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Volumn 6, Issue 10, 2010, Pages 3026-3038

Adaptive steered molecular dynamics of the long-distance unfolding of neuropeptide y

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EID: 84975465348     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct100320g     Document Type: Article
Times cited : (88)

References (65)
  • 1
    • 0033613131 scopus 로고    scopus 로고
    • A theoretical search for folding/unfolding nuclei in three-dimensional protein structure
    • Galzitskaya, O. V.; Finkclstein, A. V. A theoretical search for folding/unfolding nuclei in three-dimensional protein structure. Proc. Nail. Accui. Sci. U.S.A. 1999. 96, 11299- 11304.
    • (1999) Proc. Nail. Accui. Sci. U.S.A , vol.96 , pp. 11299-11304
    • Galzitskaya, O.V.1    Finkclstein, A.V.2
  • 2
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnasc by atomic force microscopy and molecular dynamics simulation
    • Best, R. B.; Li, B.; Steward, A.; Daggett, V.; Clarke, J.Can non-mechanical proteins withstand force? Stretching barnasc by atomic force microscopy and molecular dynamics simulation. Biophys. J. 2001. 81, 2344-2356.
    • (2001) Biophys. J , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 3
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a fnlll domain probed by protein engineering, AFM and MD simulation
    • Ng, S. P.; Rounsevcll, R. W. S.; Steward, A.; Geierhaas, C. D.; Williams, P. M.; Paci, E.; Clarke, J. Mechanical unfolding of TNfn3: The unfolding pathway of a fnlll domain probed by protein engineering, AFM and MD simulation. J. Mol. Biol. 2005, 350, 776-789.
    • (2005) J. Mol. Biol. , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevcll, R.W.S.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 4
    • 49149088606 scopus 로고    scopus 로고
    • Analysis of the unfolding process of green fluorescent protein by molecular dynamics simulation
    • Hisatomi, Y.; Katagiri, D.; Neya, S.; Hara, M.; Hoshino, T. Analysis of the unfolding process of green fluorescent protein by molecular dynamics simulation. J. Phys. Chem. li 2008. 112 (29), 8672-8680.
    • (2008) J. Phys. Chem. Li , vol.112 , Issue.29 , pp. 8672-8680
    • Hisatomi, Y.1    Katagiri, D.2    Neya, S.3    Hara, M.4    Hoshino, T.5
  • 5
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • Mayor, U.; Johnson, C. M.; Daggett, V.; Fcrsht, A. R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Noll. Acad. Sci. U.S.A. 2000. 97, 13518-13522.
    • (2000) Proc. Noll. Acad. Sci. U.S.A , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fcrsht, A.R.4
  • 6
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H.; Isralewit, B.; Krammer, A.; Vogel, V.; Schulten, K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 1998, 75, 662-671.
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewit, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 7
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force- probe molecular dynamics simulations
    • Grater, F.; Shen, J.; Jiang, H.; Gautcl, M.; Grubmuller, H. Mechanically induced titin kinase activation studied by force- probe molecular dynamics simulations. Biophys. J. 2005, 88, 790-804.
    • (2005) Biophys. J , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautcl, M.4    Grubmuller, H.5
  • 8
    • 0036428792 scopus 로고    scopus 로고
    • Identifying unfolding intermediates of FN-III10 by steered molecular dynamics
    • Gao, M.; Craig, D.; Vogel, V.; Schulten, K. Identifying unfolding intermediates of FN-III10 by steered molecular dynamics. J. Mol. Biol. 2002. 323, 939-950.
    • (2002) J. Mol. Biol , vol.323 , pp. 939-950
    • Gao, M.1    Craig, D.2    Vogel, V.3    Schulten, K.4
  • 9
    • 0033151955 scopus 로고    scopus 로고
    • Steered molecular dynamics simulations of force-induced protein domain unfolding
    • Lu, H.; Schulten, K. Steered molecular dynamics simulations of force-induced protein domain unfolding. Proteins 1999. 35, 453-463.
    • (1999) Proteins , vol.35 , pp. 453-463
    • Lu, H.1    Schulten, K.2
  • 10
    • 0022617388 scopus 로고
    • Neuropeptide Y: Anatomical distribution and possible function in mammalian nervous system
    • Gray, T.; Morley, J. Neuropeptide Y: Anatomical distribution and possible function in mammalian nervous system. Life Sci. 1986. 38. 389-401.
