메뉴 건너뛰기




Volumn 117, Issue 42, 2013, Pages 13291-13300

Structure and dynamics of urea/water mixtures investigated by vibrational spectroscopy and molecular dynamics simulation

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; MIXTURES; MOLECULAR DYNAMICS; MOLECULES; PROTEINS; THERMODYNAMICS; UREA; VIBRATIONAL SPECTROSCOPY; WATER ABSORPTION;

EID: 84886682236     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4037217     Document Type: Article
Times cited : (87)

References (96)
  • 1
    • 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
  • 2
    • 0032556206 scopus 로고    scopus 로고
    • Effect of the Protein Denaturants Urea and Guanidinium on Water Structure: A Structural and Thermodynamic Study
    • Vanzi, F.; Madan, B.; Sharp, K. Effect of the Protein Denaturants Urea and Guanidinium on Water Structure: A Structural and Thermodynamic Study J. Am. Chem. Soc. 1998, 120, 10748-10753
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10748-10753
    • Vanzi, F.1    Madan, B.2    Sharp, K.3
  • 3
    • 0036007095 scopus 로고    scopus 로고
    • Coupling of Solvent and Solute Dynamics-Molecular Dynamics Simulations of Aqueous Urea Solutions with Different Intramolecular Potentials
    • Kallies, B. Coupling of Solvent and Solute Dynamics-Molecular Dynamics Simulations of Aqueous Urea Solutions with Different Intramolecular Potentials Phys. Chem. Chem. Phys. 2002, 4, 86-95
    • (2002) Phys. Chem. Chem. Phys. , vol.4 , pp. 86-95
    • Kallies, B.1
  • 4
    • 2942555203 scopus 로고    scopus 로고
    • Importance of Excluded Volume on the Solvation of Urea in Water
    • Mountain, R. D.; Thirumalai, D. Importance of Excluded Volume on the Solvation of Urea in Water J. Phys. Chem. B 2004, 108, 6826-6831
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6826-6831
    • Mountain, R.D.1    Thirumalai, D.2
  • 5
    • 3142655877 scopus 로고    scopus 로고
    • Application of the Local-Bulk Partitioning and Competitive Binding Models to Interpret Preferential Interactions of Glycine Betaine and Urea with Protein Surface
    • Felitsky, D. J.; Record, M. T. Application of the Local-Bulk Partitioning and Competitive Binding Models to Interpret Preferential Interactions of Glycine Betaine and Urea with Protein Surface Biochemistry 2004, 43, 9276-9288
    • (2004) Biochemistry , vol.43 , pp. 9276-9288
    • Felitsky, D.J.1    Record, M.T.2
  • 6
    • 36549078761 scopus 로고    scopus 로고
    • Molecular Basis of the Apparent Near Ideality of Urea Solutions
    • Kokubo, H.; Roesgen, J.; Bolen, D. W.; Pettitt, B. M. Molecular Basis of the Apparent Near Ideality of Urea Solutions Biophys. J. 2007, 93, 3392-3407
    • (2007) Biophys. J. , vol.93 , pp. 3392-3407
    • Kokubo, H.1    Roesgen, J.2    Bolen, D.W.3    Pettitt, B.M.4
  • 7
    • 0034187378 scopus 로고    scopus 로고
    • NMR Studies on Dynamic Behavior of Water Molecule in Aqueous Denaturant Solutions at 25 C: Effects of Guanidine Hydrochloride, Urea and Alkylated Ureas
    • Shimizu, A.; Fumino, K.; Yukiyasu, K.; Taniguchi, Y. NMR Studies on Dynamic Behavior of Water Molecule in Aqueous Denaturant Solutions at 25 C: Effects of Guanidine Hydrochloride, Urea and Alkylated Ureas J. Mol. Liq. 2000, 85, 269-278
    • (2000) J. Mol. Liq. , vol.85 , pp. 269-278
    • Shimizu, A.1    Fumino, K.2    Yukiyasu, K.3    Taniguchi, Y.4
  • 8
    • 84869176141 scopus 로고    scopus 로고
    • Urea, a Structure Breaker? Answers from THz Absorption Spectroscopy
    • Funkner, S.; Havenith, M.; Schwaab, G. Urea, a Structure Breaker? Answers from THz Absorption Spectroscopy J. Phys. Chem. B 2012, 116, 13374-13380
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13374-13380
    • Funkner, S.1    Havenith, M.2    Schwaab, G.3
  • 9
    • 1242319518 scopus 로고    scopus 로고
    • Impact of Protein Denaturants and Stabilizers on Water Structure
    • Batchelor, J. D.; Olteanu, A.; Tripathy, A.; Pielak, G. J. Impact of Protein Denaturants and Stabilizers on Water Structure J. Am. Chem. Soc. 2004, 126, 1958-1961
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1958-1961
    • Batchelor, J.D.1    Olteanu, A.2    Tripathy, A.3    Pielak, G.J.4
  • 10
    • 33847036687 scopus 로고    scopus 로고
    • Liquid Structure of the Urea-Water System Studied by Dielectric Spectroscopy
