메뉴 건너뛰기




Volumn 118, Issue 30, 2014, Pages 5657-5666

Hydration of guanidinium: Second shell formation at small cluster size

Author keywords

[No Author keywords available]

Indexed keywords

HYDRATES; HYDROGEN BONDS; IONS; MOLECULAR DYNAMICS; MOLECULES;

EID: 84905372647     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp506429a     Document Type: Article
Times cited : (19)

References (81)
  • 1
    • 0014718113 scopus 로고
    • Protein Denaturation
    • Tanford, C. Protein Denaturation Adv. Protein Chem. 1970, 24, 1-95
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 2
    • 0021755210 scopus 로고
    • Protein Stabilization and Destabilization by Guanidinium Salts
    • Arakawa, T.; Timasheff, S. N. Protein Stabilization and Destabilization by Guanidinium Salts Biochemistry 1984, 23, 5924-5929
    • (1984) Biochemistry , vol.23 , pp. 5924-5929
    • Arakawa, T.1    Timasheff, S.N.2
  • 3
    • 0027730340 scopus 로고
    • Guanidinium Chloride Induction of Partial Unfolding in Amide Proton Exchange in RNase A
    • Mayo, S. L.; Baldwin, R. L. Guanidinium Chloride Induction of Partial Unfolding in Amide Proton Exchange in RNase A Science 1993, 262, 873-876
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 5
    • 0041321045 scopus 로고    scopus 로고
    • Single-Molecule Measurement of Protein Folding Kinetics
    • Lipman, E. A.; Schuler, B.; Bakajin, O.; Eaton, W. A. Single-Molecule Measurement of Protein Folding Kinetics Science 2003, 301, 1233-1235
    • (2003) Science , vol.301 , pp. 1233-1235
    • Lipman, E.A.1    Schuler, B.2    Bakajin, O.3    Eaton, W.A.4
  • 6
    • 27744533599 scopus 로고    scopus 로고
    • Comparison of Guanidine Hydrochloride (GdnHCl) and Urea Denaturation on Inactivation and Unfolding of Human Placental Cystatin (HPC)
    • Rashid, F.; Sharma, S.; Bano, B. Comparison of Guanidine Hydrochloride (GdnHCl) and Urea Denaturation on Inactivation and Unfolding of Human Placental Cystatin (HPC) Protein J. 2005, 24, 283-292
    • (2005) Protein J. , vol.24 , pp. 283-292
    • Rashid, F.1    Sharma, S.2    Bano, B.3
  • 7
    • 84858420806 scopus 로고    scopus 로고
    • Hofmeister Phenomena: An Update on Ion Specificity in Biology
    • Lo Nostro, P.; Ninham, B. W. Hofmeister Phenomena: An Update on Ion Specificity in Biology Chem. Rev. 2012, 112, 2286-2322
    • (2012) Chem. Rev. , vol.112 , pp. 2286-2322
    • Lo Nostro, P.1    Ninham, B.W.2
  • 8
  • 9
    • 4444275437 scopus 로고    scopus 로고
    • Zur Lehre von der Wirkung der Salze (About the Science of the Effect of Salts): Franz Hofmeisters Historical Papers
    • Kunz, W.; Henle, J.; Ninham, B. W. Zur Lehre von der Wirkung der Salze (About the Science of the Effect of Salts): Franz Hofmeisters Historical Papers Curr. Opin. Colloid Interface Sci. 2004, 9, 19-37
    • (2004) Curr. Opin. Colloid Interface Sci. , vol.9 , pp. 19-37
    • Kunz, W.1    Henle, J.2    Ninham, B.W.3
  • 10
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between Macromolecules and Ions: The Hofmeister Series
    • Zhang, Y. J.; Cremer, P. S. Interactions between Macromolecules and Ions: The Hofmeister Series Curr. Opin. Chem. Biol. 2006, 10, 658-663
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 658-663
    • Zhang, Y.J.1    Cremer, P.S.2
  • 11
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister Series: Salt and Solvent Effects on Interfacial Phenomena
    • Cacace, M. G.; Landau, E. M.; Ramsden, J. J. The Hofmeister Series: Salt and Solvent Effects on Interfacial Phenomena Q. Rev. Biophys. 1997, 30, 241-277
