메뉴 건너뛰기




Volumn 21, Issue 9, 2015, Pages 1578-1590

Highly sampled tetranucleotide and tetraloop motifs enable evaluation of common RNA force fields

Author keywords

AMBER; CHARMM; Enhanced sampling; Force fields; Molecular dynamics; Replica exchange; RNA

Indexed keywords

RNA;

EID: 84939789620     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.051102.115     Document Type: Article
Times cited : (119)

References (56)
  • 4
    • 43949091791 scopus 로고    scopus 로고
    • Structures, kinetics, thermodynamics, and biological functions of RNA hairpins
    • Bevilacqua PC, Blose JM. 2008. Structures, kinetics, thermodynamics, and biological functions of RNA hairpins. Annu Rev Phys Chem 59: 79-103.
    • (2008) Annu Rev Phys Chem , vol.59 , pp. 79-103
    • Bevilacqua, P.C.1    Blose, J.M.2
  • 7
    • 84884931806 scopus 로고    scopus 로고
    • Twenty-five years of nucleic acid simulations
    • Cheatham TE III, Case DA. 2013. Twenty-five years of nucleic acid simulations. Biopolymers 99: 969-977.
    • (2013) Biopolymers , vol.99 , pp. 969-977
    • Cheatham, T.E.1    Case, D.A.2
  • 8
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. Force field with improved sugar pucker phases and helical repeat
    • Cheatham TE III, Cieplak P, Kollman PA. 1999. A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat. J Biomol Struct Dyn 16: 845-862.
    • (1999) J Biomol Struct Dyn , vol.16 , pp. 845-862
    • Cheatham, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 9
    • 84885818229 scopus 로고    scopus 로고
    • High-resolution reversible folding of hyper-stable RNA tetraloops using molecular dynamics simulations
    • Chen AA, García AE. 2013. High-resolution reversible folding of hyper-stable RNA tetraloops using molecular dynamics simulations. Proc Natl Acad Sci 110: 16820-16825.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 16820-16825
    • Chen, A.A.1    García, A.E.2
  • 10
    • 73049118608 scopus 로고    scopus 로고
    • CHAMBER: Comprehensive support for CHARMM force fields within the AMBER software
    • Crowley MF, Williamson MJ, Walker RC. 2009. CHAMBER: comprehensive support for CHARMM force fields within the AMBER software. Int J Quant Chem 109: 3767-3772.
    • (2009) Int J Quant Chem , vol.109 , pp. 3767-3772
    • Crowley, M.F.1    Williamson, M.J.2    Walker, R.C.3
  • 11
    • 79955484353 scopus 로고    scopus 로고
    • ′-hydroxyl sampling on the conformational properties of RNA: Update of the CHARMM all-atom additive force field for RNA
    • ′-hydroxyl sampling on the conformational properties of RNA: update of the CHARMM all-atom additive force field for RNA. J Comput Chem 32: 1929-1943.
    • (2011) J Comput Chem , vol.32 , pp. 1929-1943
    • Denning, E.J.1    Priyakumar, U.D.2    Nilsson, L.3    MacKerell, A.D.4
  • 13
    • 0001585978 scopus 로고    scopus 로고
    • Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems
    • Feenstra KA, Hess B, Berendsen HJC. 1999. Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems. J Comput Chem 20: 786-798.
    • (1999) J Comput Chem , vol.20 , pp. 786-798
    • Feenstra, K.A.1    Hess, B.2    Berendsen, H.J.C.3
  • 14
    • 0348244547 scopus 로고    scopus 로고
    • All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data
    • Foloppe N, MacKerell AD Jr. 2000. All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data. J Comput Chem 21: 86-104.
