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Volumn 48, Issue 17, 2009, Pages 3743-3754

Molecular origin of constant m-values, denatured state collapse, and residue-dependent transition midpoints in globular proteins

Author keywords

[No Author keywords available]

Indexed keywords

COARSE-GRAINED; COLLAPSE TRANSITIONS; COMPACT STRUCTURES; DENATURANT CONCENTRATION; DENATURED STATE; GLOBULAR PROTEINS; MOLECULAR ORIGINS; MOLECULAR SIMULATIONS; MOLECULAR TRANSFER; NATIVE STATE; RADIUS OF GYRATION; RESIDUAL STRUCTURE; SECONDARY STRUCTURE ELEMENTS; SIDE CHAINS; SINGLE MOLECULE EXPERIMENTS; SOLVENT INTERACTIONS; STRUCTURAL ELEMENTS; SURFACE AREA; TOTAL SURFACE AREA; TRANSFER MODELS; TRANSITION MIDPOINT; TWO-STATE FOLDERS;

EID: 66049114131     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8021119     Document Type: Article
Times cited : (45)

References (65)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E. (1998) How do small single-domain proteins fold? Folding Des. 3, 81-91.
    • (1998) Folding Des. , vol.3 , pp. 81-91
    • Jackson, S.E.1
  • 2
    • 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. (1992) A test of the linear extrapolation of unfolding free-energy changes over an extended denaturant concentration range. Biochemistry 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 3
    • 0016292941 scopus 로고
    • Urea and guanidinehydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • Greene, R. F., and Pace, C. N. (1974) Urea and guanidinehydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J. Biol. Chem. 249, 5388-5393.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 4
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and Analysis of Urea and Gunidine Hydrochloride Denaturation Curves. Methods Enzymol. 131, 266-280. (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 5
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • DOI 10.1021/bi00421a014
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068. (Pubitemid 18254049)
    • (1988) Biochemistry , vol.27 , Issue.21 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 6
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor. 2.1. Evidence for a 2-state transition
    • Jackson, S. E., and Fersht, A. R. (1991) Folding of chymotrypsin inhibitor. 2.1. Evidence for a 2-state transition. Biochemistry 30, 10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 7
    • 20544461199 scopus 로고    scopus 로고
    • Thermodynamics of Protein Interactions with Urea and Guanidinium Hydrochloride
    • Makhatadze, G. I. (1999) Thermodynamics of Protein Interactions with Urea and Guanidinium Hydrochloride. J. Phys. Chem. B 103, 4781-4785.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 4781-4785
    • Makhatadze, G.I.1
  • 10
    • 0030631570 scopus 로고    scopus 로고
    • Characterization of the free energy spectrum of peptostreptococcal protein L
    • Yi, Q., Scalley, M. L., Simons, K. T., Gladwin, S. T., and Baker, D. (1997) Characterization of the free energy spectrum of peptostreptococcal protein L. Folding Des. 2, 271-280. (Pubitemid 127740549)
    • (1997) Folding and Design , vol.2 , Issue.5 , pp. 271-280
    • Yi, Q.1    Scalley, M.L.2    Simons, K.T.3    Gladwin, S.T.4    Baker, D.5
  • 11
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh, S., Peters, I. D., Butt, T. R., and Roder, H. (1993) Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry 32, 7054-7063. (Pubitemid 23221641)
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 12
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L
    • DOI 10.1021/bi9625758
    • Scalley, M. L., Yi, Q., Gu, H. D., McCormack, A., Yates, J. R., and Baker, D. (1997) Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L. Biochemistry 36, 3373-3382. (Pubitemid 27142412)
    • (1997) Biochemistry , vol.36 , Issue.11 , pp. 3373-3382
    • Scalley, M.L.1    Yi, Q.2    Gu, H.3    McCormack, A.4    Yates III, J.R.5    Baker, D.6
  • 13
    • 78651119214 scopus 로고
    • Solubility of amino acids and related compounds in aqueous urea solutions
    • Nozaki, Y., and Tanford, C. (1963) Solubility of amino acids and related compounds in aqueous urea solutions. J. Biol. Chem. 238, 4074-4081.