    • Hayashi, Y.; Katsumoto, Y.; Omori, S.; Kishii, N.; Yasuda, A. Liquid Structure of the Urea-Water System Studied by Dielectric Spectroscopy J. Phys. Chem. B 2007, 111, 1076-1080
    • (2007) J. Phys. Chem. B , vol.111 , pp. 1076-1080
    • Hayashi, Y.1    Katsumoto, Y.2    Omori, S.3    Kishii, N.4    Yasuda, A.5
  • 11
    • 0035104083 scopus 로고    scopus 로고
    • Water Structure Changes Induced by Hydrophobic and Polar Solutes Revealed by Simulations and Infrared Spectroscopy
    • Sharp, K. A.; Madan, B.; Manas, E.; Vanderkooi, J. M. Water Structure Changes Induced by Hydrophobic and Polar Solutes Revealed by Simulations and Infrared Spectroscopy J. Chem. Phys. 2001, 114, 1791-1796
    • (2001) J. Chem. Phys. , vol.114 , pp. 1791-1796
    • Sharp, K.A.1    Madan, B.2    Manas, E.3    Vanderkooi, J.M.4
  • 12
    • 77249111728 scopus 로고    scopus 로고
    • Water in the Half Shell: Structure of Water, Focusing on Angular Structure and Solvation
    • Sharp, K. A.; Vanderkooi, J. M. Water in the Half Shell: Structure of Water, Focusing on Angular Structure and Solvation Acc. Chem. Res. 2010, 43, 231-239
    • (2010) Acc. Chem. Res. , vol.43 , pp. 231-239
    • Sharp, K.A.1    Vanderkooi, J.M.2
  • 13
    • 77956249460 scopus 로고    scopus 로고
    • The Hydrogen Bond Network Structure within the Hydration Shell around Simple Osmolytes: Urea, Tetramethylurea, and Trimethylamine- N -oxide, Investigated Using Both a Fixed Charge and a Polarizable Water Model
    • Kuffel, A.; Zielkiewicz, J. The Hydrogen Bond Network Structure within the Hydration Shell around Simple Osmolytes: Urea, Tetramethylurea, and Trimethylamine- N -oxide, Investigated Using Both a Fixed Charge and a Polarizable Water Model J. Chem. Phys. 2010, 133, 035102/1-035102/8
    • (2010) J. Chem. Phys. , vol.133 , pp. 0351021-0351028
    • Kuffel, A.1    Zielkiewicz, J.2
  • 14
    • 75649108542 scopus 로고    scopus 로고
    • Effects of Urea, Tetramethyl Urea, and Trimethylamine N -Oxide on Aqueous Solution Structure and Solvation of Protein Backbones: A Molecular Dynamics Simulation Study
    • Wei, H.; Fan, Y.; Gao, Y. Q. Effects of Urea, Tetramethyl Urea, and Trimethylamine N -Oxide on Aqueous Solution Structure and Solvation of Protein Backbones: A Molecular Dynamics Simulation Study J. Phys. Chem. B 2010, 114, 557-568
    • (2010) J. Phys. Chem. B , vol.114 , pp. 557-568
    • Wei, H.1    Fan, Y.2    Gao, Y.Q.3
  • 15
    • 0141560450 scopus 로고    scopus 로고
    • Impact of Urea on Water Structure: A Clue to Its Properties as a Denaturant?
    • Soper, A. K.; Castner, E. W.; Luzar, A. Impact of Urea on Water Structure: A Clue to Its Properties as a Denaturant? Biophys. Chem. 2003, 105, 649-666
    • (2003) Biophys. Chem. , vol.105 , pp. 649-666
    • Soper, A.K.1    Castner, E.W.2    Luzar, A.3
  • 16
    • 36849117971 scopus 로고
    • Free Volume and Entropy in Condensed Systems: III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes
    • Frank, H. S.; Evans, M. W. Free Volume and Entropy in Condensed Systems: III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes J. Chem. Phys. 1945, 13, 507-532
    • (1945) J. Chem. Phys. , vol.13 , pp. 507-532
    • Frank, H.S.1    Evans, M.W.2
  • 17
    • 33749541104 scopus 로고
    • Structural Approach to the Solvent Power of Water for Hydrocarbons; Urea as a Structure Breaker
    • Frank, H. S.; Franks, F. Structural Approach to the Solvent Power of Water for Hydrocarbons; Urea as a Structure Breaker J. Chem. Phys. 1968, 48, 4746-4757
    • (1968) J. Chem. Phys. , vol.48 , pp. 4746-4757
    • Frank, H.S.1    Franks, F.2
  • 19
    • 0032554078 scopus 로고    scopus 로고
    • Hydrophobic Interactions in Aqueous Urea Solutions with Implications for the Mechanism of Protein Denaturation
    • Wallqvist, A.; Covell, D. G.; Thirumalai, D. Hydrophobic Interactions in Aqueous Urea Solutions with Implications for the Mechanism of Protein Denaturation J. Am. Chem. Soc. 1998, 120, 427-428
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 427-428
    • Wallqvist, A.1    Covell, D.G.2    Thirumalai, D.3
  • 20
    • 0037465426 scopus 로고    scopus 로고
    • Thermal and Urea-Induced Unfolding of the Marginally Stable Lac Repressor DNA-Binding Domain: A Model System for Analysis of Solute Effects on Protein Processes
    • Felitsky, D. J.; Record, M. T. Thermal and Urea-Induced Unfolding of the Marginally Stable Lac Repressor DNA-Binding Domain: A Model System for Analysis of Solute Effects on Protein Processes Biochemistry 2003, 42, 2202-2217