    • (2000) J Comput Chem , vol.21 , pp. 86-104
    • Foloppe, N.1    MacKerell, A.D.2
  • 15
    • 84923206685 scopus 로고    scopus 로고
    • Convergence and reproducibility in molecular dynamics simulations of the DNA duplex d(GCACGAACGAACGAACGC)
    • Galindo-Murillo R, Roe DR, Cheatham TE III. 2014a. Convergence and reproducibility in molecular dynamics simulations of the DNA duplex d(GCACGAACGAACGAACGC). Biochim Biophys Acta 1850: 1041-1058.
    • (2014) Biochim Biophys Acta , vol.1850 , pp. 1041-1058
    • Galindo-Murillo, R.1    Roe, D.R.2    Cheatham, T.E.3
  • 16
    • 84923133278 scopus 로고    scopus 로고
    • On the absence of intrahelical DNA dynamics on the μs to ms timescale
    • Galindo-Murillo R, Roe DR, Cheatham TE III. 2014b. On the absence of intrahelical DNA dynamics on the μs to ms timescale. Nat Commun 5: 5152.
    • (2014) Nat Commun , vol.5 , pp. 5152
    • Galindo-Murillo, R.1    Roe, D.R.2    Cheatham, T.E.3
  • 17
    • 84928005209 scopus 로고    scopus 로고
    • Structural fidelity and NMR relaxation analysis in a prototype RNA hairpin
    • Giambaşu GM, York DM, Case DA. 2015. Structural fidelity and NMR relaxation analysis in a prototype RNA hairpin. RNA 21: 963-974.
    • (2015) RNA , vol.21 , pp. 963-974
    • Giambaşu, G.M.1    York, D.M.2    Case, D.A.3
  • 19
    • 3142716857 scopus 로고    scopus 로고
    • Accelerated molecular dynamics: A promising and efficient simulation method for biomol-ecules
    • Hamelberg D, Mongan J, McCammon JA. 2004. Accelerated molecular dynamics: a promising and efficient simulation method for biomol-ecules. J Chem Phys 120: 11919-11929.
    • (2004) J Chem Phys , vol.120 , pp. 11919-11929
    • Hamelberg, D.1    Mongan, J.2    McCammon, J.A.3
  • 20
    • 0031578972 scopus 로고    scopus 로고
    • Parallel tempering algorithm for conformation-al studies of biological molecules
    • Hansmann UHE. 1997. Parallel tempering algorithm for conformation-al studies of biological molecules. Chem Phys Lett 281: 140-150.
    • (1997) Chem Phys Lett , vol.281 , pp. 140-150
    • Hansmann, U.H.E.1
  • 21
    • 84876471104 scopus 로고    scopus 로고
    • Reliable oligonucleo-tide conformational ensemble generation in explicit solvent for force field assessment using reservoir replica exchange molecular dynamics simulations
    • Henriksen NM, Roe DR, Cheatham TE III. 2013. Reliable oligonucleo-tide conformational ensemble generation in explicit solvent for force field assessment using reservoir replica exchange molecular dynamics simulations. J Phys Chem B 117: 4014-4027.
    • (2013) J Phys Chem B , vol.117 , pp. 4014-4027
    • Henriksen, N.M.1    Roe, D.R.2    Cheatham, T.E.3
  • 24
    • 49449085241 scopus 로고    scopus 로고
    • Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolec-ular simulations
    • Joung IS, Cheatham TE III. 2008. Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolec-ular simulations. J Phys Chem B 112: 9020-9041.
    • (2008) J Phys Chem B , vol.112 , pp. 9020-9041
    • Joung, I.S.1    Cheatham, T.E.2
  • 26
    • 79958073354 scopus 로고    scopus 로고
    • Computational approaches to RNA structure prediction, analysis, and design
    • Laing C, Schlick T. 2011. Computational approaches to RNA structure prediction, analysis, and design. Curr Opin Struct Biol 21: 306-318.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 306-318
    • Laing, C.1    Schlick, T.2
  • 29
    • 77952472539 scopus 로고    scopus 로고
    • Extensive molecular dynamics simulations showing that canonical G8 and protonated A38H+ forms are most consistent with crystal structures of hairpin ribozyme
    • Mlýnský V, Banás P, Hollas D, Réblová K, Walter NG, Sponer J, Otyepka M. 2010. Extensive molecular dynamics simulations showing that canonical G8 and protonated A38H+ forms are most consistent with crystal structures of hairpin ribozyme. J Phys Chem B 114: 6642-6652.
