메뉴 건너뛰기




Volumn 263, Issue 2, 1996, Pages 344-358

Thermodynamic characterization of the coupled folding and association of heterodimeric coiled coils (leucine zippers)

Author keywords

Co operativity; Folding enthalpy; Isothermal titration calorimetry; Protein stability curve; Thermal unfolding

Indexed keywords

ALANINE; LEUCINE; LEUCINE ZIPPER PROTEIN; POLYPEPTIDE;

EID: 0030601794     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0579     Document Type: Article
Times cited : (45)

References (59)
  • 1
    • 0026845838 scopus 로고
    • Structure of the leucine zipper
    • Thermodynamic Ilian Jelesarov * and Hans Rudolf Bosshard Biochemisches Institut der Universität Zürich Winterthurerstrasse 190 CH-8057 Zürich, Switzerland * Corresponding author
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 205-210
    • Alber, T.1
  • 3
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Arcus, V. L., Vuilleumier, S., Freund, S. M. V., Bycroft, M. & Fersht, A. R. (1995). A comparison of the pH, urea and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding. J. Mol. Biol. 254, 305-321.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 4
    • 0023442217 scopus 로고
    • Protein stability curves
    • Baldwin, E. P., Hajiseyedjavadi, O., Baase, W. A. & Matthews, B. W. (1993). The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science, 262, 1715-1718.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 6
    • 0024962376 scopus 로고
    • Equilibrium dissociation and unfolding of the Arc repressor dimer
    • Betz, S. F., Bryson, J. W. & DeGrado, W. F. (1995). Native-like and structurally characterized designed α-helical bundles. Curr. Opin. Struct. Biol. 5, 457-463.
    • (1989) Biochemistry , vol.28 , pp. 7139-7143
    • Bowie, J.U.1    Sauer, R.T.2
  • 7
    • 0015917504 scopus 로고
    • Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitor, insulin and pancreatic trypsin inhibitor
    • Bowie, J. U. & Sauer, R. T. (1989). Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry, 28, 7139-7143.
    • (1973) Biochemistry , vol.12 , pp. 2011-2024
    • Brandts, J.F.1    Kaplan, L.J.2
  • 8
    • 0026659508 scopus 로고
    • Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme
    • Brandts, J. F. & Kaplan, L. J. (1973). Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitor, insulin and pancreatic trypsin inhibitor. Biochemistry, 12, 2011-2024.
    • (1992) J. Mol. Biol. , vol.225 , pp. 939-943
    • Cooper, A.1    Eyles, S.J.2    Radford, S.E.3    Dobson, C.M.4
  • 9
    • 0026013127 scopus 로고
    • Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB1
    • Cooper, A., Eyles, S. J., Radford, S. E. & Dobson, C. M. (1992). Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme. J. Mol. Biol. 225, 939-943.
    • (1991) Biochemistry , vol.30 , pp. 143-147
    • De Francesco, R.1    Pastore, A.2    Vecchio, G.3    Cortese, R.4
  • 10
    • 0028103991 scopus 로고
    • The unfolding of trp aporepressor as a function of pH: Evidence for an unfolding intermediate
    • De Francesco, R., Pastore, A., Vecchio, G. & Cortese, R. (1991). Circular dichroism study on the conformational stability of the dimerization domain of transcription factor LFB1. Biochemistry, 30, 143-147.
    • (1994) Biochemistry , vol.33 , pp. 10220-10228
    • Eftink, M.R.1    Helton, K.J.2    Beavers, A.3    Ramsay, G.D.4
  • 11
    • 0028118685 scopus 로고
    • Getting a grip on DNA recognition: Structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains
    • Eftink, M. R., Helton, K. J., Beavers, A. & Ramsay, G. D. (1994). The unfolding of trp aporepressor as a function of pH: evidence for an unfolding intermediate. Biochemistry, 33, 10220-10228.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 12-21
    • Ellenberger, T.1
  • 12
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: Crystal structure of the protein-DNA complex
    • Ellenberger, T. (1994). Getting a grip on DNA recognition: structures of the basic region leucine zipper, and the basic region helix-loop-helix DNA-binding domains. Curr. Opin. Struct. Biol. 4, 12-21.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 13
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering experiments
    • Ellenberger, T. E., Brandl, C. J., Struhl, K. & Harrison, S. C. (1992). The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell, 71, 1223-1237.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 14
    • 85022366726 scopus 로고
    • Isothermal titration calorimetry