    • (1963) J. Biol. Chem. , vol.238 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 14
    • 33947488954 scopus 로고
    • Isothermal unfolding of globular proteins in aqueous urea solutions
    • Tanford, C. (1964) Isothermal unfolding of globular proteins in aqueous urea solutions. J. Am. Chem. Soc. 86, 2050-2059.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 2050-2059
    • Tanford, C.1
  • 17
    • 0842304735 scopus 로고    scopus 로고
    • Additive Transfer Free Energies of the Peptide Backbone Unit That Are Independent of the Model Compound and the Choice of Concentration Scale
    • DOI 10.1021/bi035908r
    • Auton, M., and Bolen, D. W. (2004) Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale. Biochemistry 43, 1329-1342. (Pubitemid 38176532)
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1329-1342
    • Auton, M.1    Bolen, D.W.2
  • 18
    • 35748981504 scopus 로고    scopus 로고
    • Application of the transfer model to understand how naturally occuring osmolytes affect protein stability
    • Auton, M., and Bolen, D. W. (2007) Application of the transfer model to understand how naturally occuring osmolytes affect protein stability. Methods Enzymol. 428, 397-418.
    • (2007) Methods Enzymol. , vol.428 , pp. 397-418
    • Auton, M.1    Bolen, D.W.2
  • 19
    • 0015222647 scopus 로고
    • Interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and Richards, F. M. (1971) Interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55, 379.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379
    • Lee, B.1    Richards, F.M.2
  • 20
    • 0029859858 scopus 로고    scopus 로고
    • Surface point mutations that significantly alter the structure and stability of a protein's denatured state
    • Smith, C. K., Bu, Z. M., Anderson, K. S., Sturtevant, J. M., Engelman, D. M., and Regan, L. (1996) Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Sci. 5, 2009-2019. (Pubitemid 26347736)
    • (1996) Protein Science , vol.5 , Issue.10 , pp. 2009-2019
    • Smith, C.K.1    Bu, Z.2    Anderson, K.S.3    Sturtevant, J.M.4    Engelman, D.M.5    Regan, L.6
  • 21
    • 0029562577 scopus 로고
    • Partially folded states of proteins: Characterization by X-ray scattering
    • Doniach, S., Bascle, J., Garel, T., and Orland, H. (1995) Partially folded states of proteins: Characterization by X-ray scattering. J. Mol. Biol. 254, 960-967.
    • (1995) J. Mol. Biol. , vol.254 , pp. 960-967
    • Doniach, S.1    Bascle, J.2    Garel, T.3    Orland, H.4
  • 22
    • 32344442512 scopus 로고    scopus 로고
    • Molecular dimensions and their distributions in early folding intermediates
    • DOI 10.1016/j.sbi.2006.01.007, PII S0959440X06000091
    • Bilsel, O., and Matthews, C. R. (2006) Molecular dimensions and their distributions in early folding intermediates. Curr. Opin. Struct. Biol. 16, 86-93. (Pubitemid 43221876)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 86-93
    • Bilsel, O.1    Matthews, C.R.2
  • 23
    • 33947315248 scopus 로고    scopus 로고
    • Microsecond Hydrophobic Collapse in the Folding of Escherichia coli Dihydrofolate Reductase, an α/β-Type Protein
    • DOI 10.1016/j.jmb.2007.01.085, PII S0022283607001635
    • Arai, M., Kondrashkina, E., Kayatekin, C., Matthews, C. R., Iwakura, M., and Bilsel, O. (2007) Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase an α/β-type protein. J. Mol. Biol. 368, 219-229. (Pubitemid 46441220)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 219-229
    • Arai, M.1    Kondrashkina, E.2    Kayatekin, C.3    Matthews, C.R.4    Iwakura, M.5    Bilsel, O.6
  • 24
    • 0035830438 scopus 로고    scopus 로고
    • Distributions of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein
    • DOI 10.1021/bi001946o
    • Navon, A., Ittah, V., Landsman, P., Scheraga, H. A., and Haas, E. (2001) Distributions of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein. Biochemistry 40, 105-118. (Pubitemid 32052682)
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 105-118
    • Navon, A.1    Ittah, V.2    Landsman, P.3    Scheraga, H.A.4    Haas, E.5
  • 25
    • 26244466045 scopus 로고    scopus 로고
    • Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition
    • DOI 10.1016/j.jmb.2005.08.056, PII S0022283605010107
    • Sinha, K. K., and Udgaonkar, J. B. (2005) Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition. J. Mol. Biol. 353, 704-718. (Pubitemid 41414742)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.3 , pp. 704-718
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 30
    • 33845923182 scopus 로고    scopus 로고
    • BPPred: A Web-based computational tool for predicting biophysical parameters of proteins
