메뉴 건너뛰기




Volumn 117, Issue 37, 2013, Pages 10779-10784

Ultrasonic and densimetric characterization of the association of cyclic AMP with the cAMP-binding domain of the exchange protein EPAC1

Author keywords

[No Author keywords available]

Indexed keywords

COMPRESSIBILITY; ENTROPY; HYDRATION; MOLECULES; ULTRASONIC TESTING; VOLUMETRIC ANALYSIS;

EID: 84884520184     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp406451p     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 33745037794 scopus 로고    scopus 로고
    • Structure and Dynamics of PKA Signaling Proteins
    • Kim, C.; Vigil, D.; Anand, G.; Taylor, S. S. Structure and Dynamics of PKA Signaling Proteins Eur. J. Cell Biol. 2006, 85, 651-654
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 651-654
    • Kim, C.1    Vigil, D.2    Anand, G.3    Taylor, S.S.4
  • 2
    • 33845800991 scopus 로고    scopus 로고
    • Capturing Cyclic Nucleotides in Action: Snapshots from Crystallographic Studies
    • Rehmann, H.; Wittinghofer, A.; Bos, J. L. Capturing Cyclic Nucleotides in Action: Snapshots from Crystallographic Studies Nat. Rev. Mol. Cell Biol. 2007, 8, 63-73
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 63-73
    • Rehmann, H.1    Wittinghofer, A.2    Bos, J.L.3
  • 6
    • 50349092827 scopus 로고    scopus 로고
    • Entropy-Driven cAMP-Dependent Allosteric Control of Inhibitory Interactions in Exchange Proteins Directly Activated by cAMP
    • Das, R.; Mazhab-Jafari, M. T.; Chowdhury, S.; SilDas, S.; Selvaratnam, R.; Melacini, G. Entropy-Driven cAMP-Dependent Allosteric Control of Inhibitory Interactions in Exchange Proteins Directly Activated by cAMP J. Biol. Chem. 2008, 283, 19691-19703
    • (2008) J. Biol. Chem. , vol.283 , pp. 19691-19703
    • Das, R.1    Mazhab-Jafari, M.T.2    Chowdhury, S.3    Sildas, S.4    Selvaratnam, R.5    Melacini, G.6
  • 7
    • 84869746585 scopus 로고    scopus 로고
    • The Auto-Inhibitory Role of the EPAC Hinge Helix as Mapped by NMR
    • Selvaratnam, R.; Mazhab-Jafari, M. T.; Das, R.; Melacini, G. The Auto-Inhibitory Role of the EPAC Hinge Helix as Mapped by NMR PLoS. One. 2012, 7, e48707
    • (2012) PLoS. One. , vol.7 , pp. 48707
    • Selvaratnam, R.1    Mazhab-Jafari, M.T.2    Das, R.3    Melacini, G.4
  • 8
    • 84856748688 scopus 로고    scopus 로고
    • The Projection Analysis of NMR Chemical Shifts Reveals Extended EPAC Autoinhibition Determinants
    • Selvaratnam, R.; VanSchouwen, B.; Fogolari, F.; Mazhab-Jafari, M. T.; Das, R.; Melacini, G. The Projection Analysis of NMR Chemical Shifts Reveals Extended EPAC Autoinhibition Determinants Biophys. J. 2012, 102, 630-639
    • (2012) Biophys. J. , vol.102 , pp. 630-639
    • Selvaratnam, R.1    Vanschouwen, B.2    Fogolari, F.3    Mazhab-Jafari, M.T.4    Das, R.5    Melacini, G.6
  • 10
    • 82755171820 scopus 로고    scopus 로고
    • Role of Dynamics in the Autoinhibition and Activation of the Exchange Protein Directly Activated by Cyclic AMP (EPAC)
    • VanSchouwen, B.; Selvaratnam, R.; Fogolari, F.; Melacini, G. Role of Dynamics in the Autoinhibition and Activation of the Exchange Protein Directly Activated by Cyclic AMP (EPAC) J. Biol. Chem. 2011, 286, 42655-42669
    • (2011) J. Biol. Chem. , vol.286 , pp. 42655-42669