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 12
    • 27944487490 scopus 로고    scopus 로고
    • Effect of Ions and Other Compatible Solutes on Enzyme Activity, and its Implication for Biocatalysis using Ionic Liquids
    • Zhao, H. Effect of Ions and Other Compatible Solutes on Enzyme Activity, and its Implication for Biocatalysis using Ionic Liquids J. Mol. Catal. B: Enzym. 2005, 37, 16-25
    • (2005) J. Mol. Catal. B: Enzym. , vol.37 , pp. 16-25
    • Zhao, H.1
  • 13
  • 14
    • 0027996937 scopus 로고
    • Hofmeister Effect in Ion-Transport - Reversible Binding of Halide Anions to the Roflamycoin Channel
    • Grigorjev, P. A.; Bezrukov, S. M. Hofmeister Effect in Ion-Transport-Reversible Binding of Halide Anions to the Roflamycoin Channel Biophys. J. 1994, 67, 2265-2271
    • (1994) Biophys. J. , vol.67 , pp. 2265-2271
    • Grigorjev, P.A.1    Bezrukov, S.M.2
  • 15
    • 33646732279 scopus 로고    scopus 로고
    • On the Nature of Ions at the Liquid Water Surface
    • Petersen, P. B.; Saykally, R. J. On the Nature of Ions at the Liquid Water Surface Annu. Rev. Phys. Chem. 2006, 57, 333-364
    • (2006) Annu. Rev. Phys. Chem. , vol.57 , pp. 333-364
    • Petersen, P.B.1    Saykally, R.J.2
  • 16
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister Series and Osmolytes: Effects on Proteins in Solution and in the Crystallization Process
    • Collins, K. D. Ions from the Hofmeister Series and Osmolytes: Effects on Proteins in Solution and in the Crystallization Process Methods 2004, 34, 300-311
    • (2004) Methods , vol.34 , pp. 300-311
    • Collins, K.D.1
  • 18
    • 65349131484 scopus 로고    scopus 로고
    • Effect of Ions on the Structure of Water: Structure Making and Breaking
    • Marcus, Y. Effect of Ions on the Structure of Water: Structure Making and Breaking Chem. Rev. 2009, 109, 1346-1370
    • (2009) Chem. Rev. , vol.109 , pp. 1346-1370
    • Marcus, Y.1
  • 19
    • 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
  • 20
    • 84885999848 scopus 로고    scopus 로고
    • Protein Denaturation with Guanidinium: A 2D-IR Study
    • Huerta-Viga, A.; Woutersen, S. Protein Denaturation with Guanidinium: A 2D-IR Study J. Phys. Chem. Lett. 2013, 4, 3397-3401
    • (2013) J. Phys. Chem. Lett. , vol.4 , pp. 3397-3401
    • Huerta-Viga, A.1    Woutersen, S.2
  • 23
    • 34250869055 scopus 로고    scopus 로고
    • Interactions between Hydrophobic and Ionic Solutes in Aqueous Guanidinium Chloride and Urea Solutions: Lessons for Protein Denaturation Mechanism
    • OBrien, 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
    • Obrien, E.P.1    Dima, R.I.2    Brooks, B.3    Thirumalai, D.4
  • 24
    • 45849084663 scopus 로고    scopus 로고
    • Urea and Guanidinium Chloride Denature Protein L in Different Ways in Molecular Dynamics Simulations
    • Camilloni, C.; Rocco, A. G.; Eberini, I.; Gianazza, E.; Broglia, R. A.; Tiana, G. Urea and Guanidinium Chloride Denature Protein L in Different Ways in Molecular Dynamics Simulations Biophys. J. 2008, 94, 4654-4661
    • (2008) Biophys. J. , vol.94 , pp. 4654-4661
    • Camilloni, C.1    Rocco, A.G.2    Eberini, I.3    Gianazza, E.4    Broglia, R.A.5    Tiana, G.6
  • 25
    • 51749109783 scopus 로고    scopus 로고
    • Chemical Denaturants Inhibit the Onset of Dewetting
    • England, J. L.; Pande, V. S.; Haran, G. Chemical Denaturants Inhibit the Onset of Dewetting J. Am. Chem. Soc. 2008, 130, 11854-11855
