메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

UV-radiation induced disruption of dry-cavities in human γd-crystallin results in decreased stability and faster unfolding

Author keywords

[No Author keywords available]

Indexed keywords

CRYGD PROTEIN, HUMAN; GAMMA CRYSTALLIN; KYNURENINE; TRYPTOPHAN; TYROSINE;

EID: 84875793902     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep01560     Document Type: Article
Times cited : (37)

References (62)
  • 2
    • 0030954844 scopus 로고    scopus 로고
    • Cataract as a protein condensation disease: The Proctor lecture
    • Benedek, G. B. Cataract as a protein condensation disease-The Proctor Lecture. Invest. Ophthalmol. Vis. Sci. 38, 1911-1921 (1997). (Pubitemid 27407509)
    • (1997) Investigative Ophthalmology and Visual Science , vol.38 , Issue.10 , pp. 1911-1921
    • Benedek, G.B.1
  • 3
    • 0017059827 scopus 로고
    • Spectroscopic evaluation and classification of the normal, aging, and cataractous lens
    • Lerman, S. & Borkman, R. Spectroscopic evaluation and classification of the normal, aging, and cataractous lens. Ophthalmic. Res. 8, 335-& (1976).
    • (1976) Ophthalmic. Res , vol.8 , pp. 335
    • Lerman, S.1    Borkman, R.2
  • 4
    • 0024436383 scopus 로고
    • Distribution of two metabolically related fluorophors in human lens measured by laser microprobe
    • DOI 10.1016/0014-4835(89)90089-4
    • Yu, N. T., Barron, B. C. & Kuck, J. F. R. Distribution of two metabolically related fluorophors in human lens measured by laser microprobe. Exp. Eye. Res. 49, 189-194 (1989). (Pubitemid 19231040)
    • (1989) Experimental Eye Research , vol.49 , Issue.2 , pp. 189-194
    • Yu, N.-T.1    Barron, B.C.2    Kuck Jr., J.F.R.3
  • 5
    • 0030789317 scopus 로고    scopus 로고
    • Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens
    • Palme, S., Slingsby, C. & Jaenicke, R. Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens. Protein Sci. 6, 1529-1536 (1997).
    • (1997) Protein Sci , vol.6 , pp. 1529-1536
    • Palme, S.1    Slingsby, C.2    Jaenicke, R.3
  • 6
    • 33947723561 scopus 로고    scopus 로고
    • Mutation of interfaces in domain-swapped human βB2-crystallin
    • DOI 10.1110/ps.062659107
    • Smith,M. A., Bateman, O. A., Jaenicke, R. & Slingsby, C. Mutation of interfaces in domain-swapped human beta B2-crystallin. Protein Sci. 16, 615-625 (2007). (Pubitemid 46506990)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 615-625
    • Smith, M.A.1    Bateman, O.A.2    Jaenicke, R.3    Slingsby, C.4
  • 7
    • 0035473032 scopus 로고    scopus 로고
    • Photo-oxidation of proteins and its role in cataractogenesis
    • DOI 10.1016/S1011-1344(01)00208-1, PII S1011134401002081
    • Davies, M. J. & Truscott, R. J. W. Photo-oxidation of proteins and its role in cataractogenesis. J. Photoch. Photobio. B 63, 114-125 (2001). (Pubitemid 33040729)
    • (2001) Journal of Photochemistry and Photobiology B: Biology , vol.63 , Issue.1-3 , pp. 114-125
    • Davies, M.J.1    Truscott, R.J.W.2
  • 8
    • 0021344070 scopus 로고
    • Photochemistry of proteins-A review
    • Grossweiner, L. I. Photochemistry of proteins-A review. Curr. Eye. Res. 3, 137-144 (1984).
    • (1984) Curr. Eye. Res , vol.3 , pp. 137-144
    • Grossweiner, L.I.1
  • 9
    • 0036043869 scopus 로고    scopus 로고
    • A review of the epidemiologic evidence linking ultraviolet radiation and cataracts
    • McCarty, C. A. & Taylor, H. R. A review of the epidemiologic evidence linking ultraviolet radiation and cataracts. Dev. Ophthalmol. 35, 21-31 (2002).
