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Volumn 11, Issue 7, 2015, Pages 3478-3490

Macromolecular Stabilization by Excluded Cosolutes: Mean Field Theory of Crowded Solutions

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EID: 84949668984     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/acs.jctc.5b00258     Document Type: Article
Times cited : (33)

References (96)
  • 1
    • 0036204260 scopus 로고    scopus 로고
    • Protein-Water Interactions
    • Parsegian, V. A. Protein-Water Interactions Int. Rev. Cytol. 2002, 215, 1-31
    • (2002) Int. Rev. Cytol. , vol.215 , pp. 1-31
    • Parsegian, V.A.1
  • 4
    • 0020336190 scopus 로고
    • Living with Water-Stress - Evolution of Osmolyte Systems
    • Yancey, P. H.; Clark, M. E.; Hand, S. C.; Bowlus, R. D.; Somero, G. N. Living with Water-Stress-Evolution of Osmolyte Systems Science 1982, 217, 1214-1222
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 5
    • 24644450812 scopus 로고    scopus 로고
    • Organic Osmolytes as Compatible, Metabolic and Counteracting Cytoprotectants in High Osmolarity and Other Stresses
    • Yancey, P. H. Organic Osmolytes as Compatible, Metabolic and Counteracting Cytoprotectants in High Osmolarity and Other Stresses J. Exp. Biol. 2005, 208, 2819-2830
    • (2005) J. Exp. Biol. , vol.208 , pp. 2819-2830
    • Yancey, P.H.1
  • 6
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and Biological Approaches for Adapting Proteostasis to Ameliorate Protein Misfolding and Aggregation Diseases: Progress and Prognosis
    • Lindquist, S. L.; Kelly, J. W. Chemical and Biological Approaches for Adapting Proteostasis to Ameliorate Protein Misfolding and Aggregation Diseases: Progress and Prognosis Cold Spring Harbor Perspect. Biol. 2011, 3, a004507
    • (2011) Cold Spring Harbor Perspect. Biol. , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 7
    • 0000063775 scopus 로고
    • On the Equilibrium of Heterogeneous Substances
    • 343-524
    • Gibbs, J. W. On the Equilibrium of Heterogeneous Substances Trans. Conn. Acad. Arts Sci. 1876, 3, 108-248/343-524
    • (1876) Trans. Conn. Acad. Arts Sci. , vol.3 , pp. 108-248
    • Gibbs, J.W.1
  • 8
    • 0016292941 scopus 로고
    • Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, A-Chymotrypsin, and B-Lactoglobulin
    • Greene, R.; Pace, C. Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, A-Chymotrypsin, and B-Lactoglobulin J. Biol. Chem. 1974, 249, 5388-5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.1    Pace, C.2
  • 9
    • 33751132430 scopus 로고
    • The Statistical Mechanical Theory of Solutions. I
    • Kirkwood, J. G.; Buff, F. P. The Statistical Mechanical Theory of Solutions. I J. Chem. Phys. 1951, 19, 774-777
    • (1951) J. Chem. Phys. , vol.19 , pp. 774-777
    • Kirkwood, J.G.1    Buff, F.P.2
  • 10
    • 84898421978 scopus 로고    scopus 로고
    • Preferential Solvation: Dividing Surface vs Excess Numbers
    • Shimizu, S.; Matubayasi, N. Preferential Solvation: Dividing Surface vs Excess Numbers J. Phys. Chem. B 2014, 118, 3922-3930
    • (2014) J. Phys. Chem. B , vol.118 , pp. 3922-3930
    • Shimizu, S.1    Matubayasi, N.2
  • 11
    • 84922778919 scopus 로고    scopus 로고
    • Is the Depletion Force Entropic? Molecular Crowding beyond Steric Interactions
    • Sapir, L.; Harries, D. Is the Depletion Force Entropic? Molecular Crowding beyond Steric Interactions Curr. Opin. Colloid Interface Sci. 2015, 20, 3-10
    • (2015) Curr. Opin. Colloid Interface Sci. , vol.20 , pp. 3-10
    • Sapir, L.1    Harries, D.2
  • 12
    • 0016814310 scopus 로고
    • Hydrophobic Interaction and Structural Changes in the Solvent
    • Ben-Naim, A. Hydrophobic Interaction and Structural Changes in the Solvent Biopolymers 1975, 14, 1337-1355
    • (1975) Biopolymers , vol.14 , pp. 1337-1355
    • Ben-Naim, A.1
  • 13
    • 36549101599 scopus 로고
    • A Thermodynamic Analysis of Solvation
    • Yu, H.-A.; Karplus, M. A Thermodynamic Analysis of Solvation J. Chem. Phys. 1988, 89, 2366
    • (1988) J. Chem. Phys. , vol.89 , pp. 2366
