메뉴 건너뛰기




Volumn 9, Issue 7, 2013, Pages 2907-2921

Local vs global motions in protein folding

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84880014653     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct4001558     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H.; Sligar, S. G.; Wolynes, P. G. The energy landscapes and motions of proteins Science 1991, 254, 1598-1603 (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 3
    • 0042797442 scopus 로고    scopus 로고
    • Cambridge University Press: Cambridge, U.K
    • Wales, D. J. Energy landscapes; Cambridge University Press: Cambridge, U.K., 2003; p 681.
    • (2003) Energy Landscapes , pp. 681
    • Wales, D.J.1
  • 6
    • 49149121255 scopus 로고    scopus 로고
    • One-dimensional barrier-preserving free-energy projections of a β-sheet miniprotein: New insights into the folding process
    • Krivov, S. V.; Muff, S.; Caflisch, A.; Karplus, M. One-dimensional barrier-preserving free-energy projections of a β-sheet miniprotein: New insights into the folding process J. Phys. Chem. B 2008, 112, 8701-8714
    • (2008) J. Phys. Chem. B , vol.112 , pp. 8701-8714
    • Krivov, S.V.1    Muff, S.2    Caflisch, A.3    Karplus, M.4
  • 7
    • 57749191492 scopus 로고    scopus 로고
    • Principal component analysis for protein folding dynamics
    • Maisuradze, G. G.; Liwo, A.; Scheraga, H. A. Principal component analysis for protein folding dynamics J. Mol. Biol. 2009, 385, 312-329
    • (2009) J. Mol. Biol. , vol.385 , pp. 312-329
    • Maisuradze, G.G.1    Liwo, A.2    Scheraga, H.A.3
  • 8
    • 67249126712 scopus 로고    scopus 로고
    • How adequate are one- and two-dimensional free energy landscapes for protein folding dynamics?
    • 238102
    • Maisuradze, G. G.; Liwo, A.; Scheraga, H. A. How adequate are one- and two-dimensional free energy landscapes for protein folding dynamics? Phys. Rev. Lett. 2009, 102 (238102) 1-4
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 1-4
    • Maisuradze, G.G.1    Liwo, A.2    Scheraga, H.A.3
  • 9
    • 77950108200 scopus 로고    scopus 로고
    • Relation between free energy landscapes of proteins and dynamics
    • Maisuradze, G. G.; Liwo, A.; Scheraga, H. A. Relation between free energy landscapes of proteins and dynamics J. Chem. Theory Comput. 2010, 6, 583-595
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 583-595
    • Maisuradze, G.G.1    Liwo, A.2    Scheraga, H.A.3
  • 10
    • 77950477912 scopus 로고    scopus 로고
    • Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force field
    • Maisuradze, G. G.; Senet, P.; Czaplewski, C.; Liwo, A.; Scheraga, H. A. Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force field J. Phys. Chem. A 2010, 114, 4471-4485
    • (2010) J. Phys. Chem. A , vol.114 , pp. 4471-4485
    • Maisuradze, G.G.1    Senet, P.2    Czaplewski, C.3    Liwo, A.4    Scheraga, H.A.5
  • 11
    • 77955792308 scopus 로고    scopus 로고
    • Evidence, from simulations, of a single state with residual native structure at the thermal denaturation midpoint of a small globular protein
    • Maisuradze, G. G.; Liwo, A.; Ołdziej, S.; Scheraga, H. A. Evidence, from simulations, of a single state with residual native structure at the thermal denaturation midpoint of a small globular protein J. Am. Chem. Soc. 2010, 132, 9444-9452
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9444-9452
    • Maisuradze, G.G.1    Liwo, A.2    Ołdziej, S.3    Scheraga, H.A.4
  • 12
    • 84859564623 scopus 로고    scopus 로고
    • Hidden folding pathways in free-energy landscapes uncovered by network analysis
    • Yin, Y.; Maisuradze, G. G.; Liwo, A.; Scheraga, H. A. Hidden folding pathways in free-energy landscapes uncovered by network analysis J. Chem. Theory Comput. 2012, 8, 1176-1189
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1176-1189
    • Yin, Y.1    Maisuradze, G.G.2    Liwo, A.3    Scheraga, H.A.4
  • 13
    • 0034061258 scopus 로고    scopus 로고
    • Structural analysis of WW domains and design of a WW prototype
    • DOI 10.1038/75144
    • Macias, M. J.; Gervais, V.; Civera, C.; Oschkinat, H. Structural analysis of WW domains and design of a WW prototype Nat. Struct. Biol. 2000, 7, 375-379 (Pubitemid 30249999)