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11854-11855
    • England, J.L.1    Pande, V.S.2    Haran, G.3
  • 26
    • 70450206186 scopus 로고    scopus 로고
    • Preferential Interactions of Guanidinum Ions with Aromatic Groups over Aliphatic Groups
    • Mason, P. E.; Dempsey, C. E.; Neilson, G. W.; Kline, S. R.; Brady, J. W. Preferential Interactions of Guanidinum Ions with Aromatic Groups over Aliphatic Groups J. Am. Chem. Soc. 2009, 131, 16689-16696
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16689-16696
    • Mason, P.E.1    Dempsey, C.E.2    Neilson, G.W.3    Kline, S.R.4    Brady, J.W.5
  • 27
    • 65249132421 scopus 로고    scopus 로고
    • Specificity of Ion-Protein Interactions: Complementary and Competitive Effects of Tetrapropylammonium, Guanidinium, Sulfate, and Chloride Ions
    • Mason, P. E.; Dempsey, C. E.; Vrbka, L.; Heyda, J.; Brady, J. W.; Jungwirth, P. Specificity of Ion-Protein Interactions: Complementary and Competitive Effects of Tetrapropylammonium, Guanidinium, Sulfate, and Chloride Ions J. Phys. Chem. B 2009, 113, 3227-3234
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3227-3234
    • Mason, P.E.1    Dempsey, C.E.2    Vrbka, L.3    Heyda, J.4    Brady, J.W.5    Jungwirth, P.6
  • 28
    • 77649101458 scopus 로고    scopus 로고
    • Unfolding of Hydrophobic Polymers in Guanidinium Chloride Solutions
    • Godawat, R.; Jamadagni, S. N.; Garde, S. Unfolding of Hydrophobic Polymers in Guanidinium Chloride Solutions J. Phys. Chem. B 2010, 114, 2246-2254
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2246-2254
    • Godawat, R.1    Jamadagni, S.N.2    Garde, S.3
  • 29
    • 79960814400 scopus 로고    scopus 로고
    • Contrasting the Denaturing Effect of Guanidinium Chloride with the Stabilizing Effect of Guanidinium Sulfate
    • Graziano, G. Contrasting the Denaturing Effect of Guanidinium Chloride with the Stabilizing Effect of Guanidinium Sulfate Phys. Chem. Chem. Phys. 2011, 13, 12008-12014
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 12008-12014
    • Graziano, G.1
  • 32
    • 80054686180 scopus 로고    scopus 로고
    • Like-Charge Guanidinium Pairing from Molecular Dynamics and Ab Initio Calculations
    • Vazdar, M.; Vymetal, J.; Heyda, J.; Vondrasek, J.; Jungwirth, P. Like-Charge Guanidinium Pairing from Molecular Dynamics and Ab Initio Calculations J. Phys. Chem. A 2011, 115, 11193-11201
    • (2011) J. Phys. Chem. A , vol.115 , pp. 11193-11201
    • Vazdar, M.1    Vymetal, J.2    Heyda, J.3    Vondrasek, J.4    Jungwirth, P.5
  • 33
    • 84860360922 scopus 로고    scopus 로고
    • Guanidinium in Aqueous Solution Studied by Quantum Mechanical Charge Field-Molecular Dynamics (QMCF-MD)
    • Weiss, A. K. H.; Hofer, T. S.; Randolf, B. R.; Rode, B. M. Guanidinium in Aqueous Solution Studied by Quantum Mechanical Charge Field-Molecular Dynamics (QMCF-MD) Phys. Chem. Chem. Phys. 2012, 14, 7012-7027
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 7012-7027
    • Weiss, A.K.H.1    Hofer, T.S.2    Randolf, B.R.3    Rode, B.M.4
  • 34
    • 84864743017 scopus 로고    scopus 로고
    • Like-Charge Ion Pairing in Water: An Ab Initio Molecular Dynamics Study of Aqueous Guanidinium Cations
    • Vazdar, M.; Uhlig, F.; Jungwirth, P. Like-Charge Ion Pairing in Water: An Ab Initio Molecular Dynamics Study of Aqueous Guanidinium Cations J. Phys. Chem. Lett. 2012, 3, 2021-2024
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 2021-2024