    • (2002) Dev. Ophthalmol , vol.35 , pp. 21-31
    • McCarty, C.A.1    Taylor, H.R.2
  • 12
    • 0036047427 scopus 로고    scopus 로고
    • High prevalence of nuclear cataract in the population of tropical and subtropical areas
    • Sasaki, H. et al. High prevalence of nuclear cataract in the population of tropical and subtropical areas. Dev. Ophthalmol. 35, 60-69 (2002).
    • (2002) Dev. Ophthalmol , vol.35 , pp. 60-69
    • Sasaki, H.1
  • 15
    • 66049087099 scopus 로고    scopus 로고
    • Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human gamma D-and gamma S-Crystallins: The gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage
    • Chen, J., Callis, P. R. & King, J. Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human gamma D-and gamma S-Crystallins: The gamma-Crystallin Fold MayHave Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage. Biochemistry (Mosc). 48, 3708-3716 (2009).
    • (2009) Biochemistry (Mosc) , vol.48 , pp. 3708-3716
    • Chen, J.1    Callis, P.R.2    King, J.3
  • 16
    • 33749005139 scopus 로고    scopus 로고
    • Mechanism of the highly efficient quenching of tryptophan fluorescence in human γD-crystallin
    • DOI 10.1021/bi060988v
    • Chen, J., Flaugh, S. L., Callis, P. R. & King, J. Mechanism of the highly efficient quenching of tryptophan fluorescence in human gamma D-crystallin. Biochemistry (Mosc). 45, 11552-11563 (2006). (Pubitemid 44454003)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11552-11563
    • Chen, J.1    Flaugh, S.L.2    Callis, P.R.3    King, J.4
  • 17
    • 53249098600 scopus 로고    scopus 로고
    • Mechanismof the efficient tryptophan fluorescence quenching in human gamma D-crystallin studied by time-resolved fluorescence
    • Chen, J., Toptygin, D., Brand, L. & King, J. Mechanismof the efficient tryptophan fluorescence quenching in human gamma D-crystallin studied by time-resolved fluorescence. Biochemistry (Mosc). 47, 10705-10721 (2008).
    • (2008) Biochemistry (Mosc) , vol.47 , pp. 10705-10721
    • Chen, J.1    Toptygin, D.2    Brand, L.3    King, J.4
  • 19
    • 35648932100 scopus 로고    scopus 로고
    • Post-translational modifications in the nuclear region of young, aged, and cataract human lenses
    • DOI 10.1021/pr070138h
    • Hains, P. G. & Truscott, R. J. W. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J. Proteome Res. 6, 3935-3943 (2007). (Pubitemid 350032557)
    • (2007) Journal of Proteome Research , vol.6 , Issue.10 , pp. 3935-3943
    • Hains, P.G.1    Truscott, R.J.W.2
  • 20
    • 0032731157 scopus 로고    scopus 로고
    • Human lens coloration and aging: Evidence for crystallin modification by the major ultraviolet filter, 3-hydroxy-kynurenine O-β-D-glucoside
    • Hood, B. D., Garner, B. & Truscott, R. J. W. Human lens coloration and aging-Evidence for crystallin modification by the major ultraviolet filter, 3-hydroxykynurenine O-beta-D-glucoside. J. Biol. Chem. 274, 32547-32550 (1999). (Pubitemid 129535278)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32547-32550
    • Hood, B.D.1    Garner, B.2    Truscott, R.J.W.3
  • 21
    • 34447644956 scopus 로고    scopus 로고
    • Protein-bound and free UV filters in cataract lenses. The concentration of UV filters is much lower than in normal lenses
    • DOI 10.1016/j.exer.2007.04.004, PII S0014483507001108
    • Korlimbinis, A., Aquilina, J. A. & Truscott, R. J. W. Protein-bound and free UV filters in cataract lenses. The concentration of UV filters is much lower than in normal lenses. Exp. Eye. Res. 85, 219-225 (2007). (Pubitemid 47087797)