    • Fersht, A. R. & Serrano, L. (1993). Principles of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3, 75-83.
    • (1990) Anal. Chem. , vol.62
    • Freire, E.1    Mayorga, O.L.2    Straume, M.3
  • 15
    • 0027146666 scopus 로고
    • Controlled formation of model mono- and heterodimer coiled coil peptides
    • Freire, E., Mayorga, O. L. & Straume, M. (1990). Isothermal titration calorimetry. Anal. Chem. 62, 950A-959A.
    • (1993) Biochemistry , vol.32 , pp. 12664-12671
    • Graddis, T.J.1    Myszka, D.G.2    Chaiken, I.M.3
  • 16
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Graddis, T. J., Myszka, D. G. & Chaiken, I. M. (1993). Controlled formation of model mono- and heterodimer coiled coil peptides. Biochemistry, 32, 12664-12671.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 17
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • Greenfield, N. & Fasman, G. D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 8, 4108-4116.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 18
    • 0029174419 scopus 로고
    • Transcription factors 1: BZIP proteins
    • Horovitz, A. & Fersht, A. R. (1990). Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214, 613-617.
    • (1995) Protein Profile , vol.2 , pp. 101-168
    • Hurst, H.C.1
  • 19
    • 0027942020 scopus 로고
    • + reductase and the role of water at the complex interface
    • Hurst, H. C. (1995). Transcription factors 1: bZIP proteins. Protein Profile, 2, 101-168.
    • (1994) Biochemistry , vol.33 , pp. 13321-13328
    • Jelesarov, I.1    Bosshard, H.R.2
  • 20
    • 0026806002 scopus 로고
    • Differential scanning calorimetry of thermal unfolding of the methionine repressor protein (MetJ) from Escherichia coli
    • + reductase and the role of water at the complex interface. Biochemistry, 33, 13321-13328.
    • (1992) Biochemistry , vol.31 , pp. 9717-9724
    • Johnson, C.M.1    Cooper, A.2    Stockley, P.G.3
  • 21
    • 0029068108 scopus 로고
    • Nuclear magnetic resonance characterization of the Jun leucine zipper domain: Unusual properties of coiled-coil interfacial polar residues
    • Johnson, C. M., Cooper, A. & Stockley, P. G. (1992). Differential scanning calorimetry of thermal unfolding of the methionine repressor protein (MetJ) from Escherichia coli. Biochemistry, 31, 9717-9724.
    • (1995) Biochemistry , vol.34 , pp. 6164-6174
    • Junius, F.K.1    Mackay, J.P.2    Bubb, W.A.3    Jensen, S.A.4    Weiss, A.S.5    King, G.F.6
  • 22
    • 15844402153 scopus 로고    scopus 로고
    • High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer
    • Junius, F. K., Mackay, J. P., Bubb, W. A., Jensen, S. A., Weiss, A. S. & King, G. F. (1995). Nuclear magnetic resonance characterization of the Jun leucine zipper domain: unusual properties of coiled-coil interfacial polar residues. Biochemistry, 34, 6164-6174.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13663-13667
    • Junius, F.K.1    O'Donoghue, S.I.2    Nilges, M.3    Weiss, A.S.4    King, G.F.5
  • 23
    • 0028805884 scopus 로고
    • The effects of interhelical electrostatic repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils
    • Junius, F. K., O'Donoghue, S. I., Nilges, M., Weiss, A. S. & King, G. F. (1996). High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. J. Biol. Chem. 271, 13663-13667.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25495-25506
    • Kohn, W.D.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4
  • 24
    • 0026666598 scopus 로고
    • Enthalpic destabilization of a mutant human lysozyme lacking a disulphide bridge between cysteine-77 and cysteine-95
    • Kohn, W. D., Monera, O. D., Kay, C. M. & Hodges, R. S. (1995). The effects of interhelical electrostatic repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 270, 25495-25506.
    • (1992) Biochemistry , vol.31 , pp. 8323-8328
    • Kuroki, R.1    Inaka, K.2    Taniyama, Y.3    Kidokoro, S.4    Matsushima, M.5    Kikuchi, M.6    Yutani, K.7
  • 25
    • 0024295767 scopus 로고
    • The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins
    • Kuroki, R., Inaka, K., Taniyama, Y., Kidokoro, S., Matsushima, M., Kikuchi, M. & Yutani, K. (1992). Enthalpic destabilization of a mutant human lysozyme lacking a disulphide bridge between cysteine-77 and cysteine-95. Biochemistry, 31, 8323-8328.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 26
    • 0027522362 scopus 로고
    • Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size
    • Landschulz, W. H., Johnson, P. F. & McKnight, S. L. (1988). The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science, 240, 1759-1764.