    • Vazdar, M.1    Uhlig, F.2    Jungwirth, P.3
  • 35
    • 84859302639 scopus 로고    scopus 로고
    • Effects of Guanidinium Ions on the Conformational Structure of Glucose Oxidase Studied by Electrochemistry, Spectroscopy, and Theoretical Calculations: Towards Developing a Chemical-Induced Protein Conformation Assay
    • Xu, X.; Wu, P.; Xu, W.; Shao, Q.; An, L.; Zhang, H.; Cai, C.; Zhao, B. Effects of Guanidinium Ions on the Conformational Structure of Glucose Oxidase Studied by Electrochemistry, Spectroscopy, and Theoretical Calculations: Towards Developing a Chemical-Induced Protein Conformation Assay Phys. Chem. Chem. Phys. 2012, 14, 5824-5836
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 5824-5836
    • Xu, X.1    Wu, P.2    Xu, W.3    Shao, Q.4    An, L.5    Zhang, H.6    Cai, C.7    Zhao, B.8
  • 36
    • 84879104874 scopus 로고    scopus 로고
    • Molecular Insight into Different Denaturing Efficiency of Urea, Guanidinium, and Methanol: A Comparative Simulation Study
    • Koishi, T.; Yasuoka, K.; Willow, S. Y.; Fujikawa, S.; Zeng, X. C. Molecular Insight into Different Denaturing Efficiency of Urea, Guanidinium, and Methanol: A Comparative Simulation Study J. Chem. Theory Comput. 2013, 9, 2540-2551
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 2540-2551
    • Koishi, T.1    Yasuoka, K.2    Willow, S.Y.3    Fujikawa, S.4    Zeng, X.C.5
  • 37
    • 84888173715 scopus 로고    scopus 로고
    • Concentration-Dependent Like-Charge Pairing of Guanidinium Ions and Effect of Guanidinium Chloride on the Structure and Dynamics of Water from All-Atom Molecular Dynamics Simulation
    • Mandal, M.; Mukhopadhyay, C. Concentration-Dependent Like-Charge Pairing of Guanidinium Ions and Effect of Guanidinium Chloride on the Structure and Dynamics of Water from All-Atom Molecular Dynamics Simulation Phys. Rev. E 2013, 88, 052708
    • (2013) Phys. Rev. e , vol.88 , pp. 052708
    • Mandal, M.1    Mukhopadhyay, C.2
  • 38
    • 12144259012 scopus 로고    scopus 로고
    • Dissecting Contributions to the Denaturant Sensitivities of Proteins
    • Dempsey, C. E.; Piggot, T. J.; Mason, P. E. Dissecting Contributions to the Denaturant Sensitivities of Proteins Biochemistry 2005, 44, 775-781
    • (2005) Biochemistry , vol.44 , pp. 775-781
    • Dempsey, C.E.1    Piggot, T.J.2    Mason, P.E.3
  • 39
    • 29344434301 scopus 로고    scopus 로고
    • Protein Stabilization by Specific Binding of Guanidinium to a Functional Arginine-binding Surface on an SH3 Domain
    • Zarrine-Afsar, A.; Mittermaier, A.; Kay, L. E.; Davidson, A. R. Protein Stabilization by Specific Binding of Guanidinium to a Functional Arginine-binding Surface on an SH3 Domain Protein Sci. 2006, 15, 162-170
    • (2006) Protein Sci. , vol.15 , pp. 162-170
    • Zarrine-Afsar, A.1    Mittermaier, A.2    Kay, L.E.3    Davidson, A.R.4
  • 40
    • 37549048251 scopus 로고    scopus 로고
    • The Reversal by Sulfate of the Denaturant Activity of Guanidinium
    • Dempsey, C. E.; Mason, P. E.; Bracly, J. W.; Neilson, G. W. The Reversal by Sulfate of the Denaturant Activity of Guanidinium J. Am. Chem. Soc. 2007, 129, 15895-15902
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15895-15902
    • Dempsey, C.E.1    Mason, P.E.2    Bracly, J.W.3    Neilson, G.W.4
  • 41
    • 0028153795 scopus 로고
    • Planar Stacking Interactions of Arginine and Aromatic Side-chains in Proteins
    • Flocco, M. M.; Mowbray, S. L. Planar Stacking Interactions of Arginine and Aromatic Side-chains in Proteins J. Mol. Biol. 1994, 235, 709-717