    • (2007) Experimental Eye Research , vol.85 , Issue.2 , pp. 219-225
    • Korlimbinis, A.1    Aquilina, J.A.2    Truscott, R.J.W.3
  • 22
    • 6944225329 scopus 로고    scopus 로고
    • Lenticular levels of amino acids and free UV filters differ significantly between normals and cataract patients
    • DOI 10.1167/iovs.04-0178
    • Streete, I. M., Jamie, J. F. & Truscott, R. J. W. Lenticular levels of amino acids and free UV filters differ significantly between normals and cataract patients. Invest. Ophthalmol. Vis. Sci. 45, 4091-4098 (2004). (Pubitemid 39411165)
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , Issue.11 , pp. 4091-4098
    • Streete, I.M.1    Jamie, J.F.2    Truscott, R.J.W.3
  • 23
    • 1542637050 scopus 로고    scopus 로고
    • Protein-bound kynurenine decreases with the progression of age-related nuclear cataract
    • DOI 10.1167/iovs.03-0558
    • Vazquez, S., Parker, N. R., Sheil, M. & Truscott, R. J. W. Protein-bound kynurenine decreases with the progression of age-related nuclear cataract. Invest. Ophthalmol. Vis. Sci. 45, 879-883 (2004). (Pubitemid 38868386)
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , Issue.3 , pp. 879-883
    • Vazquez, S.1    Parker, N.R.2    Sheil, M.3    Truscott, R.J.W.4
  • 24
    • 0028225850 scopus 로고
    • Ultraviolet radiation and cataract: A review of the epidemiological evidence
    • Dolin, P. J. Ultraviolet radiation and cataract: a review of the epidemiological evidence. Br. J. Ophthalmol. 78, 478-482 (1994). (Pubitemid 24186288)
    • (1994) British Journal of Ophthalmology , vol.78 , Issue.6 , pp. 478-482
    • Dolin, P.J.1
  • 25
    • 77649268586 scopus 로고    scopus 로고
    • Tryptophan and kynurenine levels in lenses of Wistar and accelerated-senescence OXYS rats
    • Snytnikova, O. A. et al. Tryptophan and kynurenine levels in lenses of Wistar and accelerated-senescence OXYS rats. Mol. Vis. 15, 2780-2788 (2009).
    • (2009) Mol. Vis , vol.15 , pp. 2780-2788
    • Snytnikova, O.A.1
  • 26
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution X-ray crystal structures of human γD crystallin (1.25 angstrom) and the R58H mutant (1.15 angstrom) associated with aculeiform cataract
    • DOI 10.1016/S0022-2836(03)00375-9
    • Basak, A. et al. High-resolution X-ray crystal structures of human gamma D crystallin (1.25 angstrom) and the R58H mutant (1.15 angstrom) associated with aculeiform cataract. J. Mol. Biol. 328, 1137-1147 (2003). (Pubitemid 36506879)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.5 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3    Pande, A.4    Asherie, N.5    Ogun, O.6    Benedek, G.B.7    Pande, J.8
  • 27
    • 3342948291 scopus 로고    scopus 로고
    • Probing folding and fluorescence quenching in human γD crystallin Greek key domains using triple tryptophan mutant proteins
    • DOI 10.1110/ps.04627004
    • Kosinski-Collins, M. S., Flaugh, S. L. & King, J. Probing folding and fluorescence quenching in human gamma D crystallin Greek key domains using triple tryptophan mutant proteins. Protein Sci. 13, 2223-2235 (2004). (Pubitemid 38989625)
    • (2004) Protein Science , vol.13 , Issue.8 , pp. 2223-2235
    • Kosinski-Collins, M.S.1    Flaugh, S.L.2    King, J.3
  • 28
    • 75149175314 scopus 로고    scopus 로고
    • Beta-strand interactions at the domain interface critical for the stability of human lens gamma D-crystallin
    • Das, P., King, J. A. & Zhou, R. beta-strand interactions at the domain interface critical for the stability of human lens gamma D-crystallin. Protein Sci. 19, 131-140 (2010).