    • Yu, H.-A.1    Karplus, M.2
  • 15
    • 2442610396 scopus 로고    scopus 로고
    • Energy-Entropy Compensation in the Transfer of Nonpolar Solutes from Water to Cosolvent/water Mixtures
    • van der Vegt, N. F. A.; Trzesniak, D.; Kasumaj, B.; van Gunsteren, W. F. Energy-Entropy Compensation in the Transfer of Nonpolar Solutes from Water to Cosolvent/water Mixtures ChemPhysChem 2004, 5, 144-147
    • (2004) ChemPhysChem , vol.5 , pp. 144-147
    • Van Der Vegt, N.F.A.1    Trzesniak, D.2    Kasumaj, B.3    Van Gunsteren, W.F.4
  • 16
    • 33645999511 scopus 로고
    • On Interaction between Two Bodies Immersed in a Solution of Macromolecules
    • Asakura, S.; Oosawa, F. On Interaction between Two Bodies Immersed in a Solution of Macromolecules J. Chem. Phys. 1954, 22, 1255-1256
    • (1954) J. Chem. Phys. , vol.22 , pp. 1255-1256
    • Asakura, S.1    Oosawa, F.2
  • 17
    • 0000303810 scopus 로고
    • Interaction between Particles Suspended in Solutions of Macromolecules
    • Asakura, S.; Oosawa, F. Interaction between Particles Suspended in Solutions of Macromolecules J. Polym. Sci. 1958, 33, 183-192
    • (1958) J. Polym. Sci. , vol.33 , pp. 183-192
    • Asakura, S.1    Oosawa, F.2
  • 18
    • 84985735713 scopus 로고
    • Excluded Volume as a Determinant of Macromolecular Structure and Reactivity
    • Minton, A. Excluded Volume as a Determinant of Macromolecular Structure and Reactivity Biopolymers 1981, 20, 2093-2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.1
  • 19
    • 16344389134 scopus 로고    scopus 로고
    • Molecular Crowding Enhances Native State Stability and Refolding Rates of Globular Proteins
    • Cheung, M. S.; Klimov, D.; Thirumalai, D. Molecular Crowding Enhances Native State Stability and Refolding Rates of Globular Proteins Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 4753-4758
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4753-4758
    • Cheung, M.S.1    Klimov, D.2    Thirumalai, D.3
  • 20
    • 0034635965 scopus 로고    scopus 로고
    • Osmotic Stress, Crowding, Preferential Hydration, and Binding: A Comparison of Perspectives
    • Parsegian, V. A.; Rand, R. P.; Rau, D. C. Osmotic Stress, Crowding, Preferential Hydration, and Binding: A Comparison of Perspectives Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 3987-3992
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3987-3992
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 21
    • 84896699919 scopus 로고    scopus 로고
    • Synthetic Crowding Agent Dextran Causes Excluded Volume Interactions Exclusively to Tracer Protein Apoazurin
    • Christiansen, A.; Wittung-Stafshede, P. Synthetic Crowding Agent Dextran Causes Excluded Volume Interactions Exclusively to Tracer Protein Apoazurin FEBS Lett. 2014, 588, 811-814
    • (2014) FEBS Lett. , vol.588 , pp. 811-814
    • Christiansen, A.1    Wittung-Stafshede, P.2
  • 22
    • 0028822574 scopus 로고
    • A Molecular Model for the Dependence of the Osmotic Pressure of Bovine Serum Albumin upon Concentration and pH
    • Minton, A. P. A Molecular Model for the Dependence of the Osmotic Pressure of Bovine Serum Albumin upon Concentration and pH Biophys. Chem. 1995, 57, 65-70
    • (1995) Biophys. Chem. , vol.57 , pp. 65-70
    • Minton, A.P.1
  • 24
    • 77955699308 scopus 로고    scopus 로고
    • Attractive Protein-Polymer Interactions Markedly Alter the Effect of Macromolecular Crowding on Protein Association Equilibria
    • Jiao, M.; Li, H.-T.; Chen, J.; Minton, A. P.; Liang, Y. Attractive Protein-Polymer Interactions Markedly Alter the Effect of Macromolecular Crowding on Protein Association Equilibria Biophys. J. 2010, 99, 914-923
    • (2010) Biophys. J. , vol.99 , pp. 914-923
    • Jiao, M.1    Li, H.-T.2    Chen, J.3    Minton, A.P.4    Liang, Y.5
  • 25
    • 77956022419 scopus 로고    scopus 로고
    • Enthalpically Driven Peptide Stabilization by Protective Osmolytes
    • Politi, R.; Harries, D. Enthalpically Driven Peptide Stabilization by Protective Osmolytes Chem. Commun. 2010, 46, 6449-6451
    • (2010) Chem. Commun. , vol.46 , pp. 6449-6451