    • Vanschouwen, B.1    Selvaratnam, R.2    Fogolari, F.3    Melacini, G.4
  • 13
    • 0000725483 scopus 로고
    • Thermodynamic Fluctuations in Protein Molecules
    • Cooper, A. Thermodynamic Fluctuations in Protein Molecules Proc. Natl. Acad. Sci. U.S.A. 1976, 73, 2740-2741
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 14
    • 0021726687 scopus 로고
    • Protein Fluctuations and the Thermodynamic Uncertainty Principle
    • Cooper, A. Protein Fluctuations and the Thermodynamic Uncertainty Principle Prog. Biophys. Mol. Biol. 1984, 44, 181-214
    • (1984) Prog. Biophys. Mol. Biol. , vol.44 , pp. 181-214
    • Cooper, A.1
  • 15
    • 77952068200 scopus 로고    scopus 로고
    • Communication between Tandem cAMP Binding Domains in the Regulatory Subunit of Protein Kinase A-Iα as Revealed by Domain-Silencing Mutations
    • McNicholl, E. T.; Das, R.; SilDas, S.; Taylor, S. S.; Melacini, G. Communication between Tandem cAMP Binding Domains in the Regulatory Subunit of Protein Kinase A-Iα as Revealed by Domain-Silencing Mutations J. Biol. Chem. 2010, 285, 15523-15537
    • (2010) J. Biol. Chem. , vol.285 , pp. 15523-15537
    • McNicholl, E.T.1    Das, R.2    Sildas, S.3    Taylor, S.S.4    Melacini, G.5
  • 18
    • 0000493265 scopus 로고    scopus 로고
    • Role of Water in Protein-Ligand Interactions: Volumetric Characterization of the Binding of 2′-CMP and 3′-CMP to Ribonuclease A
    • Dubins, D. N.; Filfil, R.; Macgregor, R. B.; Chalikian, T. V. Role of Water in Protein-Ligand Interactions: Volumetric Characterization of the Binding of 2′-CMP and 3′-CMP to Ribonuclease A J. Phys. Chem. B 2000, 104, 390-401
    • (2000) J. Phys. Chem. B , vol.104 , pp. 390-401
    • Dubins, D.N.1    Filfil, R.2    MacGregor, R.B.3    Chalikian, T.V.4
  • 19
    • 0037470558 scopus 로고    scopus 로고
    • The Thermodynamics of Protein-Protein Recognition as Characterized by a Combination of Volumetric and Calorimetric Techniques: The Binding of Turkey Ovomucoid Third Domain to α-Chymotrypsin
    • Filfil, R.; Chalikian, T. V. The Thermodynamics of Protein-Protein Recognition as Characterized by a Combination of Volumetric and Calorimetric Techniques: The Binding of Turkey Ovomucoid Third Domain to α-Chymotrypsin J. Mol. Biol. 2003, 326, 1271-1288
    • (2003) J. Mol. Biol. , vol.326 , pp. 1271-1288
    • Filfil, R.1    Chalikian, T.V.2
  • 20
    • 0242710675 scopus 로고    scopus 로고
    • Volumetric and Spectroscopic Characterizations of Glucose-Hexokinase Association
    • Filfil, R.; Chalikian, T. V. Volumetric and Spectroscopic Characterizations of Glucose-Hexokinase Association FEBS Lett. 2003, 554, 351-356
    • (2003) FEBS Lett. , vol.554 , pp. 351-356
    • Filfil, R.1    Chalikian, T.V.2
  • 21
    • 0842326285 scopus 로고    scopus 로고
    • Binding of Bovine Pancreatic Trypsin Inhibitor to Trypsinogen: Spectroscopic and Volumetric Studies
    • Filfil, R.; Ratavosi, A.; Chalikian, T. V. Binding of Bovine Pancreatic Trypsin Inhibitor to Trypsinogen: Spectroscopic and Volumetric Studies Biochemistry 2004, 43, 1315-1322
    • (2004) Biochemistry , vol.43 , pp. 1315-1322
    • Filfil, R.1    Ratavosi, A.2    Chalikian, T.V.3
  • 22
    • 0038487378 scopus 로고    scopus 로고
    • How Large Are the Volume Changes Accompanying Protein Transitions and Binding?
