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Volumn 62, Issue , 2011, Pages 257-277

Role of solvation effects in protein denaturation: From thermodynamics to single molecules and back

Author keywords

FRET; guanidinium chloride; hydrophobic effect; molecular dynamics simulations; protein folding; single molecule spectroscopy; urea

Indexed keywords

CHEMICAL STABILITY; CHLORINE COMPOUNDS; DENATURATION; FORSTER RESONANCE ENERGY TRANSFER; HYDROPHOBICITY; METABOLISM; MOLECULES; PROTEIN FOLDING; SOLVATION; THERMODYNAMICS; UREA;

EID: 79953759344     PISSN: 0066426X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-physchem-032210-103531     Document Type: Article
Times cited : (245)

References (85)
  • 2
    • 47749083052 scopus 로고    scopus 로고
    • From the first protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht AR. 2008. From the first protein structures to our current knowledge of protein folding: delights and scepticisms. Nat. Rev. Mol. Cell Biol. 9:650-54.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 650-654
    • Fersht, A.R.1
  • 3
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson CM. 2003. Protein folding and misfolding. Nature 426:884-90. (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 0002153177 scopus 로고
    • On the theory of the condensed states of heteropolymers
    • Grosberg A. 1984. On the theory of the condensed states of heteropolymers. J. Stat. Phys. 38:149-60.
    • (1984) J. Stat. Phys. , vol.38 , pp. 149-160
    • Grosberg, A.1
  • 6
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-58. (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 8
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso D, Dill K. 1991. Solvent denaturation and stabilization of globular proteins. Biochemistry 30:5974-85.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.1    Dill, K.2
  • 9
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff SN. 1998. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Protein Fold. Cell 51:355-432. (Pubitemid 28252477)
    • (1998) Advances in Protein Chemistry , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 10
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogen-bonded backbone in protein folding
    • Bolen DW, Rose GD. 2008. Structure and energetics of the hydrogen-bonded backbone in protein folding. Annu. Rev. Biochem. 77:339-62.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 11
    • 0034338307 scopus 로고    scopus 로고
    • Heteropolymer freezing and design: Towards physical models of protein folding
    • Pande V, Grosberg A, Tanaka T. 2000. Heteropolymer freezing and design: towards physical models of protein folding. Rev. Mod. Phys. 72:259-86.
    • (2000) Rev. Mod. Phys. , vol.72 , pp. 259-286
    • Pande, V.1    Grosberg, A.2    Tanaka, T.3
  • 13
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:266-80. (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 16
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson J, Wolynes P. 1987. Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA 84:7524-28.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.1    Wolynes, P.2
  • 17
    • 0024742246 scopus 로고
    • Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition
    • Shakhnovich EI, Finkelstein AV. 1989. Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers 28:1667-80.
    • (1989) Biopolymers , vol.28 , pp. 1667-1680
    • Shakhnovich, E.I.1    Finkelstein, A.V.2
  • 18
    • 0024357911 scopus 로고
    • Formation of unique structure in polypeptide chains: Theoretical investigation with the aid of a replica approach
    • DOI 10.1016/0301-4622(89)80058-4
    • Shakhnovich E, Gutin A. 1989. Formation of unique structure in polypeptide chains: theoretical investigation with the aid of a replica approach. Biophys. Chem. 34:187-99. (Pubitemid 20007771)
    • (1989) Biophysical Chemistry , vol.34 , Issue.3 , pp. 187-199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 19
    • 67649774570 scopus 로고    scopus 로고
    • Computing protein stabilities from their chain lengths
    • Ghosh K, Dill K. 2009. Computing protein stabilities from their chain lengths. Proc. Natl. Acad. Sci. USA 106:10649-54.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10649-10654
    • Ghosh, K.1    Dill, K.2
  • 23
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Protein Fold. Cell 14:1-63.
    • (1959) Protein Fold. Cell , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 24
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride: A calorimetric study
    • Makhatadze GI, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: a calorimetric study. J. Mol. Biol. 226:491-505.
    • (1992) J. Mol. Biol. , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 26
    • 37549043949 scopus 로고    scopus 로고
    • Interaction of urea with amino acids: Implications for urea-induced protein denaturation
    • Stumpe M, Grubm̈ uller H. 2007. Interaction of urea with amino acids: implications for urea-induced protein denaturation. J. Am. Chem. Soc. 129:16126-31.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 16126-16131