    • Politi, R.1    Harries, D.2
  • 29
    • 84870899331 scopus 로고    scopus 로고
    • Unexpected Effects of Macromolecular Crowding on Protein Stability
    • Benton, L. A.; Smith, A. E.; Young, G. B.; Pielak, G. J. Unexpected Effects of Macromolecular Crowding on Protein Stability Biochemistry 2012, 51, 9773-9775
    • (2012) Biochemistry , vol.51 , pp. 9773-9775
    • Benton, L.A.1    Smith, A.E.2    Young, G.B.3    Pielak, G.J.4
  • 30
    • 84870931817 scopus 로고    scopus 로고
    • Diversity in the Mechanisms of Cosolute Action on Biomolecular Processes
    • Sukenik, S.; Sapir, L.; Gilman-Politi, R.; Harries, D. Diversity in the Mechanisms of Cosolute Action on Biomolecular Processes Faraday Discuss. 2013, 160, 225
    • (2013) Faraday Discuss. , vol.160 , pp. 225
    • Sukenik, S.1    Sapir, L.2    Gilman-Politi, R.3    Harries, D.4
  • 32
    • 84874194203 scopus 로고    scopus 로고
    • Polymer Crowders and Protein Crowders Act Similarly on Protein Folding Stability
    • Zhou, H.-X. Polymer Crowders and Protein Crowders Act Similarly on Protein Folding Stability FEBS Lett. 2013, 587, 394-397
    • (2013) FEBS Lett. , vol.587 , pp. 394-397
    • Zhou, H.-X.1
  • 33
    • 84877014249 scopus 로고    scopus 로고
    • Soft Interactions and Crowding
    • Sarkar, M.; Li, C.; Pielak, G. J. Soft Interactions and Crowding Biophys. Rev. 2013, 5, 187-194
    • (2013) Biophys. Rev. , vol.5 , pp. 187-194
    • Sarkar, M.1    Li, C.2    Pielak, G.J.3
  • 34
    • 84903287318 scopus 로고    scopus 로고
    • Protein Stabilization by Macromolecular Crowding through Enthalpy rather than Entropy
    • Senske, M.; Törk, L.; Born, B.; Havenith, M.; Herrmann, C.; Ebbinghaus, S. Protein Stabilization by Macromolecular Crowding through Enthalpy rather than Entropy J. Am. Chem. Soc. 2014, 136, 9036-9041
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 9036-9041
    • Senske, M.1    Törk, L.2    Born, B.3    Havenith, M.4    Herrmann, C.5    Ebbinghaus, S.6
  • 35
    • 0038311869 scopus 로고    scopus 로고
    • Protein Stability in Mixed Solvents: A Balance of Contact Interaction and Excluded Volume
    • Schellman, J. A. Protein Stability in Mixed Solvents: A Balance of Contact Interaction and Excluded Volume Biophys. J. 2003, 85, 108-125
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 36
    • 84877808384 scopus 로고    scopus 로고
    • Crowding Induced Entropy-Enthalpy Compensation in Protein Association Equilibria
    • Kim, Y. C.; Mittal, J. Crowding Induced Entropy-Enthalpy Compensation in Protein Association Equilibria Phys. Rev. Lett. 2013, 110, 208102
    • (2013) Phys. Rev. Lett. , vol.110 , pp. 208102
    • Kim, Y.C.1    Mittal, J.2
  • 39
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular Crowding: Qualitative and Semiquantitative Successes, Quantitative Challenges
    • Hall, D.; Minton, A. P. Macromolecular Crowding: Qualitative and Semiquantitative Successes, Quantitative Challenges Biochim. Biophys. Acta, Proteins Proteomics 2003, 1649, 127-139
    • (2003) Biochim. Biophys. Acta, Proteins Proteomics , vol.1649 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 40
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences
    • Zhou, H.-X.; Rivas, G.; Minton, A. P. Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences Annu. Rev. Biophys. 2008, 37, 375-397
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.-X.1    Rivas, G.2    Minton, A.P.3
  • 41
  • 42
    • 84872904773 scopus 로고    scopus 로고
    • Quantitative Assessment of the Relative Contributions of Steric Repulsion and Chemical Interactions to Macromolecular Crowding
    • Minton, A. P. Quantitative Assessment of the Relative Contributions of Steric Repulsion and Chemical Interactions to Macromolecular Crowding Biopolymers 2013, 99, 239-244
    • (2013) Biopolymers , vol.99 , pp. 239-244
    • Minton, A.P.1
  • 43
    • 84898074097 scopus 로고    scopus 로고
    • Origin of Enthalpic Depletion Forces
    • Sapir, L.; Harries, D. Origin of Enthalpic Depletion Forces J. Phys. Chem. Lett. 2014, 5, 1061-1065