    • Chalikian, T. V.; Filfil, R. How Large Are the Volume Changes Accompanying Protein Transitions and Binding? Biophys. Chem. 2003, 104, 489-499
    • (2003) Biophys. Chem. , vol.104 , pp. 489-499
    • Chalikian, T.V.1    Filfil, R.2
  • 23
    • 0038451250 scopus 로고    scopus 로고
    • Hydration Changes Accompanying Nucleic Acid Intercalation Reactions: Volumetric Characterizations
    • Han, F.; Chalikian, T. V. Hydration Changes Accompanying Nucleic Acid Intercalation Reactions: Volumetric Characterizations J. Am. Chem. Soc. 2003, 125, 7219-7229
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7219-7229
    • Han, F.1    Chalikian, T.V.2
  • 24
    • 22244467382 scopus 로고    scopus 로고
    • 2: Volumetric, Calorimetric, and Spectroscopic Characterizations
    • 2: Volumetric, Calorimetric, and Spectroscopic Characterizations Biochemistry 2005, 44, 9785-9794
    • (2005) Biochemistry , vol.44 , pp. 9785-9794
    • Han, F.1    Taulier, N.2    Chalikian, T.V.3
  • 25
    • 84864200027 scopus 로고    scopus 로고
    • Volumetric Characterization of tri- N -Acetylglucosamine Binding to Lysozyme
    • Son, I.; Shek, Y. L.; Dubins, D. N.; Chalikian, T. V. Volumetric Characterization of tri- N -Acetylglucosamine Binding to Lysozyme Biochemistry 2012, 51, 5784-5790
    • (2012) Biochemistry , vol.51 , pp. 5784-5790
    • Son, I.1    Shek, Y.L.2    Dubins, D.N.3    Chalikian, T.V.4
  • 26
    • 36448948004 scopus 로고    scopus 로고
    • Understanding cAMP-Dependent Allostery by NMR Spectroscopy: Comparative Analysis of the EPAC1 cAMP-Binding Domain in Its Apo and cAMP-Bound States
    • Mazhab-Jafari, M. T.; Das, R.; Fotheringham, S. A.; SilDas, S.; Chowdhury, S.; Melacini, G. Understanding cAMP-Dependent Allostery by NMR Spectroscopy: Comparative Analysis of the EPAC1 cAMP-Binding Domain in Its Apo and cAMP-Bound States J. Am. Chem. Soc. 2007, 129, 14482-14492
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14482-14492
    • Mazhab-Jafari, M.T.1    Das, R.2    Fotheringham, S.A.3    Sildas, S.4    Chowdhury, S.5    Melacini, G.6
  • 27
    • 0028871804 scopus 로고
    • How to Measure and Predict the Molar Absorption Coefficient of a Protein
    • Pace, C. N.; Vajdos, F.; Fee, L.; Grimsley, G.; Gray, T. How to Measure and Predict the Molar Absorption Coefficient of a Protein Protein Sci. 1995, 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 28
    • 0001384941 scopus 로고
    • The Velocity of Sound in Electrolytic Solutions
    • Barnartt, S. The Velocity of Sound in Electrolytic Solutions J. Chem. Phys. 1952, 20, 278-279
    • (1952) J. Chem. Phys. , vol.20 , pp. 278-279
    • Barnartt, S.1
  • 29
    • 0001054914 scopus 로고
    • Standard Partial Molal Compressibilities by Ultrasonics. 1. Sodium Chloride and Potassium Chloride at 25 C
    • Owen, B. B.; Simons, H. L. Standard Partial Molal Compressibilities by Ultrasonics. 1. Sodium Chloride and Potassium Chloride at 25 C J. Phys. Chem. 1957, 61, 479-482
    • (1957) J. Phys. Chem. , vol.61 , pp. 479-482
    • Owen, B.B.1    Simons, H.L.2
  • 30
    • 0025855018 scopus 로고
    • Ultrasonic Velocimetry of Biological Compounds
    • Sarvazyan, A. P. Ultrasonic Velocimetry of Biological Compounds Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 321-342
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 321-342
    • Sarvazyan, A.P.1
  • 31
    • 0015700007 scopus 로고
    • Ultrasonic Measurements with Milliliter Liquid Samples in 0.5-100 MHz Range