    • (2003) Biochemistry , vol.42 , pp. 2202-2217
    • Felitsky, D.J.1    Record, M.T.2
  • 21
    • 0037343333 scopus 로고    scopus 로고
    • The Dominant Interaction between Peptide and Urea is Electrostatic in Nature: A Molecular Dynamics Study
    • Tobi, D.; Elber, R.; Thirumalai, D. The Dominant Interaction Between Peptide and Urea is Electrostatic in Nature: A Molecular Dynamics Study Biopolymers 2003, 68, 359-369
    • (2003) Biopolymers , vol.68 , pp. 359-369
    • Tobi, D.1    Elber, R.2    Thirumalai, D.3
  • 23
    • 34250869055 scopus 로고    scopus 로고
    • Interactions between Hydrophobic and Ionic Solutes in Aqueous Guanidinium Chloride and Urea Solutions: Lessons for Protein Denaturation Mechanism
    • O'Brien, E. P.; Dima, R. I.; Brooks, B.; Thirumalai, D. Interactions between Hydrophobic and Ionic Solutes in Aqueous Guanidinium Chloride and Urea Solutions: Lessons for Protein Denaturation Mechanism J. Am. Chem. Soc. 2007, 129, 7346-7353
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 7346-7353
    • O'Brien, E.P.1    Dima, R.I.2    Brooks, B.3    Thirumalai, D.4
  • 24
    • 47749106779 scopus 로고    scopus 로고
    • Atomistic Mechanism of Protein Denaturation by Urea
    • Das, A.; Mukhopadhyay, C. Atomistic Mechanism of Protein Denaturation by Urea J. Phys. Chem. B 2008, 112, 7903-7908
    • (2008) J. Phys. Chem. B , vol.112 , pp. 7903-7908
    • Das, A.1    Mukhopadhyay, C.2
  • 25
    • 55949131241 scopus 로고    scopus 로고
    • Urea Denaturation by Stronger Dispersion Interactions with Proteins than Water Implies a 2-Stage Unfolding
    • Hua, L.; Zhou, R.; Thirumalai, D.; Berne, B. J. Urea Denaturation by Stronger Dispersion Interactions with Proteins than Water Implies a 2-Stage Unfolding Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 16928-16933
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.J.4
  • 26
    • 67650363919 scopus 로고    scopus 로고
    • Urea Impedes the Hydrophobic Collapse of Partially Unfolded Proteins
    • Stumpe, M. C.; Grubmüller, H. Urea Impedes the Hydrophobic Collapse of Partially Unfolded Proteins Biophys. J. 2009, 96, 3744-3752
    • (2009) Biophys. J. , vol.96 , pp. 3744-3752
    • Stumpe, M.C.1    Grubmüller, H.2
  • 27
    • 63149153986 scopus 로고    scopus 로고
    • Urea's Action on Hydrophobic Interactions
    • Zangi, R.; Zhou, R.; Berne, B. J. Urea's Action on Hydrophobic Interactions J. Am. Chem. Soc. 2009, 131, 1535-1541
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.2    Berne, B.J.3
  • 28
    • 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
  • 29
    • 77749259034 scopus 로고    scopus 로고
    • Preferential Interactions between Small Solutes and the Protein Backbone: A Computational Analysis
    • Ma, L.; Pegram, L.; Record, M. T.; Cui, Q. Preferential Interactions between Small Solutes and the Protein Backbone: A Computational Analysis Biochemistry 2010, 49, 1954-1962
    • (2010) Biochemistry , vol.49 , pp. 1954-1962
    • Ma, L.1    Pegram, L.2    Record, M.T.3    Cui, Q.4
  • 30
    • 80054991841 scopus 로고    scopus 로고
    • Effect of Urea on the β -Hairpin Conformational Ensemble and Protein Denaturation Mechanism
    • Berteotti, A.; Barducci, A.; Parrinello, M. Effect of Urea on the β -Hairpin Conformational Ensemble and Protein Denaturation Mechanism J. Am. Chem. Soc. 2011, 133, 17200-17206
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17200-17206
    • Berteotti, A.1    Barducci, A.2    Parrinello, M.3
  • 31
    • 80054717093 scopus 로고    scopus 로고
    • Quantifying Why Urea Is a Protein Denaturant, whereas Glycine Betaine Is a Protein Stabilizer
    • Guinn, E. J.; Pegram, L. M.; Capp, M. W.; Pollock, M. N.; Record, M. T. Quantifying Why Urea Is a Protein Denaturant, Whereas Glycine Betaine Is a Protein Stabilizer Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 16932-16937
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16932-16937
    • Guinn, E.J.1    Pegram, L.M.2    Capp, M.W.3    Pollock, M.N.4    Record, M.T.5
  • 32
    • 79952860125 scopus 로고    scopus 로고
    • Comment on Urea-Mediated Protein Denaturation: A Consensus View
    • Zhou, R.; Li, J.; Hua, L.; Yang, Z.; Berne, B. J. Comment on Urea-Mediated Protein Denaturation: A Consensus View J. Phys. Chem. B 2011, 115, 1323-1326
