메뉴 건너뛰기




Volumn 117, Issue 16, 2013, Pages 4661-4669

Monitoring the folding of Trp-cage peptide by two-dimensional infrared (2DIR) spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ISOTOPES; MOLECULAR BIOLOGY; PROTEIN FOLDING; PROTEINS;

EID: 84876748955     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp309122b     Document Type: Article
Times cited : (28)

References (59)
  • 1
    • 2342514194 scopus 로고    scopus 로고
    • Many-Body Approaches for Simulating Coherent Nonlinear Spectroscopies of Electronic and Vibrational Excitons
    • Mukamel, S.; Abramavicius, D. Many-Body Approaches for Simulating Coherent Nonlinear Spectroscopies of Electronic and Vibrational Excitons Chem. Rev. 2004, 104, 2073-2098
    • (2004) Chem. Rev. , vol.104 , pp. 2073-2098
    • Mukamel, S.1    Abramavicius, D.2
  • 2
    • 77957684507 scopus 로고    scopus 로고
    • Discriminating Early Stage Aβ42 Monomer Structures Using Chirality-Induced 2DIR Spectroscopy in a Simulation Study
    • Zhuang, W.; Sgourakis, N. G.; Li, Z.; Garcia, A. E.; Mukamel, S. Discriminating Early Stage Aβ42 Monomer Structures Using Chirality-Induced 2DIR Spectroscopy in a Simulation Study Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 15687-15692
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15687-15692
    • Zhuang, W.1    Sgourakis, N.G.2    Li, Z.3    Garcia, A.E.4    Mukamel, S.5
  • 3
    • 70349783538 scopus 로고    scopus 로고
    • Coherent Multidimensional Vibrational Spectroscopy of Biomolecules; Concepts, Simulations and Challenges
    • Zhuang, W.; Hayashi, T.; Mukamel, S. Coherent Multidimensional Vibrational Spectroscopy of Biomolecules; Concepts, Simulations and Challenges Angew. Chem., Int. Ed. 2009, 48, 3750-3781
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 3750-3781
    • Zhuang, W.1    Hayashi, T.2    Mukamel, S.3
  • 4
    • 33947400829 scopus 로고    scopus 로고
    • Two-Dimensional Vibrational Optical Probes for Peptide Fast Folding Investigation
    • Zhuang, W.; Abramavicius, D.; Mukamel, S. Two-Dimensional Vibrational Optical Probes for Peptide Fast Folding Investigation Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18934-18938
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18934-18938
    • Zhuang, W.1    Abramavicius, D.2    Mukamel, S.3
  • 5
    • 78649689792 scopus 로고    scopus 로고
    • Folding Dynamics of a Small Protein at Room Temperature via Simulated Coherent Two-Dimensional Infrared Spectroscopy
    • Xiang, Y.; Duan, L. L.; Zhang, J. Z. H. Folding Dynamics of a Small Protein at Room Temperature via Simulated Coherent Two-Dimensional Infrared Spectroscopy Phys. Chem. Chem. Phys. 2010, 12, 15681-15688
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 15681-15688
    • Xiang, Y.1    Duan, L.L.2    Zhang, J.Z.H.3
  • 8
    • 79953275033 scopus 로고    scopus 로고
    • Development and Validation of Transferable Amide i Vibrational Frequency Maps for Peptides
    • Wang, L.; Middleton, 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, T.2    Zanni, M.T.3    Skinner, J.L.4
  • 10
    • 77956071045 scopus 로고    scopus 로고
    • Melting of a β-Hairpin Peptide Using Isotope-Edited 2D IR Spectroscopy and Simulations
    • Smith, A. W.; Lessing, J.; Ganim, Z.; Chunte, S. P.; Tokmakoff, A. Melting of a β-Hairpin Peptide Using Isotope-Edited 2D IR Spectroscopy and Simulations J. Phys. Chem. B 2010, 114, 10913-10924
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10913-10924
    • Smith, A.W.1    Lessing, J.2    Ganim, Z.3    Chunte, S.P.4    Tokmakoff, A.5
  • 11
    • 68549120908 scopus 로고    scopus 로고
    • 2D-IR Experiments and Simulations of the Coupling between Amide-I and Ionizable Side Chains in Proteins: Application to the Villin Headpiece
    • Bagchi, S.; Falvo, C.; Mukamel, S.; Hochstrasser, R. M. 2D-IR Experiments and Simulations of the Coupling between Amide-I and Ionizable Side Chains in Proteins: Application to the Villin Headpiece J. Phys. Chem. B 2009, 113, 11260-11273