    • Eggers, F.; Funck, T. Ultrasonic Measurements with Milliliter Liquid Samples in 0.5-100 MHz Range Rev. Sci. Instrum. 1973, 44, 969-977
    • (1973) Rev. Sci. Instrum. , vol.44 , pp. 969-977
    • Eggers, F.1    Funck, T.2
  • 32
    • 46749102915 scopus 로고    scopus 로고
    • Ultrasonic Velocity Measurements in Liquids with High Resolution - Techniques, Selected Applications and Perspectives
    • Kaatze, U.; Eggers, F.; Lautscham, K. Ultrasonic Velocity Measurements in Liquids with High Resolution-Techniques, Selected Applications and Perspectives Meas. Sci. Technol. 2008, 19, 062001
    • (2008) Meas. Sci. Technol. , vol.19 , pp. 062001
    • Kaatze, U.1    Eggers, F.2    Lautscham, K.3
  • 33
    • 0020156572 scopus 로고
    • Development of Methods of Precise Ultrasonic Measurements in Small Volumes of Liquids
    • Sarvazyan, A. P. Development of Methods of Precise Ultrasonic Measurements in Small Volumes of Liquids Ultrasonics 1982, 20, 151-154
    • (1982) Ultrasonics , vol.20 , pp. 151-154
    • Sarvazyan, A.P.1
  • 34
    • 0028142863 scopus 로고
    • Influence of Drug Binding on DNA Hydration: Acoustic and Densimetric Characterizations of Netropsin Binding to the Poly(dAdT)poly(dAdT) and Poly(dA)poly(dT) Duplexes and the Poly(dT)poly(dA)poly(dT) Triplex at 25 C
    • Chalikian, T. V.; Plum, G. E.; Sarvazyan, A. P.; Breslauer, K. J. Influence of Drug Binding on DNA Hydration: Acoustic and Densimetric Characterizations of Netropsin Binding to the Poly(dAdT)poly(dAdT) and Poly(dA)poly(dT) Duplexes and the Poly(dT)poly(dA)poly(dT) Triplex at 25 C Biochemistry 1994, 33, 8629-8640
    • (1994) Biochemistry , vol.33 , pp. 8629-8640
    • Chalikian, T.V.1    Plum, G.E.2    Sarvazyan, A.P.3    Breslauer, K.J.4
  • 35
    • 0029011017 scopus 로고
    • Volumetric Characterizations of the Native, Molten Globule and Unfolded States of Cytochrome c at Acidic pH
    • Chalikian, T. V.; Gindikin, V. S.; Breslauer, K. J. Volumetric Characterizations of the Native, Molten Globule and Unfolded States of Cytochrome c at Acidic pH J. Mol. Biol. 1995, 250, 291-306
    • (1995) J. Mol. Biol. , vol.250 , pp. 291-306
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 36
    • 0017429069 scopus 로고
    • Areas, Volumes, Packing, and Protein Structure
    • Richards, F. M. Areas, Volumes, Packing, and Protein Structure Annu. Rev. Biophys. Bioeng. 1977, 6, 151-176
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 37
    • 0022328790 scopus 로고
    • Calculation of Molecular Volumes and Areas for Structures of Known Geometry
    • Richards, F. M. Calculation of Molecular Volumes and Areas for Structures of Known Geometry Methods Enzymol. 1985, 115, 440-464
    • (1985) Methods Enzymol. , vol.115 , pp. 440-464
    • Richards, F.M.1
  • 38
    • 0037931321 scopus 로고    scopus 로고
    • Communication between the Regulatory and the Catalytic Region of the cAMP-Responsive Guanine Nucleotide Exchange Factor EPAC
    • Rehmann, H.; Rueppel, A.; Bos, J. L.; Wittinghofer, A. Communication between the Regulatory and the Catalytic Region of the cAMP-Responsive Guanine Nucleotide Exchange Factor EPAC J. Biol. Chem. 2003, 278, 23508-23514
    • (2003) J. Biol. Chem. , vol.278 , pp. 23508-23514
    • Rehmann, H.1    Rueppel, A.2    Bos, J.L.3    Wittinghofer, A.4
  • 40
    • 33747754400 scopus 로고
    • A Scaled Particle Theory of Aqueous and Nonaqueous Solutions