    • Stumpe, M.1    Grubm̈uller, H.2
  • 28
    • 34250869055 scopus 로고    scopus 로고
    • Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: Lessons for protein denaturation mechanism
    • DOI 10.1021/ja069232+
    • O'Brien E, Dima R, Brooks B, Thirumalai D. 2007. Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism. J. Am. Chem. Soc. 129:7346-53. (Pubitemid 46980813)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.23 , pp. 7346-7353
    • O'Brien, E.P.1    Dima, R.I.2    Brooks, B.3    Thirumalai, D.4
  • 29
    • 0037442337 scopus 로고    scopus 로고
    • Molecular dynamics simulations of end-to-end contact formation in hydrocarbon chains in water and aqueous urea solution
    • DOI 10.1021/ja020496f
    • Mountain R, Thirumalai D. 2003. Molecular dynamics simulations of end-to-end contact formation in hydrocarbon chains in water and aqueous urea solution. J. Am. Chem. Soc. 125:1950-57. (Pubitemid 36232587)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1950-1957
    • Mountain, R.D.1    Thirumalai, D.2
  • 30
    • 0037343333 scopus 로고    scopus 로고
    • The dominant interaction between peptide and urea is electrostatic in nature: A molecular dynamics simulation study
    • DOI 10.1002/bip.10290
    • Tobi D, Elber R,Thirumalai D. 2003. The dominant interaction between peptide and urea is electrostatic in nature: a molecular dynamics simulation study. Biopolymers 68:359-69. (Pubitemid 36342872)
    • (2003) Biopolymers , vol.68 , Issue.3 , pp. 359-369
    • Tobi, D.1    Elber, R.2    Thirumalai, D.3
  • 32
    • 62449341938 scopus 로고    scopus 로고
    • Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
    • Lim W, R̈ osgen J, Englander S. 2009. Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. Proc. Natl. Acad. Sci. USA 106:2595-600.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2595-2600
    • Lim, W.1    R̈osgen, J.2    Englander, S.3
  • 33
    • 63149153986 scopus 로고    scopus 로고
    • Urea's action on hydrophobic interactions
    • Zangi R, Zhou R, Berne BJ. 2009. Urea's action on hydrophobic interactions. J. Am. Chem. Soc. 131:1535-41.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.2    Berne, B.J.3
  • 34
    • 55949131241 scopus 로고    scopus 로고
    • Urea denaturation by stronger dispersion interactions with proteins than water implies a two-stage unfolding
    • Hua L, Zhou R, Thirumalai D, Berne B. 2008. Urea denaturation by stronger dispersion interactions with proteins than water implies a two-stage unfolding. Proc. Natl. Acad. Sci. USA 105:16928-33.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.4
  • 35
    • 77749285768 scopus 로고    scopus 로고
    • Equilibrium study of protein denaturation by urea
    • Canchi D, Paschek D, Garća A. 2010. Equilibrium study of protein denaturation by urea. J. Am. Chem. Soc. 132:2338-44.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2338-2344
    • Canchi, D.1    Paschek, D.2    Garća, A.3
  • 36
    • 77649101458 scopus 로고    scopus 로고
    • Unfolding of hydrophobic polymers in guanidinium chloride solutions
    • Godawat R, Jamadagni S, Garde S. 2010. Unfolding of hydrophobic polymers in guanidinium chloride solutions. J. Phys. Chem. B 114:2246-54.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2246-2254
    • Godawat, R.1    Jamadagni, S.2    Garde, S.3
  • 37
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • DOI 10.1038/nature04162, PII N04162
    • Chandler D. 2005. Interfaces and the driving force of hydrophobic assembly. Nature 437:640-47. (Pubitemid 41486526)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 640-647
    • Chandler, D.1
  • 38
    • 34250723399 scopus 로고    scopus 로고
    • Aqueous urea solutions: Structure, energetics, and urea aggregation
    • DOI 10.1021/jp066474n
    • Stumpe M, Grubm̈ uller H. 2007. Aqueous urea solutions: structure, energetics, and urea aggregation. J. Phys. Chem. B 111:6220-28. (Pubitemid 46966229)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.22 , pp. 6220-6228
    • Stumpe, M.C.1    Grubmuller, H.2
  • 39
    • 67650363919 scopus 로고    scopus 로고
    • Urea impedes the hydrophobic collapse of partially unfolded proteins
    • Stumpe M, Grubm̈ uller H. 2009. Urea impedes the hydrophobic collapse of partially unfolded proteins. Biophys. J. 96:3744-52.
    • (2009) Biophys. J. , vol.96 , pp. 3744-3752
    • Stumpe, M.1    Grubm̈uller, H.2
  • 40
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • DOI 10.1021/ja710446s
    • Tran HT,Mao A, Pappu RV. 2008. Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins. J. Am. Chem. Soc. 130:7380-92. (Pubitemid 351813231)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.23 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 43
    • 51749109783 scopus 로고    scopus 로고
    • Chemical denaturants inhibit the onset of dewetting
    • England J, Pande V, Haran G. 2008. Chemical denaturants inhibit the onset of dewetting. J. Am. Chem. Soc. 130:11854-55.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11854-11855