    • (1986) Life Sci , vol.38 , pp. 389-401
    • Gray, T.1    Morley, J.2
  • 11
    • 0026792438 scopus 로고
    • Neuropeptide Y and neuropeptide Y receptor subtypes in brain and peripheral tissues
    • Dumont, Y.; Fournier, A.; Quirion, R. Neuropeptide Y and neuropeptide Y receptor subtypes in brain and peripheral tissues. Progr. Neurobiol. 1992, 38, 125-167.
    • (1992) Progr. Neurobiol , vol.38 , pp. 125-167
    • Dumont, Y.1    Fournier, A.2    Quirion, R.3
  • 13
    • 0030590483 scopus 로고    scopus 로고
    • Structural diversity of receptors for neuropeptide Y, peptide YY and pancreatic polypeptide
    • Larhammar, D. Structural diversity of receptors for neuropeptide Y, peptide YY and pancreatic polypeptide. Regul. Pept. 1996. 65, 165-174.
    • (1996) Regul. Pept , vol.65 , pp. 165-174
    • Larhammar, D.1
  • 14
    • 0342313762 scopus 로고    scopus 로고
    • Evolution of the neuropeptide Y receptor family: Gene and Chromosome duplications deduced from the cloning and mapping of the five receptor subtype genes in pig
    • Wraith, A.; Tornsten, A.; Chardon, P.; Harbit, I.; Chowdhary, B. P.; Andersson, L.; Lundin, L.G.; Larhammar, D. Evolution of the neuropeptide Y receptor family: Gene and Chromosome duplications deduced from the cloning and mapping of the five receptor subtype genes in pig. Genome Res. 2000, 10, 302-310.
    • (2000) Genome Res , vol.10 , pp. 302-310
    • Wraith, A.1    Tornsten, A.2    Chardon, P.3    Harbit, I.4    Chowdhary, B.P.5    Andersson, L.6    Lundin, L.G.7    Larhammar, D.8
  • 15
    • 0029867643 scopus 로고    scopus 로고
    • Evolution of neuropeptide Y, peptide YY, and pancreatic polypeptide
    • Larhammar, D. Evolution of neuropeptide Y, peptide YY, and pancreatic polypeptide. Regul. Pept. 1996, 62, 1-11.
    • (1996) Regul. Pept. , vol.62 , pp. 1-11
    • Larhammar, D.1
  • 16
    • 0026610078 scopus 로고
    • Sequence-specific proton NMR assignments and solution structure of bovine pancreatic polypeptide
    • Li, X.; Sutcliffe, M. J.; Schwartz, T. W.; Dobson, C. M. Sequence-specific proton NMR assignments and solution structure of bovine pancreatic polypeptide. Biochemistry 1992. 31, 1245-1253.
    • (1992) Biochemistry , vol.31 , pp. 1245-1253
    • Li, X.1    Sutcliffe, M.J.2    Schwartz, T.W.3    Dobson, C.M.4
  • 17
    • 0026686896 scopus 로고
    • Solution conformation of human neuropeptide Y by IH nuclear magnetic resonance and restrained molecular dynamics
    • Darhon, H.; Bcrnassuu, J.; Delce, E. C.; Chenu, J.; Rousscl, A.; Cambillau, C. Solution conformation of human neuropeptide Y by IH nuclear magnetic resonance and restrained molecular dynamics. Eur. J. Biochem. 1992, 209, 765-771.
    • (1992) Eur. J. Biochem , vol.209 , pp. 765-771
    • Darhon, H.1    Bcrnassuu, J.2    Delce, E.C.3    Chenu, J.4    Rousscl, A.5    Cambillau, C.6
  • 18
    • 0033118234 scopus 로고    scopus 로고
    • Aspccts of the molecular structure and dynamics of neuropeptide Y
    • Nordmann, A.; Blommcrs, M.; Fret, H.; Arvintc, T.; Drake, F. Aspccts of the molecular structure and dynamics of neuropeptide Y. Eur. J. Biochem. 1999. 261, 216-226.