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11260-11273
    • Bagchi, S.1    Falvo, C.2    Mukamel, S.3    Hochstrasser, R.M.4
  • 12
    • 79960377563 scopus 로고    scopus 로고
    • Probing the Folding of Mini-Protein Beta3s by Two-Dimensional Infrared Spectroscopy: Simulation Study
    • Marai, C. N. J.; Mukamel, S.; Wang, J. Probing the Folding of Mini-Protein Beta3s by Two-Dimensional Infrared Spectroscopy: Simulation Study PMC Biophys. 2010, 3, 8
    • (2010) PMC Biophys. , vol.3 , pp. 8
    • Marai, C.N.J.1    Mukamel, S.2    Wang, J.3
  • 15
    • 77955383498 scopus 로고    scopus 로고
    • Structural Classification of the Amide i Sites of a β-Hairpin with Isotope Label 2DIR Spectroscopy
    • Roy, S.; Jansen, T. L. C.; Knoester, J. Structural Classification of the Amide I Sites of a β-Hairpin with Isotope Label 2DIR Spectroscopy Phys. Chem. Chem. Phys. 2010, 12, 9347-9357
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 9347-9357
    • Roy, S.1    Jansen, T.L.C.2    Knoester, J.3
  • 16
    • 0035913538 scopus 로고    scopus 로고
    • Heterodyned Two-Dimensional Infrared Spectroscopy of Solvent-Dependent Conformations of Acetylproline-NH2
    • Zanni, M. T.; Gnanakaran, S.; Stenger, J.; Hochstrasser, R. Heterodyned Two-Dimensional Infrared Spectroscopy of Solvent-Dependent Conformations of Acetylproline-NH2 J. Phys. Chem. B 2001, 105, 6520-6535
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6520-6535
    • Zanni, M.T.1    Gnanakaran, S.2    Stenger, J.3    Hochstrasser, R.4
  • 20
    • 0034255123 scopus 로고    scopus 로고
    • Speeding Molecular Recognition by Using the Folding Funnel: The Fly-Casting Mechanism
    • Shoemaker, B. A.; Portman, J. J.; Wolynes, P. G. Speeding Molecular Recognition by Using the Folding Funnel: The Fly-Casting Mechanism Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 8868-8873
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 21
    • 79953804451 scopus 로고    scopus 로고
    • Exploring the Thermodynamic Landscape, Kinetics, and Structural Evolution of a Protein Conformational Transition with a Microscopic Double-Well Model
    • Lai, Z. Z.; Lu, Q.; Wang, J. Exploring the Thermodynamic Landscape, Kinetics, and Structural Evolution of a Protein Conformational Transition with a Microscopic Double-Well Model J. Phys. Chem. B 2011, 115, 4147-4159
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4147-4159
    • Lai, Z.Z.1    Lu, Q.2    Wang, J.3
  • 22
    • 0037346726 scopus 로고    scopus 로고
    • The Physics and Bioinformatics of Binding and Folding- an Energy Landscape Perspective
    • Papoian, G. A.; Wolynes, P. G. The Physics and Bioinformatics of Binding and Folding- an Energy Landscape Perspective Biopolymers 2003, 68, 333-349
    • (2003) Biopolymers , vol.68 , pp. 333-349
    • Papoian, G.A.1    Wolynes, P.G.2
  • 23
    • 84860417027 scopus 로고    scopus 로고
    • Behind the Folding Funnel Diagram
    • Karplus, M. Behind the Folding Funnel Diagram Nat. Chem. Biol. 2011, 7, 648
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 648
    • Karplus, M.1
  • 24
    • 0038266221 scopus 로고    scopus 로고
    • Energy Landscape Theory, Funnels, Specificity, and Optimal Criterion of Biomolecular Binding
    • Wang, J.; Verkhivker, G. M. Energy Landscape Theory, Funnels, Specificity, and Optimal Criterion of Biomolecular Binding Phys. Rev. Lett. 2003, 90, 188101
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 188101
    • Wang, J.1    Verkhivker, G.M.2
  • 25
    • 67149105514 scopus 로고    scopus 로고
    • Uncovering the Properties of Energy-Weighted Conformation Space Networks with a Hydrophobic-Hydrophilic Model
    • Lai, Z. Z.; Su, J. G.; Chen, W. Z.; Wang, C. X. Uncovering the Properties of Energy-Weighted Conformation Space Networks with a Hydrophobic-Hydrophilic Model Int. J. Mol. Sci. 2009, 10, 1808-1823
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1808-1823