    • DOI 10.1110/ps.062383807
    • Geierhaas, C. D., Nickson, A. A., Lindorff-Larsen, K., Clarke, J., and Vendruscolo, M. (2007) BPPred: A Web-based computational tool for predicting biophysical parameters of proteins. Protein Sci. 16, 125-134. (Pubitemid 46036505)
    • (2007) Protein Science , vol.16 , Issue.1 , pp. 125-134
    • Geierhaas, C.D.1    Nickson, A.A.2    Lindorff-Larsen, K.3    Clarke, J.4    Vendruscolo, M.5
  • 31
    • 33748454896 scopus 로고    scopus 로고
    • Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions
    • DOI 10.1529/biophysj.106.086264
    • Tran, H. T., and Pappu, R. V. (2006) Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions. Biophys. J. 91, 1868-1886. (Pubitemid 44352450)
    • (2006) Biophysical Journal , vol.91 , Issue.5 , pp. 1868-1886
    • Tran, H.T.1    Pappu, R.V.2
  • 32
    • 0028297302 scopus 로고
    • Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride
    • DOI 10.1006/jmbi.1994.1173
    • Logan, T. M., Theriault, Y., and Fesik, S. W. (1994) Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol. 236, 637. (Pubitemid 24146307)
    • (1994) Journal of Molecular Biology , vol.236 , Issue.2 , pp. 637-648
    • Logan, T.M.1    Theriault, Y.2    Fesik, S.W.3
  • 34
    • 0025832142 scopus 로고
    • Effective concentrations of amino-acid side-chains in an unfolded protein
    • Muthukrishnan, K., and Nall, B. T. (1991) Effective concentrations of amino-acid side-chains in an unfolded protein. Biochemistry 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nall, B.T.2
  • 35
    • 0345352750 scopus 로고    scopus 로고
    • Spectroscopic studies of structural changes in two β-sheet-forming peptides show an ensemble of structures that unfold noncooperatively
    • DOI 10.1021/bi026893k
    • Kuznetsov, S. V., Hilario, J., Keiderling, T. A., and Ansari, A. (2003) Spectroscopic studies of structural changes in two β-sheet-forming peptides show an ensemble of structures that unfold noncooperatively. Biochemistry 42, 4321-4332. (Pubitemid 36457601)
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4321-4332
    • Kuznetsov, S.V.1    Hilario, J.2    Keiderling, T.A.3    Ansari, A.4
  • 36
    • 51649087154 scopus 로고    scopus 로고
    • Denaturant and osmolyte effects on proteins are accurately predicted using the molecular transfer model
    • O'Brien, E. P., Ziv, G., Haran, G., Brooks, B. R., and Thirumalai, D. (2008) Denaturant and osmolyte effects on proteins are accurately predicted using the molecular transfer model. Proc. Natl. Acad. Sci. U.S.A. 105, 13403-13408.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13403-13408
    • O'Brien, E.P.1    Ziv, G.2    Haran, G.3    Brooks, B.R.4    Thirumalai, D.5
  • 38
    • 0033117927 scopus 로고    scopus 로고
    • Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models
    • DOI 10.1016/S0959-440X(99)80028-1
    • Klimov, D., and Thirumalai, D. (1999) Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models. Curr. Opin. Struct. Biol. 9, 197-207. (Pubitemid 29452898)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.2 , pp. 197-207
    • Thirumalai, D.1    Klimov, D.K.2
  • 39
    • 33646931471 scopus 로고    scopus 로고
    • Protein Folding Thermodynamics and Dynamics: Where Physics, Chemistry, and Biology Meet
    • Shakhnovich, E. (2006) Protein Folding Thermodynamics and Dynamics: Where Physics, Chemistry, and Biology Meet. Chem. Rev. 106, 1559-1588.
    • (2006) Chem. Rev. , vol.106 , pp. 1559-1588
    • Shakhnovich, E.1
  • 40
    • 0242368163 scopus 로고    scopus 로고
    • Exploring the interplay between topology and secondary structural formation in the protein folding problem
    • Cheung, M. S., Finke, J. M., Callahan, B., and Onuchic, J. N. (2003) Exploring the interplay between topology and secondary structural formation in the protein folding problem. J. Phys. Chem. B 107, 11193-11200.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 11193-11200
    • Cheung, M.S.1    Finke, J.M.2    Callahan, B.3    Onuchic, J.N.4
  • 41
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • PII S0009261499011239
    • Sugita, Y., and Okamoto, Y. (1999) Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 314, 141-151. (Pubitemid 129556751)
    • (1999) Chemical Physics Letters , vol.314 , Issue.1-2 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 42
    • 0037305918 scopus 로고    scopus 로고
    • Multiplexed-replica exchange molecular dynamics method for protein folding simulation
    • Rhee, Y. M., and Pande, V. S. (2003) Multiplexed-replica exchange molecular dynamics method for protein folding simulation. Biophys. J. 84, 775-786.
