pathway of BPTI folding
    • Weissman J.S., and Kim P.S. A kinetic explanation for the rearrangement pathway of BPTI folding. Nat. Struct. Biol. 2 (Dec 1995) 1123-1130
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1123-1130
    • Weissman, J.S.1    Kim, P.S.2
  • 20
    • 0030797806 scopus 로고    scopus 로고
    • Protein folding coupled to disulphide bond formation
    • Creighton T.E. Protein folding coupled to disulphide bond formation. Biol. Chem. 378 (Aug 1997) 731-744
    • (1997) Biol. Chem. , vol.378 , pp. 731-744
    • Creighton, T.E.1
  • 21
    • 0034601830 scopus 로고    scopus 로고
    • Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A
    • Ruoppolo M., Vinci F., Klink T.A., Raines R.T., and Marino G. Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A. Biochemistry 39 (Oct 2000) 12033-12042
    • (2000) Biochemistry , vol.39 , pp. 12033-12042
    • Ruoppolo, M.1    Vinci, F.2    Klink, T.A.3    Raines, R.T.4    Marino, G.5
  • 23
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis
    • Abkevich V.I., and Shakhnovich E.I. What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioninformatics analysis. J. Mol. Biol. 300 (Jul 2000) 975-985
    • (2000) J. Mol. Biol. , vol.300 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 24
    • 0035793626 scopus 로고    scopus 로고
    • The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip
    • Augustine J.G., de La Calle A., Knarr G., Buchner J., and Frederick C.A. The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip. J. Biol. Chem. 276 (Feb 2001) 3287-3294
    • (2001) J. Biol. Chem. , vol.276 , pp. 3287-3294
    • Augustine, J.G.1    de La Calle, A.2    Knarr, G.3    Buchner, J.4    Frederick, C.A.5
  • 25
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P., Holm L., and Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 242 (Sep 1994) 309-320
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 26
    • 0018425934 scopus 로고
    • Folding pathways of immunoglobulin domains. The folding kinetics of the Cgamma3 domain of human IgG1
    • Isenman D.E., Lancet D., and Pecht I. Folding pathways of immunoglobulin domains. The folding kinetics of the Cgamma3 domain of human IgG1. Biochemistry 18 (Jul 1979) 3327-3336
    • (1979) Biochemistry , vol.18 , pp. 3327-3336
    • Isenman, D.E.1    Lancet, D.2    Pecht, I.3
  • 27
    • 0019958156 scopus 로고
    • Unfolding and refolding of the constant fragment of the immunoglobulin light chain
    • Goto Y., and Hamaguchi K. Unfolding and refolding of the constant fragment of the immunoglobulin light chain. J. Mol. Biol. 156 (Apr 1982) 891-910
    • (1982) J. Mol. Biol. , vol.156 , pp. 891-910
    • Goto, Y.1    Hamaguchi, K.2
  • 28
    • 0039154091 scopus 로고    scopus 로고
    • Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen
    • Jager M., and Pluckthun A. Folding and assembly of an antibody Fv fragment, a heterodimer stabilized by antigen. J. Mol. Biol. 285 (Feb 1999) 2005-2019
    • (1999) J. Mol. Biol. , vol.285 , pp. 2005-2019
    • Jager, M.1    Pluckthun, A.2
  • 29
    • 0033569502 scopus 로고    scopus 로고
    • Folding and association of the antibody domain CH3: prolyl isomerization precedes dimerization
    • Thies M.J., Mayer J., Augustine J.G., Frederick C.A., Lilie H., and Buchner J. Folding and association of the antibody domain CH3: prolyl isomerization precedes dimerization. J. Mol. Biol. 293 (Oct 1999) 67-79
    • (1999) J. Mol. Biol. , vol.293 , pp. 67-79
    • Thies, M.J.1    Mayer, J.2    Augustine, J.G.3    Frederick, C.A.4    Lilie, H.5    Buchner, J.6
  • 30
    • 7044247460 scopus 로고    scopus 로고
    • Folding mechanism of the CH2 antibody domain
    • Feige M.J., Walter S., and Buchner J. Folding mechanism of the CH2 antibody domain. J. Mol. Biol. 344 (Nov 2004) 107-118
    • (2004) J. Mol. Biol. , vol.344 , pp. 107-118
    • Feige, M.J.1    Walter, S.2    Buchner, J.3
  • 31
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • Clarke J., Hamill S.J., and Johnson C.M. Folding and stability of a fibronectin type III domain of human tenascin. J. Mol. Biol. 270 (Aug 1997) 771-778
    • (1997) J. Mol. Biol. , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 33
    • 0034677663 scopus 로고    scopus 로고
    • The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology
    • Hamill S.J., Steward A., and Clarke J. The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J. Mol. Biol. 297 (Mar 2000) 165-178
    • (2000) J. Mol. Biol. , vol.297 , pp. 165-178
    • Hamill, S.J.1    Steward, A.2    Clarke, J.3
  • 34
    • 0035793212 scopus 로고    scopus 로고