    • (1999) Eur. J. Biochem , vol.261 , pp. 216-226
    • Nordmann, A.1    Blommcrs, M.2    Fret, H.3    Arvintc, T.4    Drake, F.5
  • 19
    • 0026525318 scopus 로고
    • Structure of neuropeptide Y dimer in solution
    • Cowley, D.; Hoflack, J.; Pelton, J.; Saudek, V. Structure of neuropeptide Y dimer in solution. Eur. J. Biochem. 1992. 205, 1099-1106.
    • (1992) Eur. J. Biochem , vol.205 , pp. 1099-1106
    • Cowley, D.1    Hoflack, J.2    Pelton, J.3    Saudek, V.4
  • 20
    • 0026516313 scopus 로고
    • Neuropeptide Y: Optimized solid-phase synthesis and conformational analysis in trifluoroethanol
    • Mierkc, D.; Durr, H.; Kessler, H.; Jung, G. Neuropeptide Y: Optimized solid-phase synthesis and conformational analysis in trifluoroethanol. Eur. J. Biochem. 1992, 206, 39-48.
    • (1992) Eur. J. Biochem , vol.206 , pp. 39-48
    • Mierkc, D.1    Durr, H.2    Kessler, H.3    Jung, G.4
  • 22
    • 84975452638 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection
    • Bader, R;Bettio, A.; Beck Sickinger, A G.; Zerbe, O. Structure and dynamics of micelle-bound neuropeptide Y: Comparison with unligated NPY and implications for receptor selection. Genome Res. 2000. 10, 302-310.
    • (2000) Genome Res , vol.10 , pp. 302-310
    • Bader, R.1    Bettio, A.2    Beck Sickinger, A.G.3    Zerbe, O.4
  • 23
    • 3042621483 scopus 로고    scopus 로고
    • Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors
    • Lcrch, M.; Mayrhofer, M.; Zerbe, O. Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors. J. Mol. Biol. 2004. 339, 1153-1168.
    • (2004) J. Mol. Biol , vol.339 , pp. 1153-1168
    • Lcrch, M.1    Mayrhofer, M.2    Zerbe, O.3
  • 24
    • 0036083943 scopus 로고    scopus 로고
    • The neuropeptide Y monomer in solution is not folded in the pancreatic-polypeptide fold
    • Bettio, A.; Dinger, M. C.; Beck Sickinger, A. G. The neuropeptide Y monomer in solution is not folded in the pancreatic-polypeptide fold. Protein Sci. 2002, II, 1834- 1844.
    • (2002) Protein Sci. , vol.2 , pp. 1834-1844
    • Bettio, A.1    Dinger, M.C.2    Beck Sickinger, A.G.3
  • 26
    • 0019413468 scopus 로고
    • X-ray analysis (1.4-A resolution) of avian pancreatic polypeptide: Small globular protein hormone
    • Blundcll, T. L.; Pitts, J. E.; Tickle, 1. J.; Wood, S. P.; Wu, C.W. X-ray analysis (1.4-A resolution) of avian pancreatic polypeptide: Small globular protein hormone. Proc. Nail. Acad. Sci. U.S.A. 1981, 78, 4175-4179.
    • (1981) Proc. Nail. Acad. Sci. U.S.A , vol.78 , pp. 4175-4179
    • Blundcll, T.L.1    Pitts, J.E.2    Tickle, J.3    Wood, S.P.4    Wu, C.W.5
  • 27
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding
    • Daggett, V.; Fersht, A. R. Is there a unifying mechanism for protein folding. Trends Biochem. Sci. 2003, 28, 18-25.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 31
    • 33846823909 scopus 로고
    • Particle mesh Ewaldi: An N log(N) method for Ewald sums in large systems
    • Park, P. J.; Lee, S. Particle mesh Ewaldi: An N log(N) method for Ewald sums in large systems. J. Chem. Phxs. 1993, 98, 10089-10092.
    • (1993) J. Chem. Phxs , vol.98 , pp. 10089-10092
    • Park, P.J.1    Lee, S.2
  • 32
    • 0001082095 scopus 로고
    • Constant-temperature molecular dy namics
    • Nose, S. Constant-temperature molecular dy namics. J. Phxs.: Condens. Matter 1990. 2. SA115-SA119.