    • (2000) Nature Structural Biology , vol.7 , Issue.5 , pp. 375-379
    • Macias, M.J.1    Gervais, V.2    Civera, C.3    Oschkinat, H.4
  • 14
    • 0027435091 scopus 로고
    • Prediction of protein conformation on the basis of a search for compact structures: Test on avian pancreatic polypeptide
    • Liwo, A.; Pincus, M. R.; Wawak, R. J.; Rackovsky, S.; Scherega, H. A. Prediction of protein conformation on the basis of a search for compact structures; test on avian pancreatic polypeptide Protein Sci. 1993, 2, 1715-1731 (Pubitemid 23294348)
    • (1993) Protein Science , vol.2 , Issue.10 , pp. 1715-1731
    • Liwo, A.1    Pincus, M.R.2    Wawak, R.J.3    Rackovsky, S.4    Scheraga, H.A.5
  • 15
    • 0000095892 scopus 로고    scopus 로고
    • A united-residue force field for off-lattice protein-structure simulations. I. Functional forms and parameters of long-range side-chain interaction potentials from protein crystal data
    • Liwo, A.; Ołdziej, S.; Pincus, M. R.; Wawak, R. J.; Rackowsky, S.; Scheraga, H. A. A united-residue force field for off-lattice protein-structure simulations. I. Functional forms and parameters of long-range side-chain interaction potentials from protein crystal data J. Comput. Chem. 1997, 18, 849-873 (Pubitemid 127598574)
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.7 , pp. 849-873
    • Liwo, A.1    Oldziej, S.2    Pincus, M.R.3    Wawak, R.J.4    Rackovsky, S.5    Scheraga, H.A.6
  • 16
    • 0000095890 scopus 로고    scopus 로고
    • A united-residue force field for off-lattice protein-structure simulations. II. Parameterization of short-range interactions and determination of weights of energy terms by Z-score optimization
    • Liwo, A.; Pincus, M. R.; Wawak, R. J.; Rackovsky, S.; Ołdziej, S.; Scheraga, H. A. A united-residue force field for off-lattice protein-structure simulations. II: Parameterization of local interactions and determination of the weights of energy terms by Z-score optimization J. Comput. Chem. 1997, 18, 874-887 (Pubitemid 127598575)
    • (1997) Journal of Computational Chemistry , vol.18 , Issue.7 , pp. 874-887
    • Liwo, A.1    Pincus, M.R.2    Wawak, R.J.3    Rackovsky, S.4    Oldziej, S.5    Scheraga, H.A.6
  • 17
    • 0035424584 scopus 로고    scopus 로고
    • Cumulant-based expressions for the multibody terms for the correlation between local and electrostatic interactions in the united-residue force field
    • DOI 10.1063/1.1383989
    • Liwo, A.; Czaplewski, C.; Pillardy, J.; Scheraga, H. A. Cumulant-based expressions for the multibody terms for the correlation between local and electrostatic interactions in the united-residue force field J. Chem. Phys. 2001, 115, 2323-2347 (Pubitemid 32742790)
    • (2001) Journal of Chemical Physics , vol.115 , Issue.5 , pp. 2323-2347
    • Liwo, A.1    Czaplewski, C.2    Pillardy, J.3    Scheraga, H.A.4
  • 18
    • 3142681595 scopus 로고    scopus 로고
    • Parametrization of backbone-electrostatic and multibody contributions to the UNRES force field for protein-structure prediction from ab initio energy surfaces of model systems
    • Liwo, A.; Ołdziej, S.; Czaplewski, C.; Kozlowska, U.; Scheraga, H. A. Parametrization of backbone-electrostatic and multibody contributions to the UNRES force field for protein-structure prediction from ab initio energy surfaces of model systems J. Phys. Chem. B 2004, 108, 9421-9438
    • (2004) J. Phys. Chem. B , vol.108 , pp. 9421-9438
    • Liwo, A.1    Ołdziej, S.2    Czaplewski, C.3    Kozlowska, U.4    Scheraga, H.A.5
  • 19
    • 8344277888 scopus 로고    scopus 로고
    • Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 2. Off-lattice tests of the method with single proteins
    • Ołdziej, S.; Liwo, A.; Czaplewski, C.; Pillardy, J.; Scheraga, H. A. Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 2. Off-lattice tests of the method with single proteins J. Phys. Chem. B 2004, 108, 16934-16949
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16934-16949
    • Ołdziej, S.1    Liwo, A.2    Czaplewski, C.3    Pillardy, J.4    Scheraga, H.A.5
  • 20
    • 8344262957 scopus 로고    scopus 로고
    • Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 3. Use of many proteins in optimization
    • Ołdziej, S.; Lagiewka, J.; Liwo, A.; Czaplewski, C.; Chinchio, M.; Nanias, M.; Scheraga, H. A. Optimization of the UNRES force field by hierarchical design of the potential-energy landscape. 3. Use of many proteins in optimization J. Phys. Chem. B 2004, 108, 16950-16959
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16950-16959
    • Ołdziej, S.1    Lagiewka, J.2    Liwo, A.3    Czaplewski, C.4    Chinchio, M.5    Nanias, M.6    Scheraga, H.A.7
  • 21
    • 33847123661 scopus 로고    scopus 로고
    • Modification and optimization of the United-Residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins
    • DOI 10.1021/jp065380a
    • Liwo, A.; Khalili, M.; Czaplewski, C.; Kalinowski, S.; Ołdziej, S.; Wachucik, K.; Scheraga, H. A. Modification and optimization of the united-residue (UNRES) potential energy function for canonical simulations. I. Temperature dependence of the effective energy function and tests of the optimization method with single training proteins J. Phys. Chem. B 2007, 111, 260-285 (Pubitemid 46277990)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.1 , pp. 260-285
    • Liwo, A.1    Khalili, M.2    Czaplewski, C.3    Kalinowski, S.4    Oldziej, S.5    Wachucik, K.6    Scheraga, H.A.7
  • 22
    • 0037386699 scopus 로고    scopus 로고
    • The structural basis for biphasic kinetics in the folding of the WW domain from a formin-binding protein: Lessons for protein design?
    • DOI 10.1073/pnas.0731771100
    • Karanicolas, J.; Brooks, C. L., III. The structural basis for biphasic kinetics in the folding of the WW domain from a formin-binding protein: Lessons for protein design? Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3954-3959 (Pubitemid 36418138)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.7 , pp. 3954-3959
    • Karanicolas, J.1    Brooks III, C.L.2
  • 25
    • 33744927646 scopus 로고    scopus 로고
    • Folding, misfolding, and amyloid protofibril formation of WW domain FBP28
    • DOI 10.1529/biophysj.105.076406
    • Mu, Y.; Nordenskiold, L.; Tam, J. P. Folding, misfolding, and amyloid protofibril formation of WW domain FBP28 Biophys. J. 2006, 90, 3983-3992 (Pubitemid 43846115)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3983-3992
    • Mu, Y.1    Nordenskiold, L.2    Tam, J.P.3
  • 28
    • 78650415889 scopus 로고    scopus 로고
    • Computational design and experimental testing of the fastest-folding β-sheet protein
    • Piana, S.; Sarkar, K.; Lindorff-Larsen, K.; Guo, M.; Gruebele, M.; Shaw, D. E. Computational design and experimental testing of the fastest-folding β-sheet protein J. Mol. Biol. 2011, 405, 43-48
    • (2011) J. Mol. Biol. , vol.405 , pp. 43-48
    • Piana, S.1    Sarkar, K.2    Lindorff-Larsen, K.3    Guo, M.4    Gruebele, M.5    Shaw, D.E.6
  • 30
    • 84862195114 scopus 로고    scopus 로고
    • Effects of mutation, truncation and temperature on the folding kinetics of a WW domain
    • Maisuradze, G. G.; Zhou, R.; Liwo, A.; Xiao, Y.; Scheraga, H. A. Effects of mutation, truncation and temperature on the folding kinetics of a WW domain J. Mol. Biol. 2012, 420, 350-365
    • (2012) J. Mol. Biol. , vol.420 , pp. 350-365
    • Maisuradze, G.G.1    Zhou, R.2    Liwo, A.3    Xiao, Y.4    Scheraga, H.A.5
  • 35
    • 33745606942 scopus 로고    scopus 로고
    • Φ-Analysis at the Experimental Limits: Mechanism of β-Hairpin Formation
    • DOI 10.1016/j.jmb.2006.05.050, PII S0022283606006516
    • Petrovich, M.; Jonsson, A. L.; Ferguson, N.; Daggett, V.; Fersht, A. R. Φ-analysis at the experimental limits: mechanism of β-hairpin formation J. Mol. Biol. 2006, 360, 865-881 (Pubitemid 43993921)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.4 , pp. 865-881
    • Petrovich, M.1    Jonsson, A.L.2    Ferguson, N.3    Daggett, V.4    Fersht, A.R.5
  • 37
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • DOI 10.1016/S0925-4439(00)00029-6, PII S0925443900000296
    • Serpell, L. C. Alzheimer's amyloid fibrils: structure and assembly Biochim. Biophys. Acta 2000, 1502, 16-30 (Pubitemid 30433852)