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1323-1326
    • Zhou, R.1    Li, J.2    Hua, L.3    Yang, Z.4    Berne, B.J.5
  • 33
    • 79953759344 scopus 로고    scopus 로고
    • Role of Solvation Effects in Protein Denaturation: From Thermodynamics to Single Molecules and Back
    • England, J. L.; Haran, G. Role of Solvation Effects in Protein Denaturation: From Thermodynamics to Single Molecules and Back Annu. Rev. Phys. Chem. 2011, 62, 257-277
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 257-277
    • England, J.L.1    Haran, G.2
  • 34
    • 0016699207 scopus 로고
    • Macromolecular Binding
    • Schellman, J. A. Macromolecular Binding Biopolymers 1975, 14, 999-1018
    • (1975) Biopolymers , vol.14 , pp. 999-1018
    • Schellman, J.A.1
  • 35
    • 0023322630 scopus 로고
    • Selective Binding and Solvent Denaturation
    • Schellman, J. A. Selective Binding and Solvent Denaturation Biopolymers 1987, 26, 549-559
    • (1987) Biopolymers , vol.26 , pp. 549-559
    • Schellman, J.A.1
  • 36
    • 0000784156 scopus 로고
    • A Model for the Partial Reversal of Hydrophobic Hydration by Addition of a Urea-like Cosolvent
    • Muller, N. A Model for the Partial Reversal of Hydrophobic Hydration by Addition of a Urea-like Cosolvent J. Phys. Chem. 1990, 94, 3856-3859
    • (1990) J. Phys. Chem. , vol.94 , pp. 3856-3859
    • Muller, N.1
  • 37
    • 0025030410 scopus 로고
    • A Simple Model for Solvation in Mixed Solvents: Applications to the Stabilization and Destabilization of Macromolecular Structures
    • Schellman, J. A. A Simple Model for Solvation in Mixed Solvents: Applications to the Stabilization and Destabilization of Macromolecular Structures Biophys. Chem. 1990, 37, 121-140
    • (1990) Biophys. Chem. , vol.37 , pp. 121-140
    • Schellman, J.A.1
  • 38
    • 80053486881 scopus 로고    scopus 로고
    • How Does Trimethylamine N -Oxide Counteract the Denaturing Activity of Urea?
    • Graziano, G. How Does Trimethylamine N -Oxide Counteract the Denaturing Activity of Urea? Phys. Chem. Chem. Phys. 2011, 13, 17689-17695
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 17689-17695
    • Graziano, G.1
  • 39
    • 84864754081 scopus 로고    scopus 로고
    • Coherent Microscopic Picture for Urea-Induced Denaturation of Proteins
    • Yang, Z.; Xiu, P.; Shi, B.; Hua, L.; Zhou, R. Coherent Microscopic Picture for Urea-Induced Denaturation of Proteins J. Phys. Chem. B 2012, 116, 8856-8862
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8856-8862
    • Yang, Z.1    Xiu, P.2    Shi, B.3    Hua, L.4    Zhou, R.5
  • 40
    • 84867650799 scopus 로고    scopus 로고
    • Solute's Perspective on How Trimethylamine Oxide, Urea, and Guanidine Hydrochloride Affect Water's Hydrogen Bonding Ability
    • Pazos, I. M.; Gai, F. Solute's Perspective on How Trimethylamine Oxide, Urea, and Guanidine Hydrochloride Affect Water's Hydrogen Bonding Ability J. Phys. Chem. B 2012, 116, 12473-12478
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12473-12478
    • Pazos, I.M.1    Gai, F.2
  • 41
    • 79953858621 scopus 로고    scopus 로고
    • Backbone and Side-Chain Contributions in Protein Denaturation by Urea
    • Canchi, D. R.; García, A. E. Backbone and Side-Chain Contributions in Protein Denaturation by Urea Biophys. J. 2011, 100, 1526-1533
    • (2011) Biophys. J. , vol.100 , pp. 1526-1533
    • Canchi, D.R.1    García, A.E.2
  • 42
    • 33845488514 scopus 로고    scopus 로고
    • Effect of Urea on the Structural Dynamics of Water
    • Rezus, Y. L. A.; Bakker, H. J. Effect of Urea on the Structural Dynamics of Water Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18417-18420
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18417-18420
    • Rezus, Y.L.A.1    Bakker, H.J.2
  • 43
    • 0001670437 scopus 로고
    • The Densities of Aqueous Solutions of Urea at 25 and 30 and the Apparent Molal Volume of Urea
    • Gucker, F. T.; Cage, F. W.; Moser, C. E. The Densities of Aqueous Solutions of Urea at 25 and 30 and the Apparent Molal Volume of Urea J. Am. Chem. Soc. 1938, 60, 2582-2588
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 2582-2588
    • Gucker, F.T.1    Cage, F.W.2    Moser, C.E.3
  • 44
    • 0038370011 scopus 로고    scopus 로고
    • The Molecular Basis for the Chemical Denaturation of Proteins by Urea
    • Bennion, B.; Daggett, V. The Molecular Basis for the Chemical Denaturation of Proteins by Urea Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 5142-5147