    • (1990) J. Phxs.: Condens. Matter , vol.2 , pp. 115-119
    • Nose, S.1
  • 33
    • 58149163268 scopus 로고    scopus 로고
    • A vulnerability in popular molecular dynamics packages concerning langevin and andersen dynamics
    • Ccrutti, D. S.; Duke, R.; Frcddolino, P. L.; Fan, H.; Lybrand, T. P. A Vulnerability in Popular Molecular Dynamics Packages Concerning Langevin and Andersen Dynamics. J. Chem. Theory Comput. 1999, 4, 1669-1680.
    • (1999) J. Chem. Theory Comput , vol.4 , pp. 1669-1680
    • Ccrutti, D.S.1    Duke, R.2    Frcddolino, P.L.3    Fan, H.4    Lybrand, T.P.5
  • 34
    • 36049017496 scopus 로고    scopus 로고
    • Simmerling, C. Improving Convergence of Replica-Exchange Simulations through Coupling to a High-Temperature Structure Reservoir
    • Okur, A.; Roc, D. R.; Cui, G.; Hornak, V.; Simmerling, C. Improving Convergence of Replica-Exchange Simulations through Coupling to a High-Temperature Structure Reservoir. J. Chem. Theory Comput. 2007. .?. 557-568.
    • (2007) J. Chem. Theory Comput , pp. 557-568
    • Okur, A.1    Roc, D.R.2    Cui, G.3    Hornak, V.4
  • 35
    • 0036968512 scopus 로고    scopus 로고
    • Increasing temperature accelerates protein unfolding without changing the pathway of unfolding
    • Day, R.; Daggett, V. Increasing Temperature Accelerates Protein Unfolding Without Changing the Pathway of Unfolding. J. Mol. Biol. 2002. 322, 189-203.
    • (2002) J. Mol. Biol , vol.322 , pp. 189-203
    • Day, R.1    Daggett, V.2
  • 36
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhcnius kinetics
    • Chan, H. S.; Dill, K. A. Protein folding in the landscape perspective: chevron plots and non-Arrhcnius kinetics. Proteins 1998. 30, 2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 39
    • 84975500725 scopus 로고    scopus 로고
    • Tuning the free energy landscape of a WW domain by temperature, mutation, and truncation
    • Nguyen, H.; Jaeger, M.; Morctto, A.; Gruebcle, M.; Kelly, J. W. Tuning the free energy landscape of a WW domain by temperature, mutation, and truncation. Proc. Natl. Acad. Sci. U.S.A. 2003. 352, 370-381.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.352 , pp. 370-381
    • Nguyen, H.1    Jaeger, M.2    Morctto, A.3    Gruebcle, M.4    Kelly, J.W.5
  • 41
    • 4244116139 scopus 로고    scopus 로고
    • Equilibrium free-energy differences from non- equilibrium measurements: A master-equation approach
    • Jarzynski, C. Equilibrium free-energy differences from non- equilibrium measurements: A master-equation approach. Phxs. Rev. E 1997. 56, 5018-5035.
    • Phxs. Rev , vol.56 , pp. 5018-5035
    • Jarzynski, C.1
  • 42
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium equality for free energy differences
    • Jarzynski, C. Nonequilibrium equality for free energy differences. Phxs. Rev. Lett. 1997. 78, 2690-2693.
    • (1997) Phxs. Rev. Lett , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 43
    • 4143087050 scopus 로고    scopus 로고
    • Calculating potentials of mean force from steered molecular dynamics simulations
    • Park, S.; Schulten, K. Calculating potentials of mean force from steered molecular dynamics simulations. J. Chem. Phxs. 2004. 120, 5946-5961. '.
    • (2004) J. Chem. Phxs , vol.120 , pp. 5946-5961
    • Park, S.1    Schulten, K.2
  • 44
    • 33748269730 scopus 로고    scopus 로고
    • Free energy calculations with non-equilibrium methods: Applications of the Jarzynksi relationship
    • Xiong, H.; Crespo, A.; Marti, M.; Estrin, D.; Roitberg, A. E. Free energy calculations with non-equilibrium methods: applications of the Jarzynksi relationship. Theor. Chem. Acta 2006. 116, 338-346.