    • (2014) J. Phys. Chem. Lett. , vol.5 , pp. 1061-1065
    • Sapir, L.1    Harries, D.2
  • 44
    • 42749107502 scopus 로고    scopus 로고
    • Effect of Repulsive and Attractive Interactions on Depletion Forces in Colloidal Suspensions: A Density Functional Theory Treatment
    • Egorov, S. Effect of Repulsive and Attractive Interactions on Depletion Forces in Colloidal Suspensions: A Density Functional Theory Treatment Phys. Rev. E 2004, 70, 1-8
    • (2004) Phys. Rev. E , vol.70 , pp. 1-8
    • Egorov, S.1
  • 45
    • 33748687979 scopus 로고    scopus 로고
    • Effective Forces in Colloidal Mixtures: From Depletion Attraction to Accumulation Repulsion
    • Louis, A.; Allahyarov, E.; Löwen, H.; Roth, R. Effective Forces in Colloidal Mixtures: From Depletion Attraction to Accumulation Repulsion Phys. Rev. E 2002, 65, 061407
    • (2002) Phys. Rev. E , vol.65 , pp. 061407
    • Louis, A.1    Allahyarov, E.2    Löwen, H.3    Roth, R.4
  • 46
    • 84923262147 scopus 로고    scopus 로고
    • Coarse-Grained Molecular Dynamics Simulations of Depletion-Induced Interactions for Soft Matter Systems
    • Shendruk, T. N.; Bertrand, M.; Harden, J. L.; Slater, G. W.; de Haan, H. W. Coarse-Grained Molecular Dynamics Simulations of Depletion-Induced Interactions for Soft Matter Systems J. Chem. Phys. 2014, 141, 244910
    • (2014) J. Chem. Phys. , vol.141 , pp. 244910
    • Shendruk, T.N.1    Bertrand, M.2    Harden, J.L.3    Slater, G.W.4    De Haan, H.W.5
  • 47
    • 84919897990 scopus 로고    scopus 로고
    • How Soft Repulsion Enhances the Depletion Mechanism
    • Rovigatti, L.; Gnan, N.; Parola, A.; Zaccarelli, E. How Soft Repulsion Enhances the Depletion Mechanism Soft Matter 2015, 11, 692-700
    • (2015) Soft Matter , vol.11 , pp. 692-700
    • Rovigatti, L.1    Gnan, N.2    Parola, A.3    Zaccarelli, E.4
  • 49
    • 0008883222 scopus 로고
    • Thermodynamics of High Polymer Solutions
    • Flory, P. J. Thermodynamics of High Polymer Solutions J. Chem. Phys. 1942, 10, 51-61
    • (1942) J. Chem. Phys. , vol.10 , pp. 51-61
    • Flory, P.J.1
  • 50
    • 0003411482 scopus 로고
    • Cornell University Press: Ithaca, New York
    • Flory, P. J. Principles of Polymer Chemistry; Cornell University Press: Ithaca, New York, 1953; pp 495-540.
    • (1953) Principles of Polymer Chemistry , pp. 495-540
    • Flory, P.J.1
  • 51
    • 84989989842 scopus 로고
    • Thermodynamic Proerties of Solutions of Long-Chain Compounds
    • Huggins, M. L. Thermodynamic Proerties of Solutions of Long-Chain Compounds Ann. N.Y. Acad. Sci. 1942, 43, 1-32
    • (1942) Ann. N.Y. Acad. Sci. , vol.43 , pp. 1-32
    • Huggins, M.L.1
  • 52
    • 33947562256 scopus 로고
    • Some Properties of Solutions of Long-Chain Compounds
    • Huggins, M. L. Some Properties of Solutions of Long-Chain Compounds J. Phys. Chem. 1942, 46, 151-158
    • (1942) J. Phys. Chem. , vol.46 , pp. 151-158
    • Huggins, M.L.1
  • 54
    • 0014604482 scopus 로고
    • Thermodynamics of the Denaturation of Lysozyme by Guanidine Hydrochloride. II. Dependence on Denaturant Concentration at 25
    • Aune, K.; Tanford, C. Thermodynamics of the Denaturation of Lysozyme by Guanidine Hydrochloride. II. Dependence on Denaturant Concentration at 25 Biochemistry 1969, 8, 4586-4590
    • (1969) Biochemistry , vol.8 , pp. 4586-4590
    • Aune, K.1    Tanford, C.2
  • 55
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the Energetics of Osmolyte-Induced Protein Folding/unfolding
    • Auton, M.; Bolen, D. W. Predicting the Energetics of Osmolyte-Induced Protein Folding/unfolding Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 15065-15068
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 56
    • 49649112395 scopus 로고    scopus 로고
    • Thermodynamic Origin of Hofmeister Ion Effects
    • Pegram, L. M.; Record, M. T., Jr. Thermodynamic Origin of Hofmeister Ion Effects J. Phys. Chem. B 2008, 112, 9428-9436
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9428-9436
    • Pegram, L.M.1    Record, M.T.2
  • 57
    • 70350513011 scopus 로고    scopus 로고