    • (2003) Biophys. J. , vol.84 , pp. 775-786
    • Rhee, Y.M.1    Pande, V.S.2
  • 43
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties
    • Veitshans, T., Klimov, D., and Thirumalai, D. (1997) Protein folding kinetics: Timescales, pathways and energy landscapes in terms of sequence-dependent properties. Folding Des. 2, 1-22. (Pubitemid 127740447)
    • (1997) Folding and Design , vol.2 , Issue.1 , pp. 1-22
    • Veitshans, T.1    Klimov, D.2    Thirumalai, D.3
  • 45
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M., and Swendsen, R. H. (1989) Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63, 1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 46
    • 84986519238 scopus 로고
    • The Weighted Histogram Analysis Method for free-energy calculations on biomolecules. 1. The method
    • Kumar, S., Bouzida, D., Swendsen, R. H., Kollman, P. A., and Rosenberg, J. M. (1992) The Weighted Histogram Analysis Method for free-energy calculations on biomolecules. 1. The method. J. Comput. Chem. 13, 1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 47
    • 0000870658 scopus 로고    scopus 로고
    • Exploring the space of protein folding Hamiltonians: The balance of forces in a minimalist β-barrel model
    • DOI 10.1063/1.476842, PII S0021960698508318
    • Shea, J., Nochomovitz, Y. D., Guo, Z., and Brooks, C. L. (1998) Exploring the space of protein folding Hamiltonians: The balance of forces in a minimalist β-barrel model. J. Chem. Phys. 109, 2895-2903. (Pubitemid 128678183)
    • (1998) Journal of Chemical Physics , vol.109 , Issue.7 , pp. 2895-2903
    • Shea, J.-E.1    Nochomovitz, Y.D.2    Guo, Z.3    Brooks, C.L.4
  • 48
    • 0035074166 scopus 로고    scopus 로고
    • Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution
    • DOI 10.1107/S0907444901000373
    • O'Neill, J. W., Kim, D. E., Baker, D., and Zhang, K. Y. (2001) Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution. Acta Crystallogr. D57, 480-487. (Pubitemid 32296024)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.4 , pp. 480-487
    • O'Neill, J.W.1    Kim, D.E.2    Baker, D.3    Zhang, K.Y.J.4
  • 49
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • Kim, D. E., Fisher, C., and Baker, D. (2000) A breakdown of symmetry in the folding transition state of protein L. J. Mol. Biol. 298, 971-984.
    • (2000) J. Mol. Biol. , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 50
    • 55949131241 scopus 로고    scopus 로고
    • Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
    • Hua, L., Zhou, R. H., Thirumalai, D., and Berne, B. J. (2008) Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc. Natl. Acad. Sci. U.S.A. 105, 16928-16933.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.H.2    Thirumalai, D.3    Berne, B.J.4
  • 51
    • 0032558991 scopus 로고    scopus 로고
    • Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics
    • DOI 10.1021/bi981849j
    • Baskakov, I. V., and Bolen, D. W. (1998) Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics. Biochemistry 37, 18010-18017. (Pubitemid 29023957)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 18010-18017
    • Baskakov, I.V.1    Bolen, D.W.2
  • 52
    • 0033648607 scopus 로고    scopus 로고
    • Structural thermodynamics of a random coil protein in guanidine hydrochloride
    • Yang, M., Ferreon, A. C. M., and Bolen, D. W. (2000) Structural thermodynamics of a random coil protein in guanidine hydrochloride. Proteins: Struct., Funct., Genet. 4, 44-49.
    • (2000) Proteins: Struct., Funct., Genet. , vol.4 , pp. 44-49
    • Yang, M.1    Ferreon, A.C.M.2    Bolen, D.W.3
  • 53
    • 0037079586 scopus 로고    scopus 로고
    • Is there a unique melting temperature for two-state proteins?
    • DOI 10.1002/jcc.10005
    • Klimov, D. K., and Thirumalai, D. (2002) Is there a unique melting temperature for two-state proteins? J. Comput. Chem. 23, 161-165. (Pubitemid 34063140)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.1 , pp. 161-165
    • Klimov, D.K.1    Thirumalai, D.2
  • 54
    • 42749106226 scopus 로고    scopus 로고
    • Finite size effects on thermal denaturation of globular proteins
    • Li, M. S., Klimov, D. K., and Thirumalai, D. (2004) Finite size effects on thermal denaturation of globular proteins. Phys. Rev. Lett. 93, 268107.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 268107
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 55
    • 0001574528 scopus 로고
    • Scaling theory for finitesize effects in critical region
    • Fisher, M. E., and Barber, M. N. (1972) Scaling theory for finitesize effects in critical region. Phys. Rev. Lett. 28, 1516-1519.