    • (2010) Protein Sci , vol.19 , pp. 131-140
    • Das, P.1    King, J.A.2    Zhou, R.3
  • 29
    • 79960584453 scopus 로고    scopus 로고
    • Aggregation of gamma-crystallins associated with human cataracts via domain swapping at the C-terminal beta-strands
    • Das, P., King, J. A. & Zhou, R. H. Aggregation of gamma-crystallins associated with human cataracts via domain swapping at the C-terminal beta-strands. Proc. Natl. Acad. Sci. U. S. A. 108, 10514-10519 (2011).
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 10514-10519
    • Das, P.1    King, J.A.2    Zhou, R.H.3
  • 30
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation
    • DOI 10.1110/ps.0225503
    • Kosinski-Collins, M. S. & King, J. In vitro unfolding, refolding, and polymerization of human gamma D crystallin, a protein involved in cataract formation. Protein Sci. 12, 480-490 (2003). (Pubitemid 36241106)
    • (2003) Protein Science , vol.12 , Issue.3 , pp. 480-490
    • Kosinski-Collins, M.S.1    King, J.2
  • 31
    • 14144250992 scopus 로고    scopus 로고
    • Contributions of hydrophobic domain interface interactions to the folding and stability of human γD-crystallin
    • DOI 10.1110/ps.041111405
    • Flaugh, S. L., Kosinski-Collins, M. S. & King, J. Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaDcrystallin. Protein Sci. 14, 569-581 (2005). (Pubitemid 40283895)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 569-581
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 32
    • 23644457960 scopus 로고    scopus 로고
    • Interdomain side-chain interactions in human γD crystallin influencing folding and stability
    • DOI 10.1110/ps.051460505
    • Flaugh, S. L., Kosinski-Collins, M. S. & King, J. Interdomain side-chain interactions in human gamma D crystallin influencing folding and stability. Protein Sci. 14, 2030-2043 (2005). (Pubitemid 41132368)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2030-2043
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 33
    • 33750078696 scopus 로고    scopus 로고
    • Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding
    • DOI 10.1074/jbc.M603882200
    • Flaugh, S. L., Mills, I. A. & King, J. Glutamine deamidation destabilizes human gamma D-crystallin and lowers the kinetic barrier to unfolding. J. Biol. Chem. 281, 30782-30793 (2006). (Pubitemid 44582133)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30782-30793
    • Flaugh, S.L.1    Mills, I.A.2    King, J.3
  • 35
    • 4644236471 scopus 로고    scopus 로고
    • Hydrophobic collapse in multidomain protein folding
    • DOI 10.1126/science.1101176
    • Zhou, R. H., Huang, X. H., Margulis, C. J. & Berne, B. J. Hydrophobic collapse in multidomain protein folding. Science 305, 1605-1609 (2004). (Pubitemid 39296352)
    • (2004) Science , vol.305 , Issue.5690 , pp. 1605-1609
    • Zhou, R.1    Huang, X.2    Margulis, C.J.3    Berne, B.J.4
  • 36
    • 77953502244 scopus 로고    scopus 로고
    • Dewetting transitions in protein cavities
    • Young, T. et al. Dewetting transitions in protein cavities. Proteins. 78, 1856-1869 (2010).
    • (2010) Proteins , vol.78 , pp. 1856-1869
    • Young, T.1
  • 38
    • 67449084506 scopus 로고    scopus 로고
    • Annual Review of Physical Chemistry Annual Reviews
    • Berne, B. J., Weeks, J. D. & Zhou, R. H. In Annu. Rev. Phys. Chem. Vol. 60 Annual Review of Physical Chemistry 85-103 (Annual Reviews, 2009).
    • (2009) Annu. Rev. Phys. Chem , vol.60 , pp. 85-103
    • Berne, B.J.1    Weeks, J.D.2    Zhou, R.H.3
  • 39
    • 50249168222 scopus 로고    scopus 로고
    • Role of water in mediating the assembly of Alzheimer amyloidbeta a beta 16-22 protofilaments
    • Krone, M. G. et al. Role of water in mediating the assembly of Alzheimer amyloidbeta a beta 16-22 protofilaments. J. Am. Chem. Soc. 130, 11066-11072 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 11066-11072
    • Krone, M.G.1
  • 40
    • 80053116334 scopus 로고    scopus 로고
    • Dewetting Transitions in the Self-Assembly of Two Amyloidogenic beta-Sheets and the Importance of Matching Surfaces
    • Yang, Z. X., Shi, B. Y., Lu, H. J., Xiu, P. & Zhou, R. H. Dewetting Transitions in the Self-Assembly of Two Amyloidogenic beta-Sheets and the Importance of Matching Surfaces. J. Phys. Chem. B 115, 11137-11144 (2011).