    • Pierotti, R. A. A Scaled Particle Theory of Aqueous and Nonaqueous Solutions Chem. Rev. 1976, 76, 717-726
    • (1976) Chem. Rev. , vol.76 , pp. 717-726
    • Pierotti, R.A.1
  • 41
    • 0001445637 scopus 로고
    • Partial Molar Volumes of Molecules of Arbitrary Shape and the Effect of Hydrogen Bonding with Water
    • Kharakoz, D. P. Partial Molar Volumes of Molecules of Arbitrary Shape and the Effect of Hydrogen Bonding with Water J. Solution Chem. 1992, 21, 569-595
    • (1992) J. Solution Chem. , vol.21 , pp. 569-595
    • Kharakoz, D.P.1
  • 42
    • 84855965201 scopus 로고    scopus 로고
    • Size Dependence of Cavity Volume: A Molecular Dynamics Study
    • Patel, N.; Dubins, D. N.; Pomes, R.; Chalikian, T. V. Size Dependence of Cavity Volume: A Molecular Dynamics Study Biophys. Chem. 2012, 161, 46-49
    • (2012) Biophys. Chem. , vol.161 , pp. 46-49
    • Patel, N.1    Dubins, D.N.2    Pomes, R.3    Chalikian, T.V.4
  • 43
    • 0000681226 scopus 로고
    • Relation between van der Waals and Partial Molal Volumes of Organic Molecules in Water
    • Edward, J. T.; Farrell, P. G. Relation between van der Waals and Partial Molal Volumes of Organic Molecules in Water Can. J. Chem. 1975, 53, 2965-2970
    • (1975) Can. J. Chem. , vol.53 , pp. 2965-2970
    • Edward, J.T.1    Farrell, P.G.2
  • 44
    • 0008047756 scopus 로고    scopus 로고
    • The Hydration of Globular Proteins as Derived from Volume and Compressibility Measurements: Cross-Correlating Thermodynamic and Structural Data
    • Chalikian, T. V.; Totrov, M.; Abagyan, R.; Breslauer, K. J. The Hydration of Globular Proteins as Derived from Volume and Compressibility Measurements: Cross-Correlating Thermodynamic and Structural Data J. Mol. Biol. 1996, 260, 588-603
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 48
    • 0035924822 scopus 로고    scopus 로고
    • Structural Thermodynamics of Hydration
    • Chalikian, T. V. Structural Thermodynamics of Hydration J. Phys. Chem. B 2001, 105, 12566-12578
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12566-12578
    • Chalikian, T.V.1
  • 49
    • 84858040899 scopus 로고    scopus 로고
    • Free Energy Barriers for Escape of Water Molecules from Protein Hydration Layer
    • Roy, S.; Bagchi, B. Free Energy Barriers for Escape of Water Molecules from Protein Hydration Layer J. Phys. Chem. B 2012, 116, 2958-2968
    • (2012) J. Phys. Chem. B , vol.116 , pp. 2958-2968
    • Roy, S.1    Bagchi, B.2
  • 50
    • 84856776282 scopus 로고    scopus 로고
    • Thermodynamic Analysis of Water Molecules at the Surface of Proteins and Applications to Binding Site Prediction and Characterization
    • Beuming, T.; Che, Y.; Abel, R.; Kim, B.; Shanmugasundaram, V.; Sherman, W. Thermodynamic Analysis of Water Molecules at the Surface of Proteins and Applications to Binding Site Prediction and Characterization Proteins 2012, 80, 871-883
    • (2012) Proteins , vol.80 , pp. 871-883
    • Beuming, T.1    Che, Y.2    Abel, R.3    Kim, B.4    Shanmugasundaram, V.5    Sherman, W.6
  • 51
    • 80755150215 scopus 로고    scopus 로고
    • Thermodynamic Properties of Water Molecules at a Protein-Protein Interaction Surface
    • Huggins, D. J.; Marsh, M.; Payne, M. C. Thermodynamic Properties of Water Molecules at a Protein-Protein Interaction Surface J. Chem. Theory Comput. 2011, 7, 3514-3522
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 3514-3522
    • Huggins, D.J.1    Marsh, M.2    Payne, M.C.3
  • 52
    • 79955968072 scopus 로고    scopus 로고