    • (2000) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1502 , Issue.1 , pp. 16-30
    • Serpell, L.C.1
  • 38
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • DOI 10.1038/36626
    • Munoz, V.; Thompson, P. A.; Hofrichter, J.; Eaton, W. A. Folding dynamics and mechanism of β-hairpin formation Nature 1997, 390, 196-199 (Pubitemid 27507992)
    • (1997) Nature , vol.390 , Issue.6656 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 42
    • 0034718550 scopus 로고    scopus 로고
    • How does a β-hairpin fold/unfold? Competion between topology and heterogeneity in a solvable model
    • Guo, C. L.; Levine, H.; Kessler, D. A. How does a β-hairpin fold/unfold? Competion between topology and heterogeneity in a solvable model Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 10775-10779
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10775-10779
    • Guo, C.L.1    Levine, H.2    Kessler, D.A.3
  • 43
    • 23144463330 scopus 로고    scopus 로고
    • Molecular dynamics with the united-residue model of polypeptide chains. II. Langevin and Berendsen-bath dynamics and tests on model a-helical systems
    • DOI 10.1021/jp058007w
    • Khalili, M.; Liwo, A.; Jagielska, A.; Scheraga, H. A. Molecular dynamics with the united-residue model of polypeptide chains. II. Langevin and Berendsen-bath dynamics and tests on model α-helical systems J. Phys. Chem. B 2005, 109, 13798-13810 (Pubitemid 41083972)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.28 , pp. 13798-13810
    • Khalili, M.1    Liwo, A.2    Jagielska, A.3    Scheraga, H.A.4
  • 44
    • 33947091990 scopus 로고
    • A method for predicting nucleation sites for protein folding based on hydrophobic contacts
    • Matheson, R. R.; Scheraga, H. A. A method for predicting nucleation sites for protein folding based on hydrophobic contacts Macromolecules 1978, 11, 819-829
    • (1978) Macromolecules , vol.11 , pp. 819-829
    • Matheson, R.R.1    Scheraga, H.A.2
  • 45
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 10869-10873
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 46
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • DOI 10.1038/nrm1126
    • Daggett, V.; Fersht, A. R. The present view of the mechanism of protein folding Nat. Rev. Mol. Cell Biol. 2003, 4, 497-502 (Pubitemid 36648595)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.6 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 47
    • 77954758862 scopus 로고    scopus 로고
    • β-Hairpin-forming peptides; Models of early stages of protein folding
    • Lewandowska, A.; Ołdziej, S.; Liwo, A.; Scheraga, H. A. β-Hairpin-forming peptides; models of early stages of protein folding Biophys. Chem. 2010, 151, 1-9
    • (2010) Biophys. Chem. , vol.151 , pp. 1-9
    • Lewandowska, A.1    Ołdziej, S.2    Liwo, A.3    Scheraga, H.A.4
  • 49
    • 64849113583 scopus 로고
    • Generalized cumulant expansion method
    • Kubo, R. J. Generalized cumulant expansion method Phys. Soc. Jpn. 1962, 17, 1100-1120
    • (1962) Phys. Soc. Jpn. , vol.17 , pp. 1100-1120
    • Kubo, R.J.1
  • 50
    • 67649230810 scopus 로고    scopus 로고
    • An improved functional form for the temperature scaling factors of the components of the mesoscopic UNRES force field for simulations of protein structure and dynamics
    • Shen, H.; Liwo, A.; Scheraga, H. A. An improved functional form for the temperature scaling factors of the components of the mesoscopic UNRES force field for simulations of protein structure and dynamics J. Phys. Chem. B 2009, 113, 8738-8744
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8738-8744
    • Shen, H.1    Liwo, A.2    Scheraga, H.A.3
  • 53
    • 23144450194 scopus 로고    scopus 로고
    • Molecular dynamics with the united-residue model of polypeptide chains. I. Lagrange equations of motion and tests of numerical stability in the microcanonical mode
    • DOI 10.1021/jp058008o
    • Khalili, M.; Liwo, A.; Rakowski, F.; Grochowski, P.; Scheraga, H. A. Molecular dynamics with the united-residue model of polypeptide chains. I. Lagrange equations of motion and tests of numerical stability in the microcanonical mode J. Phys. Chem. B 2005, 109, 13785-13797 (Pubitemid 41083971)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.28 , pp. 13785-13797