    • Interactions of the Osmolyte Glycine Betaine with Molecular Surfaces in Water: Thermodynamics, Structural Interpretation, and Prediction of M-Values
    • Capp, M. W.; Pegram, L. M.; Saecker, R. M.; Kratz, M.; Riccardi, D.; Wendorff, T.; Cannon, J. G.; Record, M. T., Jr. Interactions of the Osmolyte Glycine Betaine with Molecular Surfaces in Water: Thermodynamics, Structural Interpretation, and Prediction of M-Values Biochemistry 2009, 48, 10372-10379
    • (2009) Biochemistry , vol.48 , pp. 10372-10379
    • Capp, M.W.1    Pegram, L.M.2    Saecker, R.M.3    Kratz, M.4    Riccardi, D.5    Wendorff, T.6    Cannon, J.G.7    Record, M.T.8
  • 58
    • 84883484766 scopus 로고    scopus 로고
    • Quantifying Additive Interactions of the Osmolyte Proline with Individual Functional Groups of Proteins: Comparisons with Urea and Glycine Betaine, Interpretation of M-Values
    • Diehl, R. C.; Guinn, E. J.; Capp, M. W.; Tsodikov, O. V.; Record, M. T. Quantifying Additive Interactions of the Osmolyte Proline with Individual Functional Groups of Proteins: Comparisons with Urea and Glycine Betaine, Interpretation of M-Values Biochemistry 2013, 52, 5997-6010
    • (2013) Biochemistry , vol.52 , pp. 5997-6010
    • Diehl, R.C.1    Guinn, E.J.2    Capp, M.W.3    Tsodikov, O.V.4    Record, M.T.5
  • 59
    • 84892576511 scopus 로고    scopus 로고
    • Unified Description of Urea Denaturation: Backbone and Side Chains Contribute Equally in the Transfer Model
    • Moeser, B.; Horinek, D. Unified Description of Urea Denaturation: Backbone and Side Chains Contribute Equally in the Transfer Model J. Phys. Chem. B 2014, 118, 107-114
    • (2014) J. Phys. Chem. B , vol.118 , pp. 107-114
    • Moeser, B.1    Horinek, D.2
  • 60
    • 84908200581 scopus 로고    scopus 로고
    • The Role of the Concentration Scale in the Definition of Transfer Free Energies
    • Moeser, B.; Horinek, D. The Role of the Concentration Scale in the Definition of Transfer Free Energies Biophys. Chem. 2015, 196, 68-76
    • (2015) Biophys. Chem. , vol.196 , pp. 68-76
    • Moeser, B.1    Horinek, D.2
  • 63
    • 80755150222 scopus 로고    scopus 로고
    • Unraveling the Molecular Mechanism of Enthalpy Driven Peptide Folding by Polyol Osmolytes
    • Gilman-Politi, R.; Harries, D. Unraveling the Molecular Mechanism of Enthalpy Driven Peptide Folding by Polyol Osmolytes J. Chem. Theory Comput. 2011, 60, 4482-3828
    • (2011) J. Chem. Theory Comput. , vol.60 , pp. 4482-3828
    • Gilman-Politi, R.1    Harries, D.2
  • 64
    • 35448999589 scopus 로고    scopus 로고
    • A Practical Guide on How Osmolytes Modulate Macromolecular Properties
    • Elsevier Academic Press Inc. New York
    • Harries, D.; Rösgen, J. A Practical Guide on How Osmolytes Modulate Macromolecular Properties. In Biophysical Tools for Biologists: Vol 1 in Vitro Techniques; Elsevier Academic Press Inc.: New York, 2008; Vol. 84, 679-735.
    • (2008) Biophysical Tools for Biologists: Vol 1 in Vitro Techniques , vol.84 , pp. 679-735
    • Harries, D.1    Rösgen, J.2
  • 65
    • 13944258032 scopus 로고    scopus 로고
    • Solutes Probe Hydration in Specific Association of Cyclodextrin and Adamantane
    • Harries, D.; Rau, D. C.; Parsegian, V. A. Solutes Probe Hydration in Specific Association of Cyclodextrin and Adamantane J. Am. Chem. Soc. 2005, 127, 2184-2190
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2184-2190
    • Harries, D.1    Rau, D.C.2    Parsegian, V.A.3
  • 66
    • 12344271184 scopus 로고    scopus 로고
    • On the Salt-Induced Stabilization of Pair and Many-Body Hydrophobic Interactions
    • Ghosh, T.; Kalra, A.; Garde, S. On the Salt-Induced Stabilization of Pair and Many-Body Hydrophobic Interactions J. Phys. Chem. B 2005, 109, 642-651
    • (2005) J. Phys. Chem. B , vol.109 , pp. 642-651
    • Ghosh, T.1    Kalra, A.2    Garde, S.3
  • 67
    • 0003516749 scopus 로고    scopus 로고
    • 9 th ed. Oxford University Press: Oxford, UK
    • Atkins, P.; De Paula, J. Physical Chemistry, 9 th ed.; Oxford University Press: Oxford, UK, 2010; pp 168-169.