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11137-11144
    • Yang, Z.X.1    Shi, B.Y.2    Lu, H.J.3    Xiu, P.4    Zhou, R.H.5
  • 41
    • 24344448662 scopus 로고    scopus 로고
    • Observation of a dewetting transition in the collapse of the melittin tetramer
    • DOI 10.1038/nature03926, PII N03926
    • Liu, P., Huang, X., Zhou, R. & Berne, B. J. Observation of a dewetting transition in the collapse of the melittin tetramer. Nature 437, 159-162 (2005). (Pubitemid 41613444)
    • (2005) Nature , vol.437 , Issue.7055 , pp. 159-162
    • Liu, P.1    Huang, X.2    Zhou, R.3    Berne, B.J.4
  • 42
    • 33846829720 scopus 로고    scopus 로고
    • A Tightly Packed Hydrophobic Cluster Directs the Formation of an Off-pathway Sub-millisecond Folding Intermediate in the α Subunit of Tryptophan Synthase, a TIM Barrel Protein
    • DOI 10.1016/j.jmb.2006.12.005, PII S0022283606016640
    • Wu, Y., Vadrevu, R., Kathuria, S., Yang, X. & Matthews, C. R. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. J. Mol. Biol. 366, 1624-1638 (2007). (Pubitemid 46215600)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.5 , pp. 1624-1638
    • Wu, Y.1    Vadrevu, R.2    Kathuria, S.3    Yang, X.4    Matthews, C.R.5
  • 43
    • 33847308554 scopus 로고    scopus 로고
    • Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography
    • DOI 10.1016/j.jmb.2006.12.021, PII S0022283606016962
    • Collins, M. D., Quillin, M. L., Hummer, G., Matthews, B. W. & Gruner, S. M. Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography. J. Mol. Biol. 367, 752-763 (2007). (Pubitemid 46330369)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.3 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 44
    • 43049122273 scopus 로고    scopus 로고
    • Annual Review of Physical Chemistry Annual Reviews
    • Rasaiah, J. C., Garde, S. & Hummer, G. In Annu. Rev. Phys. Chem. Vol. 59 Annual Review of Physical Chemistry 713-740 (Annual Reviews, 2008).
    • (2008) Annu. Rev. Phys. Chem , vol.59 , pp. 713-740
    • Rasaiah, J.C.1    Garde, S.2    Hummer, G.3
  • 46
    • 39749155117 scopus 로고    scopus 로고
    • Water penetration in the low and high pressure native states of ubiquitin
    • DOI 10.1002/prot.21562
    • Day, R. & Garcia, A. E. Water penetration in the low and high pressure native states of ubiquitin. Proteins. 70, 1175-1184 (2008). (Pubitemid 351304078)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.4 , pp. 1175-1184
    • Day, R.1    Garcia, A.E.2
  • 47
    • 34548209898 scopus 로고    scopus 로고
    • Nanoscale dewetting transition in protein complex folding
    • DOI 10.1021/jp0704923
    • Hua, L., Huang, X. H., Liu, P., Zhou, R. H. & Berne, B. J. Nanoscale dewetting transition in protein complex folding. J. Phys. Chem. B 111, 9069-9077 (2007). (Pubitemid 47317488)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.30 , pp. 9069-9077
    • Hua, L.1    Huang, X.2    Liu, P.3    Zhou, R.4    Berne, B.J.5
  • 48
    • 84860829715 scopus 로고    scopus 로고
    • Cavities determine the pressure unfolding of proteins
    • Roche, J. et al. Cavities determine the pressure unfolding of proteins. Proc. Natl. Acad. Sci. U. S. A. 109, 6945-6950 (2012).