    • (1993) Protein Sci. , vol.2 , pp. 733-738
    • Lee, B.1
  • 27
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lee, B. (1993). Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size. Protein Sci. 2, 733-738.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 28
    • 0028805495 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies II
    • Lim, W. A., Hodel, A., Sauer, R. T. & Richards, F. M. (1994). The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl Acad. Sci. USA, 91, 423-427.
    • (1995) Protein Sci. , vol.4 , pp. 2559-2561
    • Liu, Y.1    Sturtevant, J.M.2
  • 29
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • Liu, Y. & Sturtevant, J. M. (1995). Significant discrepancies between van't Hoff and calorimetric enthalpies II. Protein Sci. 4, 2559-2561.
    • (1995) Biochemistry , vol.34 , pp. 8642-9648
    • Lumb, K.L.1    Kim, P.S.2
  • 30
    • 0029147930 scopus 로고
    • Energetics of protein structure
    • Lumb, K. L. & Kim, P. S. (1995). A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry, 34, 8642-9648.
    • (1995) Advan. Protein Chem. , vol.47 , pp. 308-425
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 31
    • 0027438393 scopus 로고
    • Tryptophan replacements in the trp aporepressor from Escherichia coli: Probing the equilibrium and kinetic folding models
    • Makhatadze, G. I. & Privalov, P. L. (1995). Energetics of protein structure. Advan. Protein Chem. 47, 308-425.
    • (1993) Protein Sci. , vol.2 , pp. 1853-1861
    • Mann, C.J.1    Royer, C.A.2    Matthews, C.R.3
  • 32
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Mann, C. J., Royer, C. A. & Matthews, C. R. (1993). Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Sci. 2, 1853-1861.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Bresslauer, K.J.2
  • 33
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Marky, L. A. & Bresslauer, K. J. (1987). Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers, 26, 1601-1620.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 34
    • 0026052762 scopus 로고
    • Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase
    • Matthews, B. W. (1993). Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62, 139-160.
    • (1988) Biochemistry , vol.30 , pp. 8494-8500
    • Morin, P.E.1    Freire, E.2
  • 35
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Morin, P. E. & Freire, E. (1988). Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase. Biochemistry, 30, 8494-8500.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 36
    • 0028231730 scopus 로고
    • Design and characterization of an intramolecular antiparallel coiled coil peptide
    • Murphy, K. P. & Freire, E. (1992). Thermodynamics of structural stability and cooperative folding behavior in proteins. Advan. Protein Chem. 43, 313-361.
    • (1994) Biochemistry , vol.33 , pp. 2368-2372
    • Myszka, D.G.1    Chaiken, I.M.2
  • 37
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • Myszka, D. G. & Chaiken, I. M. (1994). Design and characterization of an intramolecular antiparallel coiled coil peptide. Biochemistry, 33, 2368-2372.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5597-5599
    • Naghibi, H.1    Tamura, A.2    Sturtevant, J.M.3
  • 38
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • Naghibi, H., Tamura, A. & Sturtevant, J. M. (1995). Significant discrepancies between van't Hoff and calorimetric enthalpies. Proc. Natl Acad. Sci. USA, 92, 5597-5599.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 39
    • 0000236570 scopus 로고
    • Peptide "Velcro": Design of a heterodimeric coiled coil
    • O'Shea, E. K., Klemm, J. D., Kim, P. S. & Alber, T. (1991). X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science, 254, 539-544.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 40
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • O'Shea, E. K., Lumb, K. J. & Kim, P. S. (1993). Peptide "Velcro": design of a heterodimeric coiled coil. Curr. Biol. 3, 658-667.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 41
    • 0024498471 scopus 로고
    • A new method for determining the heat capacity change for protein folding
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1989) Biochemistry , vol.28 , pp. 2520-2525
    • Pace, C.N.1    Laurents, D.V.2
  • 42
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Pace, C. N. & Laurents, D. V. (1989). A new method for determining the heat capacity change for protein folding. Biochemistry, 28, 2520-2525.