    • Structural Characteristics of Hydration Sites in Lysozyme
    • Soda, K.; Shimbo, Y.; Seki, Y.; Taiji, M. Structural Characteristics of Hydration Sites in Lysozyme Biophys. Chem. 2011, 156, 31-42
    • (2011) Biophys. Chem. , vol.156 , pp. 31-42
    • Soda, K.1    Shimbo, Y.2    Seki, Y.3    Taiji, M.4
  • 54
    • 0027535729 scopus 로고
    • Hydrational and Intrinsic Compressibilities of Globular Proteins
    • Kharakoz, D. P.; Sarvazyan, A. P. Hydrational and Intrinsic Compressibilities of Globular Proteins Biopolymers 1993, 33, 11-26
    • (1993) Biopolymers , vol.33 , pp. 11-26
    • Kharakoz, D.P.1    Sarvazyan, A.P.2
  • 55
    • 59849097410 scopus 로고    scopus 로고
    • Label-Free Assay for Thermodynamic Analysis of Protein-Ligand Interactions: A Multivariate Strategy for Allosteric Ligand Screening
    • Gavina, J. M.; Mazhab-Jafari, M. T.; Melacini, G.; Britz-McKibbin, P. Label-Free Assay for Thermodynamic Analysis of Protein-Ligand Interactions: A Multivariate Strategy for Allosteric Ligand Screening Biochemistry 2009, 48, 223-225
    • (2009) Biochemistry , vol.48 , pp. 223-225
    • Gavina, J.M.1    Mazhab-Jafari, M.T.2    Melacini, G.3    Britz-Mckibbin, P.4
  • 56
    • 0032318864 scopus 로고    scopus 로고
    • Structure-Based Prediction of Binding Affinities and Molecular Design of Peptide Ligands
    • Luque, I.; Freire, E. Structure-Based Prediction of Binding Affinities and Molecular Design of Peptide Ligands Methods Enzymol. 1998, 295, 100-127
    • (1998) Methods Enzymol. , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 57
    • 84857537331 scopus 로고    scopus 로고
    • Statistical Mechanics and Molecular Dynamics in Evaluating Thermodynamic Properties of Biomolecular Recognition
    • Wereszczynski, J.; Mccammon, J. A. Statistical Mechanics and Molecular Dynamics in Evaluating Thermodynamic Properties of Biomolecular Recognition Q. Rev. Biophys. 2012, 45, 1-25
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 1-25
    • Wereszczynski, J.1    McCammon, J.A.2
  • 59
    • 78149500243 scopus 로고    scopus 로고
    • Using NMR to Study Fast Dynamics in Proteins: Methods and Applications
    • Sapienza, P. J.; Lee, A. L. Using NMR to Study Fast Dynamics in Proteins: Methods and Applications Curr. Opin. Pharmacol. 2010, 10, 723-730
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 723-730
    • Sapienza, P.J.1    Lee, A.L.2
  • 60
    • 34447503697 scopus 로고    scopus 로고
    • Conformational Entropy in Molecular Recognition by Proteins
    • Frederick, K. K.; Marlow, M. S.; Valentine, K. G.; Wand, A. J. Conformational Entropy in Molecular Recognition by Proteins Nature 2007, 448, 325-329
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 62
    • 0036568354 scopus 로고    scopus 로고
    • Contributions to the Binding Free Energy of Ligands to Avidin and Streptavidin
    • Lazaridis, T.; Masunov, A.; Gandolfo, F. Contributions to the Binding Free Energy of Ligands to Avidin and Streptavidin Proteins 2002, 47, 194-208
    • (2002) Proteins , vol.47 , pp. 194-208
    • Lazaridis, T.1    Masunov, A.2    Gandolfo, F.3
  • 63
    • 70349100806 scopus 로고    scopus 로고
    • Theory of Free Energy and Entropy in Noncovalent Binding
    • Zhou, H. X.; Gilson, M. K. Theory of Free Energy and Entropy in Noncovalent Binding Chem. Rev. 2009, 109, 4092-4107
    • (2009) Chem. Rev. , vol.109 , pp. 4092-4107
    • Zhou, H.X.1    Gilson, M.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.