    • (2006) Theor. Chem. Acta , vol.116 , pp. 338-346
    • Xiong, H.1    Crespo, A.2    Marti, M.3    Estrin, D.4    Roitberg, A.E.5
  • 45
  • 46
    • 38849122815 scopus 로고    scopus 로고
    • Biased Molecular Simulations for Free-Energy Mapping: A Comparison on the KcsA Channel as a Test Case
    • Piccinini, E.; Ccccarclli, M.; Affinito, F.; Brunetti, R; Jacoboni, C. Biased Molecular Simulations for Free-Energy Mapping: A Comparison on the KcsA Channel as a Test Case. J. Chem. Theory Comput. 2008. 4. 173-183.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 173-183
    • Piccinini, E.1    Ccccarclli, M.2    Affinito, F.3    Brunetti, R.4    Jacoboni, C.5
  • 47
    • 66749085629 scopus 로고    scopus 로고
    • Comparison of Three Perturbation Molecular Dynamics Methods for Modeling Conformational Transitions
    • Huang, H.; Ozkirimli, E.; Post, C. B. Comparison of Three Perturbation Molecular Dynamics Methods for Modeling Conformational Transitions. J. Chem. Theorx Comput. 2009. 5, 1304-1314.
    • (2009) J. Chem. Theorx Comput , vol.5 , pp. 1304-1314
    • Huang, H.1    Ozkirimli, E.2    Post, C.B.3
  • 48
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality
    • Liphardt, J.; Dumont, S.; Smith, S. B.; Bustamcntc, C. Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality. Science 2002. 296, 1832-1835.
    • (2002) Science , vol.296 , pp. 1832-1835
    • Liphardt, J.1    Dumont, S.2    Smith, S.B.3    Bustamcntc, C.4
  • 49
    • 19944370453 scopus 로고    scopus 로고
    • An experimental test of the Jarzynski equality in a mechanical experiment
    • Douarche, F.; Cilibcrto, S.; Petrosyan, A.; Rabbiosi, L. An experimental test of the Jarzynski equality in a mechanical experiment. Europhys. Lett. 2005. 70, 593-599.
    • (2005) Europhys. Lett , vol.70 , pp. 593-599
    • Douarche, F.1    Cilibcrto, S.2    Petrosyan, A.3    Rabbiosi, L.4
  • 50
    • 0032023968 scopus 로고    scopus 로고
    • Nonequilibrium measurements of free energy differences for microscopically reversible Markovian systems
    • Crooks, G. E. Nonequilibrium measurements of free energy differences for microscopically reversible Markovian systems. J. Stat. Phxs. 1998. 90. 1481-1487.
    • (1998) J. Stat. Phxs , vol.90 , pp. 1481-1487
    • Crooks, G.E.1
  • 51
    • 0035957434 scopus 로고    scopus 로고
    • Free energy reconstruction from nonequilibrium single-molecule pulling experiments
    • Hummer, G.; Szabo, A. Free energy reconstruction from nonequilibrium single-molecule pulling experiments. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 3658-3661.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 3658-3661
    • Hummer, G.1    Szabo, A.2
  • 52
    • 65549103385 scopus 로고    scopus 로고
    • The work-Hamiltonian connection and the usefulness of the Jarzynski equality for free energy calculations
    • Zimanyi, E. N.; Silbcy, R. J. The work-Hamiltonian connection and the usefulness of the Jarzynski equality for free energy calculations. J. Chem. Phys. 2009, 130, 171102.
    • (2009) J. Chem. Phys , vol.130 , pp. 171102
    • Zimanyi, E.N.1    Silbcy, R.J.2
  • 53
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality
    • Park, S.; Khalili Araghi, F.; Tajkhorshid, E.; Schulten, K. Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality. J. Chem. Phys. 2003, 119, 3559-3566.
    • (2003) J. Chem. Phys , vol.119 , pp. 3559-3566
    • Park, S.1    Khalili Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 54
    • 0038610896 scopus 로고    scopus 로고
    • Developing an energy landscape lor the novel function of a (bcta/alpha)8 barrel: Ammonia conduction through HisF
    • Amaro, R.; Tajkhorshid, E.; Luthcy Schultcn, Z. Developing an energy landscape lor the novel function of a (bcta/alpha)8 barrel: Ammonia conduction through HisF. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 7599-7604.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 7599-7604
    • Amaro, R.1    Tajkhorshid, E.2    Luthcy Schultcn, Z.3
  • 56
    • 33749367332 scopus 로고    scopus 로고
    • Association of putative concave protein-binding sites with the fluctuation behavior of residues
    • Ertckin, A.; Nussinov, R.; Haliloglu, T. Association of putative concave protein-binding sites with the fluctuation behavior of residues. Protein Sci. 2006. 15, 2265-2277.