    • (2010) Physical Chemistry , pp. 168-169
    • Atkins, P.1    De Paula, J.2
  • 68
    • 33845408125 scopus 로고    scopus 로고
    • Sequence-Specific Solvent Accessibilities of Protein Residues in Unfolded Protein Ensembles
    • Bernadó, P.; Blackledge, M.; Sancho, J. Sequence-Specific Solvent Accessibilities of Protein Residues in Unfolded Protein Ensembles Biophys. J. 2006, 91, 4536-4543
    • (2006) Biophys. J. , vol.91 , pp. 4536-4543
    • Bernadó, P.1    Blackledge, M.2    Sancho, J.3
  • 69
    • 65449171120 scopus 로고    scopus 로고
    • ProtSA: A Web Application for Calculating Sequence Specific Protein Solvent Accessibilities in the Unfolded Ensemble
    • Estrada, J.; Bernadó, P.; Blackledge, M.; Sancho, J. ProtSA: A Web Application for Calculating Sequence Specific Protein Solvent Accessibilities in the Unfolded Ensemble BMC Bioinf. 2009, 10, 104
    • (2009) BMC Bioinf. , vol.10 , pp. 104
    • Estrada, J.1    Bernadó, P.2    Blackledge, M.3    Sancho, J.4
  • 71
    • 0023652256 scopus 로고
    • Crystal and Molecular Structure of the Serine Proteinase Inhibitor CI-2 from Barley Seeds
    • McPhalen, C. A.; James, M. N. Crystal and Molecular Structure of the Serine Proteinase Inhibitor CI-2 from Barley Seeds Biochemistry 1987, 26, 261-269
    • (1987) Biochemistry , vol.26 , pp. 261-269
    • McPhalen, C.A.1    James, M.N.2
  • 72
    • 0023644679 scopus 로고
    • Structure of Ubiquitin Refined at 1.8 A Resolution
    • Vijay-Kumar, S.; Bugg, C. E.; Cook, W. J. Structure of Ubiquitin Refined at 1.8 A Resolution J. Mol. Biol. 1987, 194, 531-544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 73
    • 0030585408 scopus 로고    scopus 로고
    • Crystal Structures of Guinea-Pig, Goat and Bovine Alpha-Lactalbumin Highlight the Enhanced Conformational Flexibility of Regions That Are Significant for Its Action in Lactose Synthase
    • Pike, A. C.; Brew, K.; Acharya, K. R. Crystal Structures of Guinea-Pig, Goat and Bovine Alpha-Lactalbumin Highlight the Enhanced Conformational Flexibility of Regions That Are Significant for Its Action in Lactose Synthase Structure 1996, 4, 691-703
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.1    Brew, K.2    Acharya, K.R.3
  • 74
    • 0024700561 scopus 로고
    • Thermodynamic Properties of Aqueous Polymer Solutions: Poly(ethy1ene glycol)/Dextran
    • Haynes, C. A.; Beynon, R. A.; Blanch, H. W.; Prausnitz, J. M. Thermodynamic Properties of Aqueous Polymer Solutions: Poly(ethy1ene glycol)/Dextran J. Phys. Chem. 1989, 93, 5612-5617
    • (1989) J. Phys. Chem. , vol.93 , pp. 5612-5617
    • Haynes, C.A.1    Beynon, R.A.2    Blanch, H.W.3    Prausnitz, J.M.4
  • 75
    • 46849119989 scopus 로고    scopus 로고
    • Pullulan and Dextran: Uncommon Composition Dependent Flory-Huggins Interaction Parameters of Their Aqueous Solutions
    • Eckelt, J.; Sugaya, R.; Wolf, B. A. Pullulan and Dextran: Uncommon Composition Dependent Flory-Huggins Interaction Parameters of Their Aqueous Solutions Biomacromolecules 2008, 9, 1691-1697
    • (2008) Biomacromolecules , vol.9 , pp. 1691-1697
    • Eckelt, J.1    Sugaya, R.2    Wolf, B.A.3
  • 76
    • 84855657198 scopus 로고    scopus 로고
    • Dextran-Based Polycations: Thermodynamic Interaction with Water as Compared with Unsubstituted Dextran, 2 - Flory/Huggins Interaction Parameter
    • Bercea, M.; Nichifor, M.; Eckelt, J.; Wolf, B. A. Dextran-Based Polycations: Thermodynamic Interaction with Water as Compared With Unsubstituted Dextran, 2-Flory/Huggins Interaction Parameter Macromol. Chem. Phys. 2011, 212, 1932-1940
    • (2011) Macromol. Chem. Phys. , vol.212 , pp. 1932-1940
    • Bercea, M.1    Nichifor, M.2    Eckelt, J.3    Wolf, B.A.4
  • 77
    • 0032804867 scopus 로고    scopus 로고
    • Measurement of Activity of Water in Aqueous Poly(ethylene Glycol) Solutions (Effect of Excess Volume on the Flory-Huggins Ø-Parameter)