    • (2010) J Phys Chem B , vol.114 , pp. 6642-6652
    • Mlýnský, V.1    Banás, P.2    Hollas, D.3    Réblová, K.4    Walter, N.G.5    Sponer, J.6    Otyepka, M.7
  • 30
    • 84907943526 scopus 로고    scopus 로고
    • Folding simulations for proteins with diverse topologies are accessible in days with a physics-based force field and implicit solvent
    • Nguyen H, Maier J, Huang H, Perrone V, Simmerling C. 2014. Folding simulations for proteins with diverse topologies are accessible in days with a physics-based force field and implicit solvent. J Am Chem Soc 136: 13959-13962.
    • (2014) J Am Chem Soc , vol.136 , pp. 13959-13962
    • Nguyen, H.1    Maier, J.2    Huang, H.3    Perrone, V.4    Simmerling, C.5
  • 31
    • 77449092763 scopus 로고    scopus 로고
    • High-resolution NMR structure of an RNA model system: The 14-mer cUUCGg tetraloop hairpin RNA
    • Nozinovic S, Fürtig B, Jonker HR, Richter C, Schwalbe H. 2010. High-resolution NMR structure of an RNA model system: the 14-mer cUUCGg tetraloop hairpin RNA. Nucleic Acids Res 38: 683-694.
    • (2010) Nucleic Acids Res , vol.38 , pp. 683-694
    • Nozinovic, S.1    Fürtig, B.2    Jonker, H.R.3    Richter, C.4    Schwalbe, H.5
  • 32
    • 41549127613 scopus 로고    scopus 로고
    • A temperature predictor for parallel tempering simulations
    • Patriksson A, van der Spoel D. 2008. A temperature predictor for parallel tempering simulations. Phys Chem Chem Phys 10: 2073-2077.
    • (2008) Phys Chem Chem Phys , vol.10 , pp. 2073-2077
    • Patriksson, A.1    Van Der Spoel, D.2
  • 33
    • 85056020125 scopus 로고    scopus 로고
    • Dynamics of B-DNA on the microsecond time scale
    • Pérez A, Luque FJ, Orozco M. 2007a. Dynamics of B-DNA on the microsecond time scale. J Am Chem Soc 101: 14771-14775.
    • (2007) J Am Chem Soc , vol.101 , pp. 14771-14775
    • Pérez, A.1    Luque, F.J.2    Orozco, M.3
  • 34
    • 34250318638 scopus 로고    scopus 로고
    • Refinement of the AMBER force field for nucleic acids: Improving the description of α/γ conformers
    • Pérez A, Marchán I, Svozil D, Sponer J, Cheatham TE III, Laughton CA, Orozco M. 2007b. Refinement of the AMBER force field for nucleic acids: improving the description of α/γ conformers. Biophys J 92: 3817-3829.
    • (2007) Biophys J , vol.92 , pp. 3817-3829
    • Pérez, A.1    Marchán, I.2    Svozil, D.3    Sponer, J.4    Cheatham, T.E.5    Laughton, C.A.6    Orozco, M.7
  • 35
    • 84860477162 scopus 로고    scopus 로고
    • Frontiers in molecular dynamics simulations of DNA
    • Pérez A, Luque FJ, Orozco M. 2012. Frontiers in molecular dynamics simulations of DNA. Acc Chem Res 45: 196-205.
    • (2012) Acc Chem Res , vol.45 , pp. 196-205
    • Pérez, A.1    Luque, F.J.2    Orozco, M.3
  • 37
    • 84880022273 scopus 로고    scopus 로고
    • PTRAJ and CPPTRAJ: Software for processing and analysis of molecular dynamics trajectory data
    • Roe DR, Cheatham TE III. 2013. PTRAJ and CPPTRAJ: software for processing and analysis of molecular dynamics trajectory data. J Chem Theory Comput 9: 3084-3095.