    • (2006) Protein Sci , vol.15 , pp. 2265-2277
    • Ertckin, A.1    Nussinov, R.2    Haliloglu, T.3
  • 57
    • 0347193736 scopus 로고
    • Reaction-rate theory: Fifty years after Kramers
    • and references therein
    • Hnggi, P.; Talkner, P.; Borkovec, M. Reaction-rate theory: Fifty years after Kramers. Rev. Mod. Phys. 1990, 62, 251- 341, and references therein.
    • (1990) Rev. Mod. Phys , vol.62 , pp. 251-341
    • Hnggi, P.1    Talkner, P.2    Borkovec, M.3
  • 58
    • 31144451131 scopus 로고    scopus 로고
    • Reaction rate theory: What it was, where it is today, and where is it going?
    • Pollak, E.; Talkner, P. Reaction rate theory: What it was, where it is today, and where is it going? Chaos 2005, 15, 026116-111.
    • (2005) Chaos , vol.15 , pp. 026116-27111
    • Pollak, E.1    Talkner, P.2
  • 59
    • 77953284565 scopus 로고    scopus 로고
    • Transition state theory in liquids beyond planar dividing surfaces
    • Hernandez, R.; Bartsch, T.; Uzer, T. Transition state theory in liquids beyond planar dividing surfaces. Chem. Phys. 2010, 370, 270-276.
    • (2010) Chem. Phys , vol.370 , pp. 270-276
    • Hernandez, R.1    Bartsch, T.2    Uzer, T.3
  • 60
    • 0028097051 scopus 로고
    • Complete L-alanine scan of neuropeptide Y reveals ligands binding to Yl and Y2 receptors with distinguished conformations
    • Bcck Sickinger, A. G.; Wicland, H. A.; Wittneben, H.; Willim, K.D.; Rudolf, K.; Jung, G. Complete L-alanine scan of neuropeptide Y reveals ligands binding to Yl and Y2 receptors with distinguished conformations. Eur. J. Biochem. 1994, 225 (3), 947-958.
    • (1994) Eur. J. Biochem , vol.225 , Issue.3 , pp. 947-958
    • Bcck Sickinger, A.G.1    Wicland, H.A.2    Wittneben, H.3    Willim, K.D.4    Rudolf, K.5    Jung, G.6
  • 61
    • 0028089069 scopus 로고
    • Conformational and biological studies of neuropeptide Y analogs containing structural alterations
    • Fournier, A.; Gagnon, D.; Quirion, R.; Dumont, Y.; Pheng, L.H.; St Pierre, S. Conformational and biological studies of neuropeptide Y analogs containing structural alterations. Mol. Pharmacol. 1994. 45, 93-101.
    • (1994) Mol. Pharmacol , vol.45 , pp. 93-101
    • Fournier, A.1    Gagnon, D.2    Quirion, R.3    Dumont, Y.4    Pheng, L.H.5    St Pierre, S.6
  • 62
    • 34250967320 scopus 로고    scopus 로고
    • Sur unc proprictc dc la loi dc Gauss
    • Marcinkiewicz, J. Sur unc proprictc dc la loi dc Gauss. Math. Z 1939. 44, 612-618.
    • Math , vol.44 , pp. 612-618
    • Marcinkiewicz, J.1
  • 63
    • 22944465793 scopus 로고    scopus 로고
    • One-dimensional reaction coordinates for diffusive activated rate processes in many dimensions
    • Berczhkovskii, A.; Szabo, A. One-dimensional reaction coordinates for diffusive activated rate processes in many dimensions. J. Chem. Phys. 2005. 122, 014503-014506.
    • (2005) J. Chem. Phys , vol.122 , pp. 014503-014506
    • Berczhkovskii, A.1    Szabo, A.2
  • 64
    • 17444378255 scopus 로고    scopus 로고
    • One-dimensional reaction coordinate and the corresponding potential of mean force from commitment probability distribution
    • Rhce, Y. M.; Pande, V. S. One-dimensional reaction coordinate and the corresponding potential of mean force from commitment probability distribution. J. Phys. Chem. B 2005, 109, 6780-6786.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 6780-6786
    • Rhce, Y.M.1    Pande, V.S.2


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