    • Lai, Z.Z.1    Su, J.G.2    Chen, W.Z.3    Wang, C.X.4
  • 26
    • 84860503044 scopus 로고    scopus 로고
    • Configuration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding
    • Xu, W. X.; Lai, Z. Z.; Oliveira, R. J.; Leite, V. B. P.; Wang, J. Configuration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding J. Phys. Chem. B 2012, 116, 5152-5159
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5152-5159
    • Xu, W.X.1    Lai, Z.Z.2    Oliveira, R.J.3    Leite, V.B.P.4    Wang, J.5
  • 27
    • 84862274056 scopus 로고    scopus 로고
    • Conformational Dynamics of the Trp-Cage Miniprotein at Its Folding Temperature
    • Halabis, A.; Zmudzinska, W.; Liwo, A.; Oldziej, S. Conformational Dynamics of the Trp-Cage Miniprotein at Its Folding Temperature J. Phys. Chem. B 2012, 116, 6898-6907
    • (2012) J. Phys. Chem. B , vol.116 , pp. 6898-6907
    • Halabis, A.1    Zmudzinska, W.2    Liwo, A.3    Oldziej, S.4
  • 28
    • 0344824394 scopus 로고    scopus 로고
    • Trp-Cage: Folding Free Energy Landscape in Explicit Water
    • Zhou, R. H. Trp-Cage: Folding Free Energy Landscape in Explicit Water Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 13280-13285
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13280-13285
    • Zhou, R.H.1
  • 29
    • 0001861319 scopus 로고
    • How to Fold Graciously
    • In; Debrunner, P. Tsibris, J. Munck, E. University of Illinois Press: Urbana, IL
    • Levinthal, C. How to Fold Graciously. In Proceedings in Mossbauer Spectroscopy in Biological Systems; Debrunner, P.; Tsibris, J.; Munck, E., Eds.; University of Illinois Press: Urbana, IL, 1969; p 22.
    • (1969) Proceedings in Mossbauer Spectroscopy in Biological Systems , pp. 22
    • Levinthal, C.1
  • 30
    • 0001209011 scopus 로고    scopus 로고
    • Statistics of Kinetic Pathways on Biased Rough Energy Landscapes with Applications to Protein Folding
    • Wang, J.; Onuchic, J. N.; Wolynes, P. G. Statistics of Kinetic Pathways on Biased Rough Energy Landscapes with Applications to Protein Folding Phys. Rev. Lett. 1996, 76, 4861
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 4861
    • Wang, J.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 32
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded Proteins and Protein Folding Studied by NMR
    • Dyson, H. J.; Wright, P. E. Unfolded Proteins and Protein Folding Studied by NMR Chem. Rev. 2004, 104, 3607-3622
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 33
    • 24144459872 scopus 로고    scopus 로고
    • Coherent Third-Order Spectroscopic Probes of Molecular Chirality
    • Abramavicius, D.; Mukamel, S. Coherent Third-Order Spectroscopic Probes of Molecular Chirality J. Chem. Phys. 2005, 122, 134305
    • (2005) J. Chem. Phys. , vol.122 , pp. 134305
    • Abramavicius, D.1    Mukamel, S.2
  • 34
    • 33947400829 scopus 로고    scopus 로고
    • Two-Dimensional Vibrational Optical Probes for Peptide Fast Folding Investigation
    • Zhuang, W.; Abramavicius, D.; Mukamel, S. Two-Dimensional Vibrational Optical Probes for Peptide Fast Folding Investigation Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18934
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18934
    • Zhuang, W.1    Abramavicius, D.2    Mukamel, S.3
  • 35
    • 79956106725 scopus 로고    scopus 로고
    • Probing Amyloid Fibril Growth by Two-Dimensional Near-Ultraviolet Spectroscopy
    • Jiang, J.; Mukamel, S. Probing Amyloid Fibril Growth by Two-Dimensional Near-Ultraviolet Spectroscopy J. Phys. Chem. B 2011, 115, 6321-6328
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6321-6328
    • Jiang, J.1    Mukamel, S.2
  • 36
    • 79251591658 scopus 로고    scopus 로고
    • Two-Dimensional Near-Ultraviolet Spectroscopy of Aromatic Residues in Amyloid Fibrils: A First Principles Study
    • Jiang, J.; Mukamel, S. Two-Dimensional Near-Ultraviolet Spectroscopy of Aromatic Residues in Amyloid Fibrils: a First Principles Study Phys. Chem. Chem. Phys. 2011, 13, 2394-2400