    • (1994) J. Mol. Biol. , vol.235 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 44
    • 0037446864 scopus 로고    scopus 로고
    • The Hydration Structure of Guanidinium and Thiocyanate Ions: Implications for Protein Stability in Aqueous Solution
    • Mason, P. E.; Neilson, G. W.; Dempsey, C. E.; Barnes, A. C.; Cruickshank, J. M. The Hydration Structure of Guanidinium and Thiocyanate Ions: Implications for Protein Stability in Aqueous Solution Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 4557-4561
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4557-4561
    • Mason, P.E.1    Neilson, G.W.2    Dempsey, C.E.3    Barnes, A.C.4    Cruickshank, J.M.5
  • 45
    • 56049116742 scopus 로고    scopus 로고
    • Changes in Water Structure Induced by the Guanidinium Cation and Implications for Protein Denaturation
    • Scott, J. N.; Nucci, N. V.; Vanderkooi, J. M. Changes in Water Structure Induced by the Guanidinium Cation and Implications for Protein Denaturation J. Phys. Chem. A 2008, 112, 10939-10948
    • (2008) J. Phys. Chem. A , vol.112 , pp. 10939-10948
    • Scott, J.N.1    Nucci, N.V.2    Vanderkooi, J.M.3
  • 46
    • 33846988307 scopus 로고    scopus 로고
    • Infrared Spectroscopy of Cationized Arginine in the Gas Phase: Direct Evidence for the Transition from Nonzwitterionic to Zwitterionic Structure
    • Bush, M. F.; OBrien, J. T.; Prell, J. S.; Saykally, R. J.; Williams, E. R. Infrared Spectroscopy of Cationized Arginine in the Gas Phase: Direct Evidence for the Transition from Nonzwitterionic to Zwitterionic Structure J. Am. Chem. Soc. 2007, 129, 1612-1622
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1612-1622
    • Bush, M.F.1    Obrien, J.T.2    Prell, J.S.3    Saykally, R.J.4    Williams, E.R.5
  • 49
    • 84866720099 scopus 로고    scopus 로고
    • Wheres the Charge? Protonation Sites in Gaseous Ions Change with Hydration
    • Chang, T. M.; Prell, J. S.; Warrick, E. R.; Williams, E. R. Wheres the Charge? Protonation Sites in Gaseous Ions Change with Hydration J. Am. Chem. Soc. 2012, 134, 15805-15813
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15805-15813
    • Chang, T.M.1    Prell, J.S.2    Warrick, E.R.3    Williams, E.R.4
  • 55
    • 84881166101 scopus 로고    scopus 로고
    • Hydrated Alkali Metal Ions: Spectroscopic Evidence for Clathrates
    • Cooper, R. J.; Chang, T. M.; Williams, E. R. Hydrated Alkali Metal Ions: Spectroscopic Evidence for Clathrates J. Phys. Chem. A 2013, 117, 6571-6579
    • (2013) J. Phys. Chem. A , vol.117 , pp. 6571-6579
    • Cooper, R.J.1    Chang, T.M.2    Williams, E.R.3
  • 57
    • 84878625207 scopus 로고    scopus 로고
    • Isomer-selective Detection of Hydrogen-bond Vibrations in the Protonated Water Hexamer
    • Heine, N.; Fagiani, M. R.; Rossi, M.; Wende, T.; Berden, G.; Blum, V.; Asmis, K. R. Isomer-selective Detection of Hydrogen-bond Vibrations in the Protonated Water Hexamer J. Am. Chem. Soc. 2013, 135, 8266-8273
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8266-8273
    • Heine, N.1    Fagiani, M.R.2    Rossi, M.3    Wende, T.4    Berden, G.5    Blum, V.6    Asmis, K.R.7
  • 58
    • 0343323323 scopus 로고
    • Infrared and Raman Spectra of Polyatomic Molecules
    • Van Nostrand and Co. Inc. Princeton, NJ
    • Herzberg, G. Infrared and Raman Spectra of Polyatomic Molecules; Molecular Structure and Molecular Spectra II; Van Nostrand and Co., Inc.: Princeton, NJ, 1945.
