메뉴 건너뛰기




Volumn 10, Issue 6, 2009, Pages 1469-1477

Desiccation induced structural alterations in a 66-amino acid fragment of an anhydrobiotic nematode late embryogenesis abundant (LEA) protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID FRAGMENTS; ANHYDROBIOSIS; AQUEOUS SOLUTIONS; ELECTROSTATIC INTERACTIONS; HAIRPIN-LIKE; HYDROGEN BONDING INTERACTIONS; LATE EMBRYOGENESIS ABUNDANT PROTEINS; LEA PROTEIN; LENNARD-JONES INTERACTION; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN FUNCTIONS; PROTEIN STRUCTURES; RANDOM COIL; STRUCTURAL ALTERATIONS; STRUCTURAL FORMATION; VAN DER WAALS INTERACTIONS; WATER DEFICITS;

EID: 67049098975     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm9002688     Document Type: Article
Times cited : (30)

References (70)
  • 2
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis: Plant desiccation gene found in a nematode
    • Browne, J.; Tunnacliffe, A.; Burnell, A. Anhydrobiosis: plant desiccation gene found in a nematode. Nature 2002, 416 (6876), 38.
    • (2002) Nature , vol.416 , Issue.6876 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 3
    • 0033282707 scopus 로고    scopus 로고
    • Desiccation survival of parasitic nematodes
    • Perry, R. N. Desiccation survival of parasitic nematodes. Parasitology 1999, 119, S19-30.
    • (1999) Parasitology , vol.119
    • Perry, R.N.1
  • 5
    • 67049161039 scopus 로고    scopus 로고
    • Stabilization of dry mammalian cells: Lessons from nature
    • Crowe, J. H.; Crowe, L. M.; Tablin, F. Stabilization of dry mammalian cells: Lessons from nature. Integr. Comp. Biol. 2004, 44 (6), 542-1542
    • (2004) Integr. Comp. Biol. , vol.44 , Issue.6 , pp. 542-1542
    • Crowe, J.H.1    Crowe, L.M.2    Tablin, F.3
  • 6
    • 0033973790 scopus 로고    scopus 로고
    • Preservation of mammalian cells - Learning nature's tricks
    • DOI 10.1038/72580
    • Crowe, J. H.; Crowe, L. M. Preservation of mammalian cells-learning nature's tricks. Nat. Biotechnol. 2000, 18 (2), 145-146 (Pubitemid 30091168)
    • (2000) Nature Biotechnology , vol.18 , Issue.2 , pp. 145-146
    • Crowe, J.H.1    Crowe, L.M.2
  • 8
    • 40749146436 scopus 로고    scopus 로고
    • The LEA proteins and trehalose loving couple: A step forward in anhydrobiotic engineering
    • Iturriaga, G. The LEA proteins and trehalose loving couple: a step forward in anhydrobiotic engineering. Biochem. J. 2008, 410 (2), 1-2.
    • (2008) Biochem. J. , vol.410 , Issue.2 , pp. 1-2
    • Iturriaga, G.1
  • 9
    • 35748972953 scopus 로고    scopus 로고
    • Desiccation response of mammalian cells: Anhydrosignaling
    • Huang, Z.; Tunnacliffe, A. Desiccation response of mammalian cells: anhydrosignaling. Methods Enzymol. 2007, 428, 269-277
    • (2007) Methods Enzymol. , vol.428 , pp. 269-277
    • Huang, Z.1    Tunnacliffe, A.2
  • 10
    • 0036188985 scopus 로고    scopus 로고
    • Anhydrobiotic engineering of bacterial and mammalian cells: Is intracellular trehalose sufficient?
    • Tunnacliffe, A.; Garcia de Castro, A.; Manzanera, M. Anhydrobiotic engineering of bacterial and mammalian cells: is intracellular trehalose sufficient. Cryobiology 2001, 43 (2), 124-132 (Pubitemid 33780251)
    • (2001) Cryobiology , vol.43 , Issue.2 , pp. 124-132
    • Tunnacliffe, A.1    De Castro, A.G.2    Manzanera, M.3
  • 12
    • 0019874708 scopus 로고
    • Developmental biochemistry of cottonseed embryogenesis and germination: Changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis
    • Dure, L., 3rd.; Greenway, S. C.; Galau, G. A. Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis. Biochemistry 1981, 20 (14), 4162-4168
    • (1981) Biochemistry , vol.20 , Issue.14 , pp. 4162-4168
    • Dure III, L.1    Greenway, S.C.2    Galau, G.A.3
  • 14
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • DOI 10.1042/BJ20041931
    • Goyal, K.; Walton, L. J.; Tunnacliffe, A. LEA proteins prevent protein aggregation due to water stress. Biochem. J. 2005, 388 (Pt 1), 151-157 (Pubitemid 40732942)
    • (2005) Biochemical Journal , vol.388 , Issue.1 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 15
    • 2942549269 scopus 로고    scopus 로고
    • LEAping to conclusions: A computational reanalysis of late embryogenesis abundant proteins and their possible roles
    • Wise, M. J. LEAping to conclusions: A computational reanalysis of late embryogenesis abundant proteins and their possible roles. BMC Bioinf. 2003, 4, -.
    • (2003) BMC Bioinf. , vol.4
    • Wise, M.J.1
  • 16
    • 17444426801 scopus 로고    scopus 로고
    • Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying
    • DOI 10.1104/pp.104.052480
    • Grelet, J.; Benamar, A.; Teyssier, E.; Avelange-Macherel, M. H.; Grunwald, D.; Macherel, D