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2394-2400
    • Jiang, J.1    Mukamel, S.2
  • 37
    • 80755174397 scopus 로고    scopus 로고
    • Distinguishing Amyloid Fibril Structures in Alzheimer's Disease (AD) by Two-Dimensional Ultraviolet (2DUV) Spectroscopy
    • Lam, A.; Jiang, J.; Mukamel, S. Distinguishing Amyloid Fibril Structures in Alzheimer's Disease (AD) by Two-Dimensional Ultraviolet (2DUV) Spectroscopy Biochemistry 2011, 50, 9809-9816
    • (2011) Biochemistry , vol.50 , pp. 9809-9816
    • Lam, A.1    Jiang, J.2    Mukamel, S.3
  • 39
    • 0036264457 scopus 로고    scopus 로고
    • Mini-Proteins Trp the Light Fantastic
    • Gellman, S. H.; Woolfson, D. N. Mini-Proteins Trp the Light Fantastic Nat. Struct. Biol. 2002, 9, 408-410
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 408-410
    • Gellman, S.H.1    Woolfson, D.N.2
  • 40
    • 23744503388 scopus 로고    scopus 로고
    • UV-Resonance Raman Thermal Unfolding Study of Trp-Cage Shows That It Is Not a Simple Two-State Miniprotein
    • Ahmed, Z.; Beta, I. A.; Mikhonin, A. V.; Asher, S. A. UV-Resonance Raman Thermal Unfolding Study of Trp-Cage Shows That It Is Not a Simple Two-State Miniprotein J. Am. Chem. Soc. 2005, 127, 10943-10950
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10943-10950
    • Ahmed, Z.1    Beta, I.A.2    Mikhonin, A.V.3    Asher, S.A.4
  • 42
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters
    • Hornak, V.; Abel, R.; Okur, A.; Strockbine, B.; Roitberg, A.; Simmerling, C. Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters Proteins 2006, 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 44
    • 1842479952 scopus 로고    scopus 로고
    • Exploring Protein Native States and Large-Scale Conformational Changes with a Modified Generalized Born Model
    • Onufriev, A.; Bashford, D.; Case, D. A. Exploring Protein Native States and Large-Scale Conformational Changes With a Modified Generalized Born Model Proteins 2004, 55, 383-394
    • (2004) Proteins , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 45
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of N-Alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of N-Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 46
    • 27744526374 scopus 로고    scopus 로고
    • Electrostatic DFT Map for the Complete Vibrational Amide Band of NMA
    • Hayashi, T.; Zhuang, W.; Mukamel, S. Electrostatic DFT Map for the Complete Vibrational Amide Band of NMA J. Phys. Chem. A 2005, 109, 9747-9759
    • (2005) J. Phys. Chem. A , vol.109 , pp. 9747-9759
    • Hayashi, T.1    Zhuang, W.2    Mukamel, S.3
  • 47
    • 0035819028 scopus 로고    scopus 로고
    • Ab Initio Calculation of Amide Carbonyl Stretch Vibrational Frequencies in Solution with Modified Basis Sets. 1. N-Methyl Acetamide
    • Kubelka, J.; Keiderling, T. A. Ab Initio Calculation of Amide Carbonyl Stretch Vibrational Frequencies in Solution with Modified Basis Sets. 1. N-Methyl Acetamide J. Phys. Chem. A 2001, 105, 10922-10928
    • (2001) J. Phys. Chem. A , vol.105 , pp. 10922-10928
    • Kubelka, J.1    Keiderling, T.A.2
  • 48
    • 0001326710 scopus 로고    scopus 로고
    • Structure of the Amide i Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy
    • Hamm, P.; Lim, M.; Hochstrasser, R. M. Structure of the Amide I Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy J. Phys. Chem. B 1998, 102, 6123-6138
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6123-6138
    • Hamm, P.1    Lim, M.2    Hochstrasser, R.M.3
  • 49
    • 84860232114 scopus 로고    scopus 로고
    • Coherent Two-Dimensional Infrared Spectroscopy: Quantitative Analysis of Protein Secondary Structure in Solution
    • Baiz, C. R.; Sam, P. C.; Reppert, M. K.; Jones, K. C.; Tokmakoff, A. Coherent Two-Dimensional Infrared Spectroscopy: Quantitative Analysis of Protein Secondary Structure in Solution Analyst 2012, 137, 1793-1799