    • Eliassi, A.; Modarress, H.; Mansoori, G. A. Measurement of Activity of Water in Aqueous Poly(ethylene Glycol) Solutions (Effect of Excess Volume on the Flory-Huggins Ø-Parameter) J. Chem. Eng. Data 1999, 44, 52-55
    • (1999) J. Chem. Eng. Data , vol.44 , pp. 52-55
    • Eliassi, A.1    Modarress, H.2    Mansoori, G.A.3
  • 78
    • 77749285768 scopus 로고    scopus 로고
    • Equilibrium Study of Protein Denaturation by Urea
    • Canchi, D. R.; Paschek, D.; García, A. E. Equilibrium Study of Protein Denaturation by Urea J. Am. Chem. Soc. 2010, 132, 2338-2344
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2338-2344
    • Canchi, D.R.1    Paschek, D.2    García, A.E.3
  • 79
    • 76749109966 scopus 로고    scopus 로고
    • Hydrogen Bonding Progressively Strengthens upon Transfer of the Protein Urea-Denatured State to Water and Protecting Osmolytes
    • Holthauzen, L. M. F.; Rösgen, J.; Bolen, D. W. Hydrogen Bonding Progressively Strengthens upon Transfer of the Protein Urea-Denatured State to Water and Protecting Osmolytes Biochemistry 2010, 49, 1310-1318
    • (2010) Biochemistry , vol.49 , pp. 1310-1318
    • Holthauzen, L.M.F.1    Rösgen, J.2    Bolen, D.W.3
  • 80
    • 84903757486 scopus 로고    scopus 로고
    • Direct Osmolyte-Macromolecule Interactions Confer Entropic Stability to Folded States
    • Rodríguez-Ropero, F.; van der Vegt, N. F. A. Direct Osmolyte-Macromolecule Interactions Confer Entropic Stability to Folded States J. Phys. Chem. B 2014, 118, 7327-7334
    • (2014) J. Phys. Chem. B , vol.118 , pp. 7327-7334
    • Rodríguez-Ropero, F.1    Van Der Vegt, N.F.A.2
  • 81
    • 84873675053 scopus 로고    scopus 로고
    • Rationalizing Polymer Swelling and Collapse under Attractive Cosolvent Conditions
    • Heyda, J.; Muzdalo, A.; Dzubiella, J. Rationalizing Polymer Swelling and Collapse under Attractive Cosolvent Conditions Macromolecules 2013, 46, 1231-1238
    • (2013) Macromolecules , vol.46 , pp. 1231-1238
    • Heyda, J.1    Muzdalo, A.2    Dzubiella, J.3
  • 82
    • 84921375862 scopus 로고    scopus 로고
    • Polymer Collapse in Miscible Good Solvents Is a Generic Phenomenon Driven by Preferential Adsorption
    • Mukherji, D.; Marques, C. M.; Kremer, K. Polymer Collapse in Miscible Good Solvents Is a Generic Phenomenon Driven by Preferential Adsorption Nat. Commun. 2014, 5, 4882
    • (2014) Nat. Commun. , vol.5 , pp. 4882
    • Mukherji, D.1    Marques, C.M.2    Kremer, K.3
  • 83
    • 42649140251 scopus 로고    scopus 로고
    • Long-Range Influence of Carbohydrates on the Solvation Dynamics of Water - Answers from Terahertz Absorption Measurements and Molecular Modeling Simulations
    • Heyden, M.; Bründermann, E.; Heugen, U.; Niehues, G.; Leitner, D. M.; Havenith, M. Long-Range Influence of Carbohydrates on the Solvation Dynamics of Water - Answers from Terahertz Absorption Measurements and Molecular Modeling Simulations J. Am. Chem. Soc. 2008, 130, 5773-5779
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5773-5779
    • Heyden, M.1    Bründermann, E.2    Heugen, U.3    Niehues, G.4    Leitner, D.M.5    Havenith, M.6
  • 84
    • 79957591665 scopus 로고    scopus 로고
    • Disaccharide Topology Induces Slowdown in Local Water Dynamics
    • Verde, A. V.; Campen, R. K. Disaccharide Topology Induces Slowdown in Local Water Dynamics J. Phys. Chem. B 2011, 115, 7069-7084
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7069-7084
    • Verde, A.V.1    Campen, R.K.2
  • 86
    • 79952088670 scopus 로고    scopus 로고
    • Linking Trehalose Self-Association with Binary Aqueous Solution Equation of State
    • Sapir, L.; Harries, D. Linking Trehalose Self-Association with Binary Aqueous Solution Equation of State J. Phys. Chem. B 2011, 115, 624-634
    • (2011) J. Phys. Chem. B , vol.115 , pp. 624-634
    • Sapir, L.1    Harries, D.2
  • 87
    • 20544474519 scopus 로고    scopus 로고