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 6945-6950
    • Roche, J.1
  • 49
    • 68149147539 scopus 로고    scopus 로고
    • Direct evidence for a dry molten globule intermediate during the unfolding of a small protein
    • Jha, S. K. &Udgaonkar, J. B. Direct evidence for a dry molten globule intermediate during the unfolding of a small protein. Proc. Natl. Acad. Sci. U. S. A. 106, 12289-12294 (2009).
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 12289-12294
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 50
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • DOI 10.1038/nature01160
    • Snow, C. D., Nguyen, N., Pande, V. S. & Gruebele, M. Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420, 102-106 (2002). (Pubitemid 35291448)
    • (2002) Nature , vol.420 , Issue.6911 , pp. 102-106
    • Snow, C.D.1    Nguyen, H.2    Pande, V.S.3    Gruebele, M.4
  • 51
    • 79961218875 scopus 로고    scopus 로고
    • Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments
    • Beauchamp, K. A., Ensign, D. L., Das, R. & Pande, V. S. Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments. Proc. Natl. Acad. Sci. U. S. A. 108, 12734-12739 (2011).
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 12734-12739
    • Beauchamp, K.A.1    Ensign, D.L.2    Das, R.3    Pande, V.S.4
  • 52
    • 84862180145 scopus 로고    scopus 로고
    • Mechanism of enhanced mechanical stability of a minimal RNA kissing complex elucidated by nonequilibrium molecular dynamics simulations
    • Chen, A. A. & Garcia, A. E. Mechanism of enhanced mechanical stability of a minimal RNA kissing complex elucidated by nonequilibrium molecular dynamics simulations. Proc. Natl. Acad. Sci. U. S. A. 109, E1530-E1539 (2012).
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109
    • Chen, A.A.1    Garcia, A.E.2
  • 53
    • 58149512801 scopus 로고    scopus 로고
    • Random walk in orthogonal space to achieve efficient free-energy simulation of complex systems
    • Zheng, L. Q., Chen, M. G. & Yang, W. Random walk in orthogonal space to achieve efficient free-energy simulation of complex systems. Proc. Natl. Acad. Sci. U. S. A. 105, 20227-20232 (2008).
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 20227-20232
    • Zheng, L.Q.1    Chen, M.G.2    Yang, W.3
  • 54
    • 79956370148 scopus 로고    scopus 로고
    • Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins
    • Liu, Z. X., Reddy, G., O'Brien, E. P. & Thirumalai, D. Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins. Proc. Natl. Acad. Sci. U. S. A. 108, 7787-7792 (2011).
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 7787-7792
    • Liu, Z.X.1    Reddy, G.2    O'Brien, E.P.3    Thirumalai, D.4
  • 55
    • 33645519597 scopus 로고    scopus 로고
    • A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids
    • Grossfield, A., Feller, S. E. & Pitman, M. C. A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids. Proc. Natl. Acad. Sci. U. S. A. 103, 4888-4893 (2006).
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 4888-4893
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 59
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks, B. R. et al. CHARMM: the biomolecular simulation program. J. Comput. Chem. 30, 1545-1614 (2009).
    • (2009) J. Comput. Chem , vol.30 , pp. 1545-1614
    • Brooks, B.R.1
  • 60
    • 0000843443 scopus 로고    scopus 로고
    • A position dependent friction model for solution reactions in the high friction regime: Proton transfer in triosephosphate isomerase (TIM)
    • Neria, E.&Karplus, M.Aposition dependent friction model for solution reactions in the high friction regime: Proton transfer in triosephosphate isomerase (TIM). J. Chem. Phys. 105, 10812-10818 (1996). (Pubitemid 126748021)
    • (1996) Journal of Chemical Physics , vol.105 , Issue.24 , pp. 10812-10818
    • Neria, E.1    Karplus, M.2
  • 62
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An NlogN method for Ewald sums in large systems
    • Darden, T. A., York, D. M. & Pedersen, L. G. Particle mesh Ewald: An NlogN method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092 (1993).
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.