    • (2012) Analyst , vol.137 , pp. 1793-1799
    • Baiz, C.R.1    Sam, P.C.2    Reppert, M.K.3    Jones, K.C.4    Tokmakoff, A.5
  • 50
    • 36449001245 scopus 로고
    • Model Calculations on the Amide-I Infrared Bands of Globular Proteins
    • Torii, H.; Tasumi, M. Model Calculations on the Amide-I Infrared Bands of Globular Proteins J. Chem. Phys. 1992, 96, 3379
    • (1992) J. Chem. Phys. , vol.96 , pp. 3379
    • Torii, H.1    Tasumi, M.2
  • 51
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of Activation Free Energies in Molecular Systems
    • Neria, E.; Fischer, S.; Karplus, M. Simulation of Activation Free Energies in Molecular Systems J. Chem. Phys. 1996, 105, 1902
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 52
    • 67649261996 scopus 로고    scopus 로고
    • Coherent Multidimensional Optical Spectroscopy of Excitons in Molecular Aggregates; Quasiparticle versus Supermolecule Perspectives
    • Abramavicius, D.; Palmieri, B.; Voronine, D. V.; Sanda, F.; Mukamel, S. Coherent Multidimensional Optical Spectroscopy of Excitons in Molecular Aggregates; Quasiparticle versus Supermolecule Perspectives Chem. Rev. 2009, 109, 2350-2408
    • (2009) Chem. Rev. , vol.109 , pp. 2350-2408
    • Abramavicius, D.1    Palmieri, B.2    Voronine, D.V.3    Sanda, F.4    Mukamel, S.5
  • 53
    • 0032380752 scopus 로고    scopus 로고
    • Multidimensional Femtosecond Spectroscopies of Molecular Aggregates and Semiconductor Nanostructures: The Nonlinear Exciton Equations
    • Chernyak, V.; Zhang, W. M.; Mukamel, S. Multidimensional Femtosecond Spectroscopies of Molecular Aggregates and Semiconductor Nanostructures: The Nonlinear Exciton Equations J. Chem. Phys. 1998, 109, 9587
    • (1998) J. Chem. Phys. , vol.109 , pp. 9587
    • Chernyak, V.1    Zhang, W.M.2    Mukamel, S.3
  • 54
    • 0000028325 scopus 로고    scopus 로고
    • Multidimensional Femtosecond Correlation Spectroscopies of Electronic and Vibrational Excitons
    • Zhang, W. M.; Chernyak, V.; Mukamel, S. Multidimensional Femtosecond Correlation Spectroscopies of Electronic and Vibrational Excitons J. Chem. Phys. 1999, 110, 5011
    • (1999) J. Chem. Phys. , vol.110 , pp. 5011
    • Zhang, W.M.1    Chernyak, V.2    Mukamel, S.3
  • 55
    • 0000873587 scopus 로고    scopus 로고
    • Multidimensional Femtosecond Correlation Spectroscopies of Electronic and Vibrational Excitations
    • Mukamel, S. Multidimensional Femtosecond Correlation Spectroscopies of Electronic and Vibrational Excitations Annu. Rev. Phys. Chem. 2000, 51, 691-729
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 691-729
    • Mukamel, S.1
  • 56
    • 33644914712 scopus 로고    scopus 로고
    • Simulation Protocols for Coherent Femtosecond Vibrational Spectra of Peptides
    • Zhuang, W.; Abramavicius, D.; Hayashi, T.; Mukamel, S. Simulation Protocols for Coherent Femtosecond Vibrational Spectra of Peptides J. Phys. Chem. B 2006, 110, 3362-3374
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3362-3374
    • Zhuang, W.1    Abramavicius, D.2    Hayashi, T.3    Mukamel, S.4
  • 58
    • 44949149185 scopus 로고    scopus 로고
    • Identifying Stabilizing Key Residues in Proteins Using Interresidue Interaction Energy Matrix
    • Bendova-Biedermannova, L.; Hobza, P.; Vondrasek, J. Identifying Stabilizing Key Residues in Proteins Using Interresidue Interaction Energy Matrix Proteins 2008, 72, 402-413
    • (2008) Proteins , vol.72 , pp. 402-413
    • Bendova-Biedermannova, L.1    Hobza, P.2    Vondrasek, J.3
  • 59
    • 80855133540 scopus 로고    scopus 로고
    • Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-Cage
    • Culik, R. M.; Serrano, A. L.; Bunagan, M. R.; Gai, F. Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp-Cage Angew. Chem., Int. Ed. 2011, 50, 10884-10887
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 10884-10887
    • Culik, R.M.1    Serrano, A.L.2    Bunagan, M.R.3    Gai, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.