    • The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold
    • Cota E., Steward A., Fowler S.B., and Clarke J. The folding nucleus of a fibronectin type III domain is composed of core residues of the immunoglobulin-like fold. J. Mol. Biol. 305 (Feb 2001) 1185-1194
    • (2001) J. Mol. Biol. , vol.305 , pp. 1185-1194
    • Cota, E.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 35
    • 0037007446 scopus 로고    scopus 로고
    • A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments
    • Hoyer W., Ramm K., and Pluckthun A. A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments. Biophys. Chemist. 96 (May 2002) 273-284
    • (2002) Biophys. Chemist. , vol.96 , pp. 273-284
    • Hoyer, W.1    Ramm, K.2    Pluckthun, A.3
  • 36
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez I.E., and Kiefhaber T. Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol. 325 (Jan 2003) 367-376
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 37
    • 1642307617 scopus 로고    scopus 로고
    • The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions
    • Vu N.-D., Feng H., and Bai Y. The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. Biochemistry 43 (Mar 2004) 3346-3356
    • (2004) Biochemistry , vol.43 , pp. 3346-3356
    • Vu, N.-D.1    Feng, H.2    Bai, Y.3
  • 38
    • 20544462511 scopus 로고    scopus 로고
    • Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding
    • White G.W.N., Gianni S., Grossmann J.G., Jemth P., Fersht A.R., and Daggett V. Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding. J. Mol. Biol. 350 (Jul 2005) 757-775
    • (2005) J. Mol. Biol. , vol.350 , pp. 757-775
    • White, G.W.N.1    Gianni, S.2    Grossmann, J.G.3    Jemth, P.4    Fersht, A.R.5    Daggett, V.6
  • 39
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto Y., and Hamaguchi K. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. (Tokyo) 86 (Nov 1979) 1433-1441
    • (1979) J. Biochem. (Tokyo) , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 40
    • 0019965821 scopus 로고
    • Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain. Kinetic role of the intrachain disulfide bond
    • Goto Y., and Hamaguchi K. Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain. Kinetic role of the intrachain disulfide bond. J. Mol. Biol. 156 (Apr 1982) 911-926
    • (1982) J. Mol. Biol. , vol.156 , pp. 911-926
    • Goto, Y.1    Hamaguchi, K.2
  • 41
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for cell surface recognition
    • Williams A.F., and Barclay A.N. The immunoglobulin superfamily-domains for cell surface recognition. Annu. Rev. Immunol. 6 (1988) 381-405
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 44
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate
    • Wildegger G., and Kiefhaber T. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270 (Jul 1997) 294-304
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 45
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization: I. Theoretical models
    • Kiefhaber T., Kohler H.H., and Schmid F.X. Kinetic coupling between protein folding and prolyl isomerization: I. Theoretical models. J. Mol. Biol. 224 (Mar 1992) 217-229
    • (1992) J. Mol. Biol. , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Kohler, H.H.2    Schmid, F.X.3
  • 46
    • 0023285350 scopus 로고
    • Conformation of the constant fragment of the immunoglobulin light chain: effect of cleavage of the polypeptide chain and the disulfide bond
    • Goto Y., Tsunenaga M., Kawata Y., and Hamaguchi K. Conformation of the constant fragment of the immunoglobulin light chain: effect of cleavage of the polypeptide chain and the disulfide bond. J. Biochem. (Tokyo) 101 (Feb 1987) 319-329
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 319-329
    • Goto, Y.1    Tsunenaga, M.2    Kawata, Y.3    Hamaguchi, K.4
  • 47
    • 0014604482 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride: II. Dependence on denaturant concentration at 25 degrees
    • Aune K.C., and Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride: II. Dependence on denaturant concentration at 25 degrees. Biochemistry 8 (Nov 1969) 4586-4590
    • (1969) Biochemistry , vol.8 , pp. 4586-4590
    • Aune, K.C.1    Tanford, C.2
  • 48
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: a balance of contact interaction and excluded volume
    • (Evaluation Studies)
    • Schellman J.A. Protein stability in mixed solvents: a balance of contact interaction and excluded volume. Biophys. J. 85 (Jul 2003) 108-125 (Evaluation Studies)
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 49