    • (1982) Advan. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 43
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. L. (1982). Stability of proteins. Proteins which do not present a single cooperative system. Advan. Protein Chem. 35, 1-104.
    • (1988) Advan. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 45
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Semisotnov, G. V., Rodionova, N. A., Razgulayev, O. I., Uversky, V. N., Gropas, A. F. & Gilmanshin, R. I. (1991). Study of the "molten globule" intermediate state in protein folding by hydrophobic fluorescent probe. Biopolymers, 31, 119-128.
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.1
  • 46
    • 0029126043 scopus 로고
    • Effects of cavity-creating mutations on conformational stability and structure of the dimeric 4-α-helical protein ROP: Thermal unfolding studies
    • Shortle, D. (1996). The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10, 27-34.
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 83-96
    • Steif, C.1    Hinz, H.J.2    Cesareni, G.3
  • 47
    • 0013800421 scopus 로고
    • The interaction of naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Steif, C., Hinz, H. J. & Cesareni, G. (1995). Effects of cavity-creating mutations on conformational stability and structure of the dimeric 4-α-helical protein ROP: thermal unfolding studies. Proteins: Struct. Funct. Genet. 23, 83-96.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 48
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Stryer, L. (1965). The interaction of naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 2236-2241
    • Sturtevant, J.M.1
  • 50
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thomas, R. M., Wendt, H., Zampieri, A. & Bosshard, H. R. (1995). α-Helical coiled coils: simple models for self-associating peptide and protein systems. Prog. Coll. Polymer. Sci. 99, 24-30.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 52
    • 0025875214 scopus 로고
    • The contribution of dna single-stranded order to the thermodynamics of duplex formation
    • Tiktopulo, E. I., Privalov, P. L., Odintsova, T. I., Ermokhina, T. M., Krasheninnikov, I. A., Aviles, F. X., Gary, P. D. & Crane-Robinson, C. (1982). The central tryptic fragment of histones H1 and H5 is a fully compact domain and is the only folded region in the polypeptide chain. A thermodynamic study. Eur. J. Biochem. 122, 327-331.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3569-3573
    • Vesnaver, G.1    Breslauer, K.J.2
  • 53
  • 54
    • 0029086386 scopus 로고
    • Structural energetics of barstar studied by differential scanning microcalorimetry
    • Wendt, H., Berger, C., Baici, A., Thomas, R. M. & Bosshard, H. R. (1995). Kinetics of folding of leucine zipper domains. Biochemistry, 34, 4097-4107.
    • (1995) Protein Sci. , vol.4 , pp. 1528-1534
    • Wintrode, P.L.1    Griko, Y.V.2    Privalov, P.L.3
  • 55
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wintrode, P. L., Griko, Y. V. & Privalov, P. L. (1995). Structural energetics of barstar studied by differential scanning microcalorimetry. Protein Sci. 4, 1528-1534.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 56
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease a stability
    • Wiseman, T., Williston, S., Brandts, J. F. & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 57
    • 0026650710 scopus 로고
    • Synthetic model proteins: The relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded alpha-helical coiled-coil
    • Yao, M. & Bolen, D. W. (1995). How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry, 34, 3771-3781.
    • (1992) Biochemistry , vol.31 , pp. 5739-5746
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 58
    • 0026609553 scopus 로고
    • The two-stranded alpha-helical coiled coil is an ideal model for studying protein stability and subunit interactions
    • Zhou, N. E., Kay, C. M. & Hodges, R. S. (1992a). Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded alpha-helical coiled-coil. Biochemistry, 31, 5739-5746.
    • (1992) Biopolymers , vol.32 , pp. 419-426
    • Zhou, N.E.1    Zhu, B.Y.2    Kay, C.M.3    Hodges, R.S.4
  • 59
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
    • Zhou, N. E., Zhu, B. Y., Kay, C. M. & Hodges, R. S. (1992b). The two-stranded alpha-helical coiled coil is an ideal model for studying protein stability and subunit interactions. Biopolymers, 32, 419-426.
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.