    • (1945) Molecular Structure and Molecular Spectra II
    • Herzberg, G.1
  • 59
    • 79953890799 scopus 로고    scopus 로고
    • Structural and Electric Field Effects of Ions in Aqueous Nanodrops
    • Prell, J. S.; OBrien, J. T.; Williams, E. R. Structural and Electric Field Effects of Ions in Aqueous Nanodrops J. Am. Chem. Soc. 2011, 133, 4810-4818
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4810-4818
    • Prell, J.S.1    Obrien, J.T.2    Williams, E.R.3
  • 60
    • 35648978904 scopus 로고    scopus 로고
    • Hydration of the Calcium Dication: Direct Evidence for Second Shell Formation from Infrared Spectroscopy
    • Bush, M. F.; Saykally, R. J.; Williams, E. R. Hydration of the Calcium Dication: Direct Evidence for Second Shell Formation from Infrared Spectroscopy ChemPhysChem 2007, 8, 2245-2253
    • (2007) ChemPhysChem , vol.8 , pp. 2245-2253
    • Bush, M.F.1    Saykally, R.J.2    Williams, E.R.3
  • 63
    • 33847311818 scopus 로고    scopus 로고
    • Structures, Energetics, and Spectra of Aqua-Cesium (I) Complexes: An ab initio and Experimental Study
    • Kolaski, M.; Lee, H. M.; Choi, Y. C.; Kim, K. S.; Tarakeshwar, P.; Miller, D. J.; Lisy, J. M. Structures, Energetics, and Spectra of Aqua-Cesium (I) Complexes: An ab initio and Experimental Study J. Chem. Phys. 2007, 126, 074302
    • (2007) J. Chem. Phys. , vol.126 , pp. 074302
    • Kolaski, M.1    Lee, H.M.2    Choi, Y.C.3    Kim, K.S.4    Tarakeshwar, P.5    Miller, D.J.6    Lisy, J.M.7
  • 64
    • 56449088862 scopus 로고    scopus 로고
    • x=2-5Ar Cluster Ions for M = Li, Na, K, and Cs
    • x=2-5Ar Cluster Ions for M = Li, Na, K, and Cs J. Am. Chem. Soc. 2008, 130, 15381-15392
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15381-15392
    • Miller, D.J.1    Lisy, J.M.2
  • 65
    • 56449087816 scopus 로고    scopus 로고
    • x=2-5 Cluster Ions for M = Li, Na, K, and Cs
    • x=2-5 Cluster Ions for M = Li, Na, K, and Cs J. Am. Chem. Soc. 2008, 130, 15393-15404
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15393-15404
    • Miller, D.J.1    Lisy, J.M.2
  • 66
    • 67849127102 scopus 로고    scopus 로고
    • Structures of Thermal, Mass-Selected Water Clusters Probed with Hydrophobic Ion Tags and Infrared Photodissociation Spectroscopy
    • Prell, J. S.; Williams, E. R. Structures of Thermal, Mass-Selected Water Clusters Probed with Hydrophobic Ion Tags and Infrared Photodissociation Spectroscopy J. Am. Chem. Soc. 2009, 131, 4110-4119
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4110-4119
    • Prell, J.S.1    Williams, E.R.2
  • 67
    • 0030785917 scopus 로고    scopus 로고
    • Binding Energies of the Proton-bound Amino Acid Dimers GlyGly, AlaAla, GlyAla, and LysLys Measured by Blackbody Infrared Radiative Dissociation
    • Price, W. D.; Schnier, P. D.; Williams, E. R. Binding Energies of the Proton-bound Amino Acid Dimers GlyGly, AlaAla, GlyAla, and LysLys Measured by Blackbody Infrared Radiative Dissociation J. Phys. Chem. B 1997, 101, 664-673
    • (1997) J. Phys. Chem. B , vol.101 , pp. 664-673
    • Price, W.D.1    Schnier, P.D.2    Williams, E.R.3
  • 72
    • 84255160609 scopus 로고    scopus 로고