    • England, J.1    Pande, V.2    Haran, G.3
  • 44
    • 34247500338 scopus 로고    scopus 로고
    • Effect of ions on the hydrophobic interaction between two plates
    • DOI 10.1021/ja068305m
    • Zangi R, Hagen M, Berne BJ. 2007. Effect of ions on the hydrophobic interaction between two plates. J. Am. Chem. Soc. 129:4678-86. (Pubitemid 46648766)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.15 , pp. 4678-4686
    • Zangi, R.1    Hagen, M.2    Berne, B.J.3
  • 45
    • 0014718113 scopus 로고
    • Protein denaturation: Part C. Theoretical models for the mechanism of denaturation
    • Tanford C. 1970. Protein denaturation: part C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24:1-95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 46
    • 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. 86:2050-59.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 2050-2059
    • Tanford, C.1
  • 47
    • 78651119214 scopus 로고
    • The solubility of amino acids and related compounds in aqueous urea solutions
    • Nozaki Y, Tanford C. 1963. The solubility of amino acids and related compounds in aqueous urea solutions. J. Biol. Chem. 238:4074-81.
    • (1963) J. Biol. Chem. , vol.238 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 48
    • 0014939368 scopus 로고
    • The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
    • Nozaki Y, Tanford C. 1970. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions. J. Biol. Chem. 245:1648-52.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1648-1652
    • Nozaki, Y.1    Tanford, C.2
  • 50
    • 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, Bolen DW. 2004. Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale. Biochemistry 43:1329-42. (Pubitemid 38176532)
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1329-1342
    • Auton, M.1    Bolen, D.W.2
  • 51
    • 0030933329 scopus 로고    scopus 로고
    • Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility
    • DOI 10.1021/bi962819o
    • Creamer TP, Srinivasan R, Rose GD. 1997. Modeling unfolded states of proteins and peptides. II. Backbone solvent accessibility. Biochemistry 36:2832-35. (Pubitemid 27138565)
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 2832-2835
    • Creamer, T.P.1    Srinivasan, R.2    Rose, G.D.3
  • 52
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • Schellman JA. 2003. Protein stability in mixed solvents: a balance of contact interaction and excluded volume. Biophys. J. 85:108-25. (Pubitemid 36753621)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 108-125
    • Schellman, J.A.1
  • 53
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. 1968. Protein denaturation. Protein Fold. Cell 23:121-282.
    • (1968) Protein Fold. Cell , vol.23 , pp. 121-282
    • Tanford, C.1
  • 54
    • 0036400715 scopus 로고    scopus 로고
    • Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    • DOI 10.1016/S0065-3233(02)62012-1
    • Dyson HJ, Wright PE. 2002. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv. Protein Chem. 62:311-40. (Pubitemid 35204875)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 311-340
    • Dyson, H.J.1    Wright, P.E.2
  • 55
    • 0038581168 scopus 로고    scopus 로고
    • Polymeric aspects of protein folding: A brief overview
    • DOI 10.2174/0929866033478988
    • Tcherkasskaya O, Uversky VN. 2003. Polymeric aspects of protein folding: a brief overview. Protein Peptide Lett. 10:239-45. (Pubitemid 36614848)
    • (2003) Protein and Peptide Letters , vol.10 , Issue.3 , pp. 239-245
    • Tcherkasskaya, O.1    Uversky, V.N.2
  • 59
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • DOI 10.1016/j.sbi.2007.01.009, PII S0959440X07000103, Foldinf and Binding / Protein-Nucleic Interactions
    • Mittag T, Forman-Kay JD. 2007. Atomic-level characterization of disordered protein ensembles. Curr. Opin. Struct. Biol. 17:3-14. (Pubitemid 46240819)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 60
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by single-molecule FRET
    • Schuler B, Eaton WA. 2008. Protein folding studied by single-molecule FRET. Curr. Opin. Struct. Biol. 18:16-26.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 63
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • Schuler B, Lipman EA, EatonWA. 2002. Probing the free energy surface for protein folding with single molecule fluorescence spectroscopy. Nature 419:743-47. (Pubitemid 35177962)
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 64
    • 33644767158 scopus 로고    scopus 로고
    • Single-molecule FRET study of denaturant induced unfolding of RNase H
    • DOI 10.1016/j.jmb.2005.12.061, PII S0022283605016372
    • Kuzmenkina EV, Heyes CD, Nienhaus GU. 2006. Single-molecule FRET study of denaturant induced unfolding of RNase H. J. Mol. Biol. 357:313-24. (Pubitemid 43339333)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.1 , pp. 313-324
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Ulrich Nienhaus, G.3