    • Khalili, M.1    Liwo, A.2    Rakowski, F.3    Grochowski, P.4    Scheraga, H.A.5
  • 54
    • 10844292652 scopus 로고    scopus 로고
    • Energy landscape of a small peptide revealed by dihedral angle principal component analysis
    • DOI 10.1002/prot.20310
    • Mu, Y.; Nguyen, P. H.; Stock, G. Energy landscape of a small peptide revealed by dihedral angle principal component analysis Proteins 2005, 58, 45-52 (Pubitemid 39665615)
    • (2005) Proteins: Structure, Function and Genetics , vol.58 , Issue.1 , pp. 45-52
    • Mu, Y.1    Nguyen, P.H.2    Stock, G.3
  • 55
    • 34547297406 scopus 로고    scopus 로고
    • Dihedral angle principal component analysis of molecular dynamics simulations
    • 244111
    • Altis, A.; Nguyen, P. H.; Hegger, R.; Stock, G. Dihedral angle principal component analysis of molecular dynamics simulations J. Chem. Phys. 2007, 126 (244111) 1-10
    • (2007) J. Chem. Phys. , vol.126 , pp. 1-10
    • Altis, A.1    Nguyen, P.H.2    Hegger, R.3    Stock, G.4
  • 56
    • 34247261990 scopus 로고    scopus 로고
    • Free energy landscape of a biomolecule in dihedral principal component space: Sampling convergence and correspondence between structures and minima
    • DOI 10.1002/prot.21344
    • Maisuradze, G. G.; Leitner, D. M. Free energy landscape of a biomolecule in dihedral principal component space: sampling convergence and correspondence between structures and minima Proteins 2007, 67, 569-578 (Pubitemid 46625574)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.3 , pp. 569-578
    • Maisuradze, G.G.1    Leitner, D.M.2
  • 58
    • 78650586007 scopus 로고    scopus 로고
    • Nonexponential decay of internal rotational correlation functions of native proteins and self-similar structural fluctuations
    • Cote, Y.; Senet, P.; Delarue, P.; Maisuradze, G. G.; Scheraga, H. A. Nonexponential decay of internal rotational correlation functions of native proteins and self-similar structural fluctuations Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 19844-19849
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19844-19849
    • Cote, Y.1    Senet, P.2    Delarue, P.3    Maisuradze, G.G.4    Scheraga, H.A.5
  • 59
    • 84862981350 scopus 로고    scopus 로고
    • Anomalous diffusion and dynamical correlation between the side chains and the main chain of proteins in their native state
    • Cote, Y.; Senet, P.; Delarue, P.; Maisuradze, G. G.; Scheraga, H. A. Anomalous diffusion and dynamical correlation between the side chains and the main chain of proteins in their native state Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 10346-10351
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10346-10351
    • Cote, Y.1    Senet, P.2    Delarue, P.3    Maisuradze, G.G.4    Scheraga, H.A.5
  • 60
    • 0000081668 scopus 로고
    • Collective variable description of native protein dynamics
    • Hayward, S.; Goß, N. Collective variable description of native protein dynamics Annu. Rev. Phys. Chem. 1995, 46, 223-250
    • (1995) Annu. Rev. Phys. Chem. , vol.46 , pp. 223-250
    • Hayward, S.1    Goß, N.2
  • 61
    • 0000629279 scopus 로고
    • Mathematical contributions to the theory of evolution. III Regression, heredity and panmixia
    • Pearson, K. Mathematical contributions to the theory of evolution. III Regression, heredity and panmixia Philos. Trans. R. Soc., A 1896, 187, 253-318
    • (1896) Philos. Trans. R. Soc., A , vol.187 , pp. 253-318
    • Pearson, K.1
  • 62
    • 11244304395 scopus 로고    scopus 로고
    • Toward assessing the position-dependent contributions of backbone hydrogen bonding to β-sheet folding thermodynamics employing amide-to-ester perturbations
    • Deechongkit, S.; Dawson, P. E.; Kelly, J. W. Toward assessing the position-dependent contributions of backbone hydrogen bonding to β-sheet folding thermodynamics employing amide-to-ester perturbations J. Am. Chem. Soc. 2004, 126, 16762-16771
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16762
    • Deechongkit, S.1    Dawson, P.E.2    Kelly, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.