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5142-5147
    • Bennion, B.1    Daggett, V.2
  • 46
    • 0037075401 scopus 로고    scopus 로고
    • Molecular Association in Solution: A Kirkwood-Buff Analysis of Sodium Chloride, Ammonium Sulfate, Guanidinium Chloride, Urea, and 2,2,2- Trifluoroethanol in Water
    • Chitra, R.; Smith, P. E. Molecular Association in Solution: A Kirkwood-Buff Analysis of Sodium Chloride, Ammonium Sulfate, Guanidinium Chloride, Urea, and 2,2,2-Trifluoroethanol in Water J. Phys. Chem. B 2002, 106, 1491-1500
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1491-1500
    • Chitra, R.1    Smith, P.E.2
  • 47
    • 34250723399 scopus 로고    scopus 로고
    • Aqueous Urea Solutions: Structure, Energetics, and Urea Aggregation
    • Stumpe, M. C.; Grubmüller, H. Aqueous Urea Solutions: Structure, Energetics, and Urea Aggregation J. Phys. Chem. B 2007, 111, 6220-6228
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6220-6228
    • Stumpe, M.C.1    Grubmüller, H.2
  • 48
    • 23244452958 scopus 로고    scopus 로고
    • Effect of Urea on Peptide Conformation in Water: Molecular Dynamics and Experimental Characterization
    • Caballero-Herrera, A.; Nordstrand, K.; Berndt, K. D.; Nilsson, L. Effect of Urea on Peptide Conformation in Water: Molecular Dynamics and Experimental Characterization Biophys. J. 2005, 89, 842-857
    • (2005) Biophys. J. , vol.89 , pp. 842-857
    • Caballero-Herrera, A.1    Nordstrand, K.2    Berndt, K.D.3    Nilsson, L.4
  • 49
    • 70349289438 scopus 로고    scopus 로고
    • Urea-Mediated Protein Denaturation: A Consensus View
    • Das, A.; Mukhopadhyay, C. Urea-Mediated Protein Denaturation: A Consensus View J. Phys. Chem. B 2009, 113, 12816-12824
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12816-12824
    • Das, A.1    Mukhopadhyay, C.2
  • 50
    • 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
  • 51
    • 77951669557 scopus 로고    scopus 로고
    • Chemistry of Hofmeister Anions and Osmolytes
    • Zhang, Y.; Cremer, P. S. Chemistry of Hofmeister Anions and Osmolytes Annu. Rev. Phys. Chem. 2010, 61, 63-83
    • (2010) Annu. Rev. Phys. Chem. , vol.61 , pp. 63-83
    • Zhang, Y.1    Cremer, P.S.2
  • 53
    • 0000619798 scopus 로고
    • Raman Spectroscopic Investigation of the Dynamics of Urea-Water Complexes
    • Hoccart, X.; Turrell, G. Raman Spectroscopic Investigation of the Dynamics of Urea-Water Complexes J. Chem. Phys. 1993, 99, 8498-8503
    • (1993) J. Chem. Phys. , vol.99 , pp. 8498-8503
    • Hoccart, X.1    Turrell, G.2
  • 54
    • 77949638476 scopus 로고    scopus 로고
    • Vibrational Spectroscopy as a Probe of Structure and Dynamics in Liquid Water
    • Bakker, H.; Skinner, J. L. Vibrational Spectroscopy as a Probe of Structure and Dynamics in Liquid Water Chem. Rev. 2010, 110, 1498-1517
    • (2010) Chem. Rev. , vol.110 , pp. 1498-1517
    • Bakker, H.1    Skinner, J.L.2
  • 55
    • 0037179644 scopus 로고    scopus 로고
    • Urea and Urea-Water Solutions - An Infrared Study
    • Grdadolnik, J.; Maréchal, Y. Urea and Urea-Water Solutions-An Infrared Study J. Mol. Struct. 2002, 615, 177-189
    • (2002) J. Mol. Struct. , vol.615 , pp. 177-189
    • Grdadolnik, J.1    Maréchal, Y.2
  • 56
    • 0021754413 scopus 로고
    • Molecular Dynamics Study of Solvation in Urea-Water Solution
    • Kuharski, R. A.; Rossky, P. J. Molecular Dynamics Study of Solvation in Urea-Water Solution J. Am. Chem. Soc. 1984, 106, 5786-5793
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 5786-5793
    • Kuharski, R.A.1    Rossky, P.J.2
  • 57
    • 0033720021 scopus 로고    scopus 로고
    • A Molecular Dynamics Study of the Urea/Water Mixture
    • Idrissi, A.; Sokolić, F.; Perera, A. A Molecular Dynamics Study of the Urea/Water Mixture J. Chem. Phys. 2000, 112, 9479-9488
    • (2000) J. Chem. Phys. , vol.112 , pp. 9479-9488
    • Idrissi, A.1    Sokolić, F.2    Perera, A.3
  • 58
    • 0000973069 scopus 로고
    • Molecular Dynamics Simulations of 2 m Aqueous Urea Solutions
    • Åstrand, P.-O.; Wallqvist, A.; Karlström, G. Molecular Dynamics Simulations of 2 m Aqueous Urea Solutions J. Phys. Chem. 1994, 98, 8224-8233
    • (1994) J. Phys. Chem. , vol.98 , pp. 8224-8233
    • Åstrand, P.-O.1    Wallqvist, A.2    Karlström, G.3
  • 59
    • 0037154353 scopus 로고    scopus 로고