  • 66
    • 0029859858 scopus 로고    scopus 로고
    • Surface point mutations that significantly alter the structure and stability of a protein's denatured state
    • Smith CK, Bu Z, Anderson KS, Sturtevant JM, Engelman DM, Regan L. 1996. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Sci. 5:2009-19. (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
  • 67
    • 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, KayatekinC,MatthewsCR, IwakuraM, Bilsel O. 2007. Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an α/β-type protein. J. Mol. Biol. 368:219-29. (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
  • 69
    • 0032978994 scopus 로고    scopus 로고
    • Chain collapse can occur concomitantly with the rate-limiting step in protein folding
    • DOI 10.1038/9329
    • Plaxco KW, Millett IS, Segel DJ, Doniach S, Baker D. 1999. Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nat. Struct. Biol. 6:554-56. (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
  • 71
    • 33847401358 scopus 로고    scopus 로고
    • Fully Reduced Ribonuclease A Does not Expand at High Denaturant Concentration or Temperature
    • DOI 10.1016/j.jmb.2007.01.012, PII S0022283607000381
    • Jacob J, Dothager RS, Thiyagarajan P, Sosnick TR. 2007. Fully reduced ribonuclease A does not expand at high denaturant concentration or temperature. J. Mol. Biol. 367:609-15. (Pubitemid 46343734)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.3 , pp. 609-615
    • Jacob, J.1    Dothager, R.S.2    Thiyagarajan, P.3    Sosnick, T.R.4
  • 72
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin PR. 2000. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7:730-34.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 73
    • 33646937406 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of protein folding and conformational dynamics
    • DOI 10.1021/cr0404343
    • Michalet X,Weiss S, Jager M. 2006. Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem. Rev. 106:1785-813. (Pubitemid 43792781)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1785-1813
    • Michalet, X.1    Weiss, S.2    Jager, M.3
  • 74
    • 5844250551 scopus 로고
    • The coil-globule transition: Radius of gyration of polystyrene in cyclohexane
    • Sun ST, Nishio I, Swislow G, Tanaka T. 1980. The coil-globule transition: radius of gyration of polystyrene in cyclohexane. J. Chem. Phys. 73:5971-75.
    • (1980) J. Chem. Phys. , vol.73 , pp. 5971-5975
    • Sun, S.T.1    Nishio, I.2    Swislow, G.3    Tanaka, T.4
  • 75
  • 76
    • 0026839336 scopus 로고
    • Quantitative theory of the globule-to-coil transition. 1. Link density distribution in a globule and its radius of gyration
    • Grosberg AY, Kuznetsov DV. 1992. Quantitative theory of the globule-to-coil transition. 1. Link density distribution in a globule and its radius of gyration. Macromolecules 25:1970-79.
    • (1992) Macromolecules , vol.25 , pp. 1970-1979
    • Grosberg, A.Y.1    Kuznetsov, D.V.2
  • 77
    • 0001237577 scopus 로고
    • Phase transition behavior of the isolated polymer chain
    • Sanchez IC. 1979. Phase transition behavior of the isolated polymer chain. Macromolecules 12:980-88.
    • (1979) Macromolecules , vol.12 , pp. 980-988
    • Sanchez, I.C.1
  • 79
    • 67749142097 scopus 로고    scopus 로고
    • Protein folding, protein collapse, and Tanford's transfer model: Lessons from single-molecule FRET
    • Ziv G, Haran G. 2009. Protein folding, protein collapse, and Tanford's transfer model: lessons from single-molecule FRET. J. Am. Chem. Soc. 131:2942-47.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2942-2947
    • Ziv, G.1    Haran, G.2
  • 82
  • 83
    • 51649087154 scopus 로고    scopus 로고
    • Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model
    • O'Brien EP, Ziv G, Haran G, Brooks BR, Thirumalai D. 2008. Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer model. Proc. Natl. Acad. Sci. USA 105:13403-8.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13403-13408
    • O'Brien, E.P.1    Ziv, G.2    Haran, G.3    Brooks, B.R.4    Thirumalai, D.5
  • 84
    • 65249157127 scopus 로고    scopus 로고
    • Why water reorientation slows without iceberg formation around hydrophobic solutes
    • Laage D, Stirnemann G, Hynes JT. 2009. Why water reorientation slows without iceberg formation around hydrophobic solutes. J. Phys. Chem. B 113:2428-35.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2428-2435
    • Laage, D.1    Stirnemann, G.2    Hynes, J.T.3
  • 85
    • 70449562714 scopus 로고    scopus 로고
    • Ultrafast vibrational spectroscopy of a degenerate mode of guanidinium chloride
    • Vorobyev DY, Kuo CH, Chen JX, Kuroda DG, Scott JN, et al. 2009. Ultrafast vibrational spectroscopy of a degenerate mode of guanidinium chloride. J. Phys. Chem. B 113:15382-91
    • (2009) J. Phys. Chem. B , vol.113 , pp. 15382-15391
    • Vorobyev, D.Y.1    Kuo, C.H.2    Chen, J.X.3    Kuroda, D.G.4    Scott, J.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.