    • (2013) J Chem Theory Comput , vol.9 , pp. 3084-3095
    • Roe, D.R.1    Cheatham, T.E.2
  • 38
    • 84898068360 scopus 로고    scopus 로고
    • Evaluation of enhanced sampling provided by accelerated molecular dynamics with Hamil-tonian replica exchange methods
    • Roe DR, Bergonzo C, Cheatham TE III. 2014. Evaluation of enhanced sampling provided by accelerated molecular dynamics with Hamil-tonian replica exchange methods. J Phys Chem B 118: 3543-3552.
    • (2014) J Phys Chem B , vol.118 , pp. 3543-3552
    • Roe, D.R.1    Bergonzo, C.2    Cheatham, T.E.3
  • 39
    • 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 HJC. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 40
    • 84884192184 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald
    • Salomon-Ferrer R, Götz AW, Poole D, Le Grand S, Walker RC. 2013. Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald. J Chem Theory Comput 9: 3878-3888.
    • (2013) J Chem Theory Comput , vol.9 , pp. 3878-3888
    • Salomon-Ferrer, R.1    Götz, A.W.2    Poole, D.3    Le Grand, S.4    Walker, R.C.5
  • 41
    • 36649006642 scopus 로고    scopus 로고
    • Clustering molecular dynamics trajectories: 1. Characterizing the performance of different clustering algorithms
    • Shao J, Tanner SW, Thompson N, Cheatham TE III. 2007. Clustering molecular dynamics trajectories: 1. Characterizing the performance of different clustering algorithms. J Chem Theory Comput 3: 2312-2334.
    • (2007) J Chem Theory Comput , vol.3 , pp. 2312-2334
    • Shao, J.1    Tanner, S.W.2    Thompson, N.3    Cheatham, T.E.4
  • 43
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling C, Strockbine B, Roitberg AE. 2002. All-atom structure prediction and folding simulations of a stable protein. J Am Chem Soc 124: 11258-11259.
    • (2002) J Am Chem Soc , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 44
    • 67650072432 scopus 로고    scopus 로고
    • Bad seeds sprout perilous dynamics: Stochastic thermostat induced trajectory synchronization in biomolecules
    • Sindhikara DJ, Kim S, Voter AF, Roitberg AE. 2009. Bad seeds sprout perilous dynamics: stochastic thermostat induced trajectory synchronization in biomolecules. J Chem Theory Comput 5: 1624-1631.
    • (2009) J Chem Theory Comput , vol.5 , pp. 1624-1631
    • Sindhikara, D.J.1    Kim, S.2    Voter, A.F.3    Roitberg, A.E.4
  • 45
    • 0036297661 scopus 로고    scopus 로고
    • RNA simulations: Probing hairpin unfolding and the dynamics of a GNRA tet-raloop
    • Sorin EJ, Engelhardt MA, Herschlag D, Pande VS. 2002. RNA simulations: probing hairpin unfolding and the dynamics of a GNRA tet-raloop. J Mol Biol 317: 493-506.
    • (2002) J Mol Biol , vol.317 , pp. 493-506
    • Sorin, E.J.1    Engelhardt, M.A.2    Herschlag, D.3    Pande, V.S.4
  • 46
  • 47
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita Y, Okamoto Y. 1999. Replica-exchange molecular dynamics method for protein folding. Chem Phys Lett 314: 141-151.
    • (1999) Chem Phys Lett , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 49
    • 84873670994 scopus 로고    scopus 로고
    • The nuclear magnetic resonance of CCCC RNA reveals a right-handed helix, and revised parameters for AMBER force field torsions improve structural predictions from molecular dynamics
    • Tubbs JD, Condon DE, Kennedy SD, Hauser M, Bevilacqua PC, Turner DH. 2013. The nuclear magnetic resonance of CCCC RNA reveals a right-handed helix, and revised parameters for AMBER force field torsions improve structural predictions from molecular dynamics. Biochemistry 52: 996-1010.