    • Coordination Numbers of Hydrated Divalent Transition Metal Ions Investigated with IRPD Spectroscopy
    • OBrien, J. T.; Williams, E. R. Coordination Numbers of Hydrated Divalent Transition Metal Ions Investigated with IRPD Spectroscopy J. Phys. Chem. A 2011, 115, 14612-14619
    • (2011) J. Phys. Chem. A , vol.115 , pp. 14612-14619
    • Obrien, J.T.1    Williams, E.R.2
  • 75
    • 77953115563 scopus 로고    scopus 로고
    • Hydration Isomers of Protonated Phenylalanine and Derivatives: Relative Stabilities from Infrared Photodissociation
    • Prell, J. S.; Chang, T. M.; OBrien, J. T.; Williams, E. R. Hydration Isomers of Protonated Phenylalanine and Derivatives: Relative Stabilities from Infrared Photodissociation J. Am. Chem. Soc. 2010, 132, 7811-7819
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7811-7819
    • Prell, J.S.1    Chang, T.M.2    Obrien, J.T.3    Williams, E.R.4
  • 76
    • 77958494430 scopus 로고    scopus 로고
    • Entropy Drives an Attached Water Molecule from the C- to N-Terminus on Protonated Proline
    • Prell, J. S.; Correra, T. C.; Chang, T. M.; Biles, J. A.; Williams, E. R. Entropy Drives an Attached Water Molecule from the C- to N-Terminus on Protonated Proline J. Am. Chem. Soc. 2010, 132, 14733-14735
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14733-14735
    • Prell, J.S.1    Correra, T.C.2    Chang, T.M.3    Biles, J.A.4    Williams, E.R.5
  • 77
    • 79953284236 scopus 로고    scopus 로고
    • Isomer Population Analysis of Gaseous Ions from Infrared Multiple Photon Dissociation Kinetics
    • Prell, J. S.; Chang, T. M.; Biles, J. A.; Berden, G.; Oomens, J.; Williams, E. R. Isomer Population Analysis of Gaseous Ions from Infrared Multiple Photon Dissociation Kinetics J. Phys. Chem. A 2011, 115, 2745-2751
    • (2011) J. Phys. Chem. A , vol.115 , pp. 2745-2751
    • Prell, J.S.1    Chang, T.M.2    Biles, J.A.3    Berden, G.4    Oomens, J.5    Williams, E.R.6
  • 78
    • 84857045794 scopus 로고    scopus 로고
    • The Guanidinium Ion
    • Marcus, Y. The Guanidinium Ion J. Chem. Thermodyn. 2012, 48, 70-74
    • (2012) J. Chem. Thermodyn. , vol.48 , pp. 70-74
    • Marcus, Y.1
  • 79
    • 0001432987 scopus 로고
    • Ion Thermochemistry and Solvation from Gas-Phase Ion Equilibria
    • Kebarle, P. Ion Thermochemistry and Solvation from Gas-Phase Ion Equilibria Annu. Rev. Phys. Chem. 1977, 28, 445-476
    • (1977) Annu. Rev. Phys. Chem. , vol.28 , pp. 445-476
    • Kebarle, P.1
  • 80
    • 0000196643 scopus 로고    scopus 로고
    • 2+ from Gas-Phase Ion-Water Molecule Equilibria Determinations
    • 2+ from Gas-Phase Ion-Water Molecule Equilibria Determinations J. Phys. Chem. A 1998, 102, 9978-9985
    • (1998) J. Phys. Chem. A , vol.102 , pp. 9978-9985
    • Peschke, M.1    Blades, A.T.2    Kebarle, P.3
  • 81
    • 0031029477 scopus 로고    scopus 로고
    • Charge Density-Dependent Strength of Hydration and Biological Structure
    • Collins, K. D. Charge Density-Dependent Strength of Hydration and Biological Structure Biophys. J. 1997, 72, 65-76
    • (1997) Biophys. J. , vol.72 , pp. 65-76
    • Collins, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.