    • Concentrated Aqueous Urea Solutions: A Molecular Dynamics Study of Different Models
    • Sokolić, F.; Idrissi, A.; Perera, A. Concentrated Aqueous Urea Solutions: A Molecular Dynamics Study of Different Models J. Chem. Phys. 2002, 116, 1636-1646
    • (2002) J. Chem. Phys. , vol.116 , pp. 1636-1646
    • Sokolić, F.1    Idrissi, A.2    Perera, A.3
  • 60
    • 0037997632 scopus 로고    scopus 로고
    • A Kirkwood-Buff Derived Force Field for Mixtures of Urea and Water
    • Weerasinghe, S.; Smith, P. E. A Kirkwood-Buff Derived Force Field for Mixtures of Urea and Water J. Phys. Chem. B 2003, 107, 3891-3898
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3891-3898
    • Weerasinghe, S.1    Smith, P.E.2
  • 61
    • 9144247835 scopus 로고    scopus 로고
    • A Theoretical Investigation of the Shape and Hydration Properties of Aqueous Urea: Evidence for Nonplanar Urea Geometry
    • Ishida, T.; Rossky, P. J. A Theoretical Investigation of the Shape and Hydration Properties of Aqueous Urea: Evidence for Nonplanar Urea Geometry J. Phys. Chem. B 2004, 108, 17583-17590
    • (2004) J. Phys. Chem. B , vol.108 , pp. 17583-17590
    • Ishida, T.1    Rossky, P.J.2
  • 62
    • 0742286773 scopus 로고    scopus 로고
    • Computer Simulation of Urea-Water Mixtures: A Test of Force Field Parameters for Use in Biomolecular Simulation
    • Smith, L. J.; Berendsen, H. J. C.; van Gunsteren, W. F. Computer Simulation of Urea-Water Mixtures: A Test of Force Field Parameters for Use in Biomolecular Simulation J. Phys. Chem. B 2004, 108, 1065-1071
    • (2004) J. Phys. Chem. B , vol.108 , pp. 1065-1071
    • Smith, L.J.1    Berendsen, H.J.C.2    Van Gunsteren, W.F.3
  • 63
    • 34249806047 scopus 로고    scopus 로고
    • Preferential Solvation in Urea Solutions at Different Concentrations: Properties from Simulation Studies
    • Kokubo, H.; Pettitt, B. M. Preferential Solvation in Urea Solutions at Different Concentrations: Properties from Simulation Studies J. Phys. Chem. B 2007, 111, 5233-5242
    • (2007) J. Phys. Chem. B , vol.111 , pp. 5233-5242
    • Kokubo, H.1    Pettitt, B.M.2
  • 64
    • 35349029315 scopus 로고    scopus 로고
    • Planar or Nonplanar: What is the Structure of Urea in Aqueous Solution?
    • Hermida-Ramón, J. M.; Öhrn, A.; Karlström, G. Planar or Nonplanar: What is the Structure of Urea in Aqueous Solution? J. Phys. Chem. B 2007, 111, 11511-11515
    • (2007) J. Phys. Chem. B , vol.111 , pp. 11511-11515
    • Hermida-Ramón, J.M.1    Öhrn, A.2    Karlström, G.3
  • 65
    • 55349095778 scopus 로고    scopus 로고
    • Hydration Free Energy Difference of Acetone, Acetamide, and Urea
    • Jedlovszky, P.; Idrissi, A. Hydration Free Energy Difference of Acetone, Acetamide, and Urea J. Chem. Phys. 2008, 129, 164501/1-164501/7
    • (2008) J. Chem. Phys. , vol.129 , pp. 1645011-1645017
    • Jedlovszky, P.1    Idrissi, A.2
  • 66
    • 55349087236 scopus 로고    scopus 로고
    • Self-Association of Urea in Aqueous Solutions: A Voronoi Polyhedron Analysis Study
    • Idrissi, A.; Damay, P.; Yukichi, K.; Jedlovszky, P. Self-Association of Urea in Aqueous Solutions: A Voronoi Polyhedron Analysis Study J. Chem. Phys. 2008, 129, 164512/1-164512/9
    • (2008) J. Chem. Phys. , vol.129 , pp. 1645121-1645129
    • Idrissi, A.1    Damay, P.2    Yukichi, K.3    Jedlovszky, P.4
  • 68
    • 45149121970 scopus 로고    scopus 로고
    • IR and Raman Spectra of Liquid Water: Theory and Interpretation
    • Auer, B. M.; Skinner, J. L. IR and Raman Spectra of Liquid Water: Theory and Interpretation J. Chem. Phys. 2008, 128, 224511/1-224511/12
    • (2008) J. Chem. Phys. , vol.128 , pp. 2245111-22451112
    • Auer, B.M.1    Skinner, J.L.2
  • 69
    • 77955366246 scopus 로고    scopus 로고
    • On the Calculation of Rotational Anisotropy Decay, as Measured by Ultrafast Polarization-Resolved Vibrational Pump-Probe Experiments
    • Lin, Y.-S.; Pieniazek, P. A.; Yang, M.; Skinner, J. L. On the Calculation of Rotational Anisotropy Decay, as Measured by Ultrafast Polarization-Resolved Vibrational Pump-Probe Experiments J. Chem. Phys. 2010, 132, 174505/1-174505/8
    • (2010) J. Chem. Phys. , vol.132 , pp. 1745051-1745058
    • Lin, Y.-S.1    Pieniazek, P.A.2    Yang, M.3    Skinner, J.L.4
  • 70
    • 80555129396 scopus 로고    scopus 로고
    • Vibrational Energy Transfer and Anisotropy Decay in Liquid Water: Is the Förster Model Valid?