    • (2013) Biochemistry , vol.52 , pp. 996-1010
    • Tubbs, J.D.1    Condon, D.E.2    Kennedy, S.D.3    Hauser, M.4    Bevilacqua, P.C.5    Turner, D.H.6
  • 50
    • 0025061676 scopus 로고
    • Tetraloops and RNA folding
    • Uhlenbeck OC 1990. Tetraloops and RNA folding. Nature 346: 613-614.
    • (1990) Nature , vol.346 , pp. 613-614
    • Uhlenbeck, O.C.1
  • 51
    • 59849110790 scopus 로고    scopus 로고
    • Stochastic gating and drug-ribo-some interactions
    • Vaiana AC, Sanbonmatsu KY. 2009. Stochastic gating and drug-ribo-some interactions. J Mol Biol 386: 648-661.
    • (2009) J Mol Biol , vol.386 , pp. 648-661
    • Vaiana, A.C.1    Sanbonmatsu, K.Y.2
  • 52
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J, Cieplak P, Kollman PA. 2000. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J Comput Chem 21: 1049-1074.
    • (2000) J Comput Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 53
    • 0025047647 scopus 로고
    • Architecture of ribosomal RNA: Constraints on the sequence of "tetra-loops"
    • Woese CR, Winkers S, Gutell RR. 1990. Architecture of ribosomal RNA: constraints on the sequence of "tetra-loops". Proc Natl Acad Sci 87: 8467-8471.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 8467-8471
    • Woese, C.R.1    Winkers, S.2    Gutell, R.R.3
  • 54
    • 79960650298 scopus 로고    scopus 로고
    • Benchmarking AMBER force fields for RNA: Comparisons to NMR spectra for single-stranded r(GACC) are improved by revised X torsions
    • Yildirim I, Stern HA, Tubbs JD, Kennedy SD, Turner DH. 2011. Benchmarking AMBER force fields for RNA: comparisons to NMR spectra for single-stranded r(GACC) are improved by revised X torsions. J Phys Chem B 115: 9261-9270.
    • (2011) J Phys Chem B , vol.115 , pp. 9261-9270
    • Yildirim, I.1    Stern, H.A.2    Tubbs, J.D.3    Kennedy, S.D.4    Turner, D.H.5
  • 55
    • 84855656902 scopus 로고    scopus 로고
    • Revision of AMBER torsional parameters for RNA improves free energy predictions for tetramer duplexes with GC and iGiC base pairs
    • Yildirim I, Kennedy SD, Stern HA, Hart JM, Kierzek R, Turner DH. 2012. Revision of AMBER torsional parameters for RNA improves free energy predictions for tetramer duplexes with GC and iGiC base pairs. J Chem Theory Comput 8: 172-181.
    • (2012) J Chem Theory Comput , vol.8 , pp. 172-181
    • Yildirim, I.1    Kennedy, S.D.2    Stern, H.A.3    Hart, J.M.4    Kierzek, R.5    Turner, D.H.6
  • 56
    • 80052820313 scopus 로고    scopus 로고
    • Refinement of the Cornell et al. Nucleic acids force field based on reference quantum chemical calculations of glycosidic torsion profiles
    • Zgarbová M, Otyepka M, Sponer J, Mládek A, Banás P, Cheatham TE III, Jurecka P. 2011. Refinement of the Cornell et al. nucleic acids force field based on reference quantum chemical calculations of glycosidic torsion profiles. J Chem Theory Comput 7: 2886-2902.
    • (2011) J Chem Theory Comput , vol.7 , pp. 2886-2902
    • Zgarbová, M.1    Otyepka, M.2    Sponer, J.3    Mládek, A.4    Banás, P.5    Cheatham, T.E.6    Jurecka, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.