    • 0023412433 scopus 로고
    • Fluorescence of the tryptophyl residues of the constant fragment of the immunoglobulin light chain
    • Kikuchi H., Goto Y., Hamaguchi K., Ito S., Yamamoto M., and Nishijima Y. Fluorescence of the tryptophyl residues of the constant fragment of the immunoglobulin light chain. J. Biochem. (Tokyo) 102 (Sep 1987) 651-656
    • (1987) J. Biochem. (Tokyo) , vol.102 , pp. 651-656
    • Kikuchi, H.1    Goto, Y.2    Hamaguchi, K.3    Ito, S.4    Yamamoto, M.5    Nishijima, Y.6
  • 50
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (Oct 1995) 2138-2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 52
    • 4644229995 scopus 로고    scopus 로고
    • The importance of loop length in the folding of an immunoglobulin domain
    • Wright C.F., Christodoulou J., Dobson C.M., and Clarke J. The importance of loop length in the folding of an immunoglobulin domain. Protein Eng. Des. Sel. 17 (May 2004) 443-453
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 443-453
    • Wright, C.F.1    Christodoulou, J.2    Dobson, C.M.3    Clarke, J.4
  • 53
    • 0033957144 scopus 로고    scopus 로고
    • Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module
    • Cota E., and Clarke J. Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module. Protein Sci. 9 (Jan 2000) 112-120
    • (2000) Protein Sci. , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 54
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 55
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro M.M., and Bolen D.W. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31 (May 1992) 4901-4907
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 56
    • 0001909564 scopus 로고    scopus 로고
    • Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy
    • Liu M., Mao X., He C., Huang H., Nicholson J.K., and Lindon J.C. Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy. J. Magn. Reson. 132 (1998) 125-129
    • (1998) J. Magn. Reson. , vol.132 , pp. 125-129
    • Liu, M.1    Mao, X.2    He, C.3    Huang, H.4    Nicholson, J.K.5    Lindon, J.C.6
  • 57
    • 0001424822 scopus 로고    scopus 로고
    • Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments
    • Jerschow A.M., and Mueller N. Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments. J. Magn. Reson. 125 (1997) 372-375
    • (1997) J. Magn. Reson. , vol.125 , pp. 372-375
    • Jerschow, A.M.1    Mueller, N.2
  • 58
    • 33646376290 scopus 로고
    • Spin diffusion measurements-spin echoes in presence of a time-dependent field gradient
    • Stejskal E.O., and Tanner J.E. Spin diffusion measurements-spin echoes in presence of a time-dependent field gradient. J. Chem. Phys. 42 (1965) 288-292
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 59
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • de la Torre J.G., Huertas M.L., and Carrasco B. HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. J. Magn. Reson. 147 (2000) 138-146
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • de la Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 61
    • 0344734168 scopus 로고    scopus 로고
    • Time-resolved and steady-state fluorescence quenching of N-acetyl-l-tryptophanamide by acrylamide and iodide
    • Zelent B., Kusba J., Gryczynski I., Johnson M.L., and Lakowicz J.R. Time-resolved and steady-state fluorescence quenching of N-acetyl-l-tryptophanamide by acrylamide and iodide. Biophys. Chemist. 73 (Jul 1998) 53-75
    • (1998) Biophys. Chemist. , vol.73 , pp. 53-75
    • Zelent, B.1    Kusba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 62
    • 0018143763 scopus 로고
    • Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization
    • Schmid F.X., and Baldwin R.L. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proc. Natl Acad. Sci. USA 75 (Oct 1978) 4764-4768
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4764-4768
    • Schmid, F.X.1    Baldwin, R.L.2
  • 63
    • 0025195733 scopus 로고
    • Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
    • Kiefhaber T., Quaas R., Hahn U., and Schmid F.X. Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29 (Mar 1990) 3053-3061
    • (1990) Biochemistry , vol.29 , pp. 3053-3061
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 64
    • 0015918856 scopus 로고
    • Kinetics of unfolding and refolding of proteins: I. Mathematical analysis
    • Ikai A., and Tanford C. Kinetics of unfolding and refolding of proteins: I. Mathematical analysis. J. Mol. Biol. 73 (Jan 1973) 145-163
    • (1973) J. Mol. Biol. , vol.73 , pp. 145-163
    • Ikai, A.1    Tanford, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.