    • Yang, M.; Li, F.; Skinner, J. L. Vibrational Energy Transfer and Anisotropy Decay in Liquid Water: Is the Förster Model Valid? J. Chem. Phys. 2011, 135, 164505/1-164505/10
    • (2011) J. Chem. Phys. , vol.135 , pp. 1645051-16450510
    • Yang, M.1    Li, F.2    Skinner, J.L.3
  • 71
    • 85005481062 scopus 로고
    • Urea: Potential Function, log P, and Free Energy of Hydration
    • Duffy, E. M.; Severance, D. L.; Jorgensen, W. L. Urea: Potential Function, log P, and Free Energy of Hydration Israel J. Chem. 1993, 33, 323-330
    • (1993) Israel J. Chem. , vol.33 , pp. 323-330
    • Duffy, E.M.1    Severance, D.L.2    Jorgensen, W.L.3
  • 73
    • 79953059618 scopus 로고    scopus 로고
    • Urea-Induced Drying of Hydrophobic Nanotubes: Comparison of Different Urea Models
    • Xiu, P.; Yang, Z.; Zhou, B.; Das, P.; Fang, H.; Zhou, R. Urea-Induced Drying of Hydrophobic Nanotubes: Comparison of Different Urea Models J. Phys. Chem. B 2011, 115, 2988-2994
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2988-2994
    • Xiu, P.1    Yang, Z.2    Zhou, B.3    Das, P.4    Fang, H.5    Zhou, R.6
  • 74
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the Helix-Coil Transition via All-Atom Equilibrium Ensemble Simulations
    • Sorin, E. J.; Pande, V. S. Exploring the Helix-Coil Transition via All-Atom Equilibrium Ensemble Simulations Biophys. J. 2005, 88, 2472-2493
    • (2005) Biophys. J. , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 80
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 81
    • 35748960831 scopus 로고    scopus 로고
    • Are Water Simulation Models Consistent with Steady-State and Ultrafast Vibrational Spectroscopy Experiments?
    • Schmidt, J. R.; Roberts, S. T.; Loparo, J. J.; Tokmakoff, A.; Fayer, M. D.; Skinner, J. L. Are Water Simulation Models Consistent with Steady-State and Ultrafast Vibrational Spectroscopy Experiments? Chem. Phys. 2007, 341, 143-157
    • (2007) Chem. Phys. , vol.341 , pp. 143-157
    • Schmidt, J.R.1    Roberts, S.T.2    Loparo, J.J.3    Tokmakoff, A.4    Fayer, M.D.5    Skinner, J.L.6
  • 82
    • 70350439546 scopus 로고    scopus 로고
    • Water Structure, Dynamics, and Vibrational Spectroscopy in Sodium Bromide Solutions
    • Lin, Y.-S.; Auer, B. M.; Skinner, J. L. Water Structure, Dynamics, and Vibrational Spectroscopy in Sodium Bromide Solutions J. Chem. Phys. 2009, 131, 144511/1-144511/13
    • (2009) J. Chem. Phys. , vol.131 , pp. 1445111-14451113
    • Lin, Y.-S.1    Auer, B.M.2    Skinner, J.L.3
  • 83
    • 80555139750 scopus 로고    scopus 로고
    • Vibrational Spectroscopy of Water in Hydrated Lipid Multi-Bilayers. II. Two-Dimensional Infrared and Peak Shift Observables within Different Theoretical Approximations
    • Gruenbaum, S. M.; Pieniazek, P. A.; Skinner, J. L. Vibrational Spectroscopy of Water in Hydrated Lipid Multi-Bilayers. II. Two-Dimensional Infrared and Peak Shift Observables within Different Theoretical Approximations J. Chem. Phys. 2011, 135, 164506/1-164506/12
    • (2011) J. Chem. Phys. , vol.135 , pp. 1645061-16450612
    • Gruenbaum, S.M.1    Pieniazek, P.A.2    Skinner, J.L.3
  • 84
    • 80052056551 scopus 로고    scopus 로고
    • Vibrational Spectroscopy of Water in Hydrated Lipid Multi-Bilayers. I. Infrared Spectra and Ultrafast Pump-Probe Observables
    • Gruenbaum, S. M.; Skinner, J. L. Vibrational Spectroscopy of Water in Hydrated Lipid Multi-Bilayers. I. Infrared Spectra and Ultrafast Pump-Probe Observables J. Chem. Phys. 2011, 135, 075101/1-075101/13
    • (2011) J. Chem. Phys. , vol.135 , pp. 0751011-07510113
    • Gruenbaum, S.M.1    Skinner, J.L.2
  • 86
    • 79953275033 scopus 로고    scopus 로고
    • Development and Validation of Transferable Amide i Vibrational Frequency Maps for Peptides
    • Wang, L.; Middleton, C. T.; Zanni, M. T.; Skinner, J. L. Development and Validation of Transferable Amide I Vibrational Frequency Maps for Peptides J. Phys. Chem. B 2011, 115, 3713-3724