    • How Homogeneous Are the Trehalose, Maltose, and Sucrose Water Solutions? An Insight from Molecular Dynamics Simulations
    • Lerbret, A.; Bordat, P.; Affouard, F.; Descamps, M.; Migliardo, F. How Homogeneous Are the Trehalose, Maltose, and Sucrose Water Solutions? An Insight from Molecular Dynamics Simulations J. Phys. Chem. B 2005, 109, 11046-11057
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11046-11057
    • Lerbret, A.1    Bordat, P.2    Affouard, F.3    Descamps, M.4    Migliardo, F.5
  • 88
    • 33746772798 scopus 로고    scopus 로고
    • Preferential Hydration of DNA: The Magnitude and Distance Dependence of Alcohol and Polyol Interactions
    • Stanley, C.; Rau, D. C. Preferential Hydration of DNA: The Magnitude and Distance Dependence of Alcohol and Polyol Interactions Biophys. J. 2006, 91, 912-920
    • (2006) Biophys. J. , vol.91 , pp. 912-920
    • Stanley, C.1    Rau, D.C.2
  • 89
    • 67649515630 scopus 로고    scopus 로고
    • The Impact of Polyols on Water Structure in Solution: A Computational Study
    • Politi, R.; Sapir, L.; Harries, D. The Impact of Polyols on Water Structure in Solution: A Computational Study J. Phys. Chem. A 2009, 113, 7548-7555
    • (2009) J. Phys. Chem. A , vol.113 , pp. 7548-7555
    • Politi, R.1    Sapir, L.2    Harries, D.3
  • 90
    • 73349101519 scopus 로고    scopus 로고
    • Osmolyte-Induced Perturbations of Hydrogen Bonding between Hydration Layer Waters: Correlation with Protein Conformational Changes
    • Guo, F.; Friedman, J. M. Osmolyte-Induced Perturbations of Hydrogen Bonding between Hydration Layer Waters: Correlation with Protein Conformational Changes J. Phys. Chem. B 2009, 113, 16632-16642
    • (2009) J. Phys. Chem. B , vol.113 , pp. 16632-16642
    • Guo, F.1    Friedman, J.M.2
  • 91
    • 84856888342 scopus 로고    scopus 로고
    • Structural Examination of the Impact of Glycerol on Water Structure
    • Towey, J. J.; Dougan, L. Structural Examination of the Impact of Glycerol on Water Structure J. Phys. Chem. B 2012, 116, 1633-1641
    • (2012) J. Phys. Chem. B , vol.116 , pp. 1633-1641
    • Towey, J.J.1    Dougan, L.2
  • 92
    • 84870369242 scopus 로고    scopus 로고
    • Molecular Insight into the Hydrogen Bonding and Micro-Segregation of a Cryoprotectant Molecule
    • Towey, J.; Soper, A.; Dougan, L. Molecular Insight into the Hydrogen Bonding and Micro-Segregation of a Cryoprotectant Molecule J. Phys. Chem. B 2012, 116, 13898-13904
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13898-13904
    • Towey, J.1    Soper, A.2    Dougan, L.3
  • 94
    • 84903975517 scopus 로고    scopus 로고
    • A Statistical Theory of Cosolvent-Induced Coil-Globule Transitions in Dilute Polymer Solution
    • Budkov, Y. A.; Kolesnikov, A. L.; Georgi, N.; Kiselev, M. G. A Statistical Theory of Cosolvent-Induced Coil-Globule Transitions in Dilute Polymer Solution J. Chem. Phys. 2014, 141, 014902
    • (2014) J. Chem. Phys. , vol.141 , pp. 014902
    • Budkov, Y.A.1    Kolesnikov, A.L.2    Georgi, N.3    Kiselev, M.G.4
  • 95
    • 84862817183 scopus 로고    scopus 로고
    • Effect of Polyols on the Native Structure of A-Chymotrypsin: A Comparable Study
    • Kumar, A.; Attri, P.; Venkatesu, P. Effect of Polyols on the Native Structure of A-Chymotrypsin: A Comparable Study Thermochim. Acta 2012, 536, 55-62
    • (2012) Thermochim. Acta , vol.536 , pp. 55-62
    • Kumar, A.1    Attri, P.2    Venkatesu, P.3
  • 96
    • 84864479275 scopus 로고    scopus 로고
    • Effects of Macromolecular Crowding on the Structural Stability of Human A-Lactalbumin
    • Zhang, D.-L.; Wu, L.-J.; Chen, J.; Liang, Y. Effects of Macromolecular Crowding on the Structural Stability of Human A-Lactalbumin Acta Biochim. Biophys. Sin. 2012, 44, 703-711
    • (2012) Acta Biochim. Biophys. Sin. , vol.44 , pp. 703-711
    • Zhang, D.-L.1    Wu, L.-J.2    Chen, J.3    Liang, Y.4


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