    • (1972) Phys. Rev. Lett. , vol.28 , pp. 1516-1519
    • Fisher, M.E.1    Barber, M.N.2
  • 56
    • 0030872054 scopus 로고    scopus 로고
    • Thermal unfolding in a GCN4-like leucine zipper: C-13 α NMR chemical shifts and local unfolding
    • Holtzer, M. E., Lovett, E. G., d'Avignon, D. A., and Holtzer, A. (1997) Thermal unfolding in a GCN4-like leucine zipper: C-13 α NMR chemical shifts and local unfolding. Biophys. J. 73, 1031.
    • (1997) Biophys. J. , vol.73 , pp. 1031
    • Holtzer, M.E.1    Lovett, E.G.2    D'Avignon, D.A.3    Holtzer, A.4
  • 57
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • DOI 10.1038/nature04859, PII NATURE04859
    • Sadqi, M., Fushman, D., and Munoz, V. (2006) Atom-by-atom analysis of global downhill protein folding. Nature 442, 317-321. (Pubitemid 44114908)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Munoz, V.3
  • 58
    • 0001504441 scopus 로고    scopus 로고
    • Cooperativity in protein folding: From lattice models with sidechains to real proteins
    • DOI 10.1016/S1359-0278(98)00018-2
    • Klimov, D. K., and Thirumalai, D. (1998) Cooperativity in protein folding: From lattice models with sidechains to real proteins. Folding Des. 3, 127-139. (Pubitemid 28166184)
    • (1998) Folding and Design , vol.3 , Issue.2 , pp. 127-139
    • Klimov, D.K.1    Thirumalai, D.2
  • 59
    • 0037633978 scopus 로고    scopus 로고
    • Measuring the stability of partly folded proteins using TMAO
    • DOI 10.1110/ps.0372903
    • Mello, C. C., and Barrick, D. (2003) Measuring the stability of partly folded proteins using TMAO. Protein Sci. 12, 1522-1529. (Pubitemid 36759355)
    • (2003) Protein Science , vol.12 , Issue.7 , pp. 1522-1529
    • Mello, C.C.1    Barrick, D.2
  • 60
    • 0032978994 scopus 로고    scopus 로고
    • Chain collapse can occur concomitantly with the rate-limiting step in protein folding
    • DOI 10.1038/9329
    • Plaxco, K. W., Millett, I. S., Segel, D. J., Doniach, S., and Baker, D. (1999) Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nat. Struct. Biol. 6, 554-556. (Pubitemid 29252835)
    • (1999) Nature Structural Biology , vol.6 , Issue.6 , pp. 554-556
    • Plaxco, K.W.1    Millett, I.S.2    Segel, D.J.3    Doniach, S.4    Baker, D.5
  • 61
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic Simulations of the Effects of Polyglutamine Chain Length and Solvent Quality on Conformational Equilibria and Spontaneous Homodimerization
    • Vitalis, A., Wang, X. L., and Pappu, R. V. (2008) Atomistic Simulations of the Effects of Polyglutamine Chain Length and Solvent Quality on Conformational Equilibria and Spontaneous Homodimerization. J. Mol. Biol. 384, 279-297.
    • (2008) J. Mol. Biol. , vol.384 , pp. 279-297
    • Vitalis, A.1    Wang, X.L.2    Pappu, R.V.3
  • 62
    • 0021195067 scopus 로고
    • Amino-Acid, peptide, and protein volume in solution
    • Zamyatnin, A. A. (1984) Amino-Acid, peptide, and protein volume in solution. Annu. ReV. Biophys. Bioeng. 13, 145-165.
    • (1984) Annu. ReV. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 63
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H., and Zehfus, M. H. (1985) Hydrophobicity of amino-acid residues in globular proteins. Science 229, 834-838. (Pubitemid 16246583)
    • (1985) Science , vol.229 , Issue.4716 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3
  • 64
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • DOI 10.1002/prot.340230412
    • Frishman, D., and Argos, P. (1995) Knowledge-based protein secondary structure assignment. Proteins 23, 566-579. (Pubitemid 26009520)
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 65
    • 67749142097 scopus 로고    scopus 로고
    • Protein folding, protein collapse, and Tanford's transfer model: Lessons from single-molecule FRET
    • Ziv, G., and Haran, G. (2009) Protein folding, protein collapse, and Tanford's transfer model: Lessons from single-molecule FRET. J. Am. Chem. Soc. 131, 2942-2947.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2942-2947
    • Ziv, G.1    Haran, G.2


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