    • (2011) J. Phys. Chem. B , vol.115 , pp. 3713-3724
    • Wang, L.1    Middleton, C.T.2    Zanni, M.T.3    Skinner, J.L.4
  • 87
    • 79960043610 scopus 로고    scopus 로고
    • Surface of Liquid Water: Three-Body Interactions and Vibrational Sum-Frequency Spectrum
    • Pieniazek, P. A.; Tainter, C. J.; Skinner, J. L. Surface of Liquid Water: Three-Body Interactions and Vibrational Sum-Frequency Spectrum J. Am. Chem. Soc. 2011, 133, 10360-10363
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10360-10363
    • Pieniazek, P.A.1    Tainter, C.J.2    Skinner, J.L.3
  • 88
    • 34548099699 scopus 로고    scopus 로고
    • Pronounced Non-Condon Effects in the Ultrafast Infrared Spectroscopy of Water
    • Schmidt, J. R.; Corcelli, S. A.; Skinner, J. L. Pronounced Non-Condon Effects in the Ultrafast Infrared Spectroscopy of Water J. Chem. Phys. 2005, 123, 044513/1-044513/13
    • (2005) J. Chem. Phys. , vol.123 , pp. 0445131-04451313
    • Schmidt, J.R.1    Corcelli, S.A.2    Skinner, J.L.3
  • 89
    • 79961051077 scopus 로고    scopus 로고
    • Interpretation of the Water Surface Vibrational Sum-Frequency Spectrum
    • Pieniazek, P. A.; Tainter, C. J.; Skinner, J. L. Interpretation of the Water Surface Vibrational Sum-Frequency Spectrum J. Chem. Phys. 2011, 135, 044701/1-044701/12
    • (2011) J. Chem. Phys. , vol.135 , pp. 0447011-04470112
    • Pieniazek, P.A.1    Tainter, C.J.2    Skinner, J.L.3
  • 90
    • 25444459902 scopus 로고    scopus 로고
    • On the Orientation Relaxation of HOD in Liquid Water
    • Rezus, Y. L. A.; Bakker, H. J. On the Orientation Relaxation of HOD in Liquid Water J. Chem. Phys. 2005, 123, 114502/1-114502/7
    • (2005) J. Chem. Phys. , vol.123 , pp. 1145021-1145027
    • Rezus, Y.L.A.1    Bakker, H.J.2
  • 91
    • 33646450410 scopus 로고    scopus 로고
    • Testing the Core/Shell Model of Nanoconfined Water in Reverse Micelles Using Linear and Nonlinear IR Spectroscopy
    • Piletic, I. R.; Moilanen, D. E.; Spry, D. B.; Levinger, N. E.; Fayer, M. D. Testing the Core/Shell Model of Nanoconfined Water in Reverse Micelles Using Linear and Nonlinear IR Spectroscopy J. Phys. Chem. A 2006, 110, 4985-4999
    • (2006) J. Phys. Chem. A , vol.110 , pp. 4985-4999
    • Piletic, I.R.1    Moilanen, D.E.2    Spry, D.B.3    Levinger, N.E.4    Fayer, M.D.5
  • 92
    • 65249157127 scopus 로고    scopus 로고
    • Why Water Reorientation Slows without Iceberg Formation around Hydrophobic Solutes
    • Laage, D.; Stirnemann, G.; Hynes, J. T. Why Water Reorientation Slows without Iceberg Formation around Hydrophobic Solutes J. Phys. Chem. B 2009, 113, 2428-2435
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2428-2435
    • Laage, D.1    Stirnemann, G.2    Hynes, J.T.3
  • 94
    • 0037254829 scopus 로고    scopus 로고
    • 2O. III. Spectral Diffusion, and Hydrogen-Bonding and Rotational Dynamics
    • 2O. III. Spectral Diffusion, and Hydrogen-Bonding and Rotational Dynamics J. Chem. Phys. 2003, 118, 264-272
    • (2003) J. Chem. Phys. , vol.118 , pp. 264-272
    • Lawrence, C.P.1    Skinner, J.L.2
  • 95
    • 33748257791 scopus 로고    scopus 로고
    • Characterization of Spectral Diffusion from Two-Dimensional Line Shapes
    • Roberts, S. T.; Loparo, J. J.; Tokmakoff, A. Characterization of Spectral Diffusion from Two-Dimensional Line Shapes J. Chem. Phys. 2006, 125, 084502/1-084502/8
    • (2006) J. Chem. Phys. , vol.125 , pp. 0845021-0845028
    • Roberts, S.T.1    Loparo, J.J.2    Tokmakoff, A.3
  • 96
    • 77954173282 scopus 로고    scopus 로고
    • Vibrational Line Shapes, Spectral Diffusion, and Hydrogen Bonding in Liquid Water
    • Skinner, J. L.; Auer, B. M.; Lin, Y.-S. Vibrational Line Shapes, Spectral Diffusion, and Hydrogen Bonding in Liquid Water Adv. Chem. Phys. 2009, 142, 59-103
    • (2009) Adv. Chem. Phys. , vol.142 , pp. 59-103
    • Skinner, J.L.1    Auer, B.M.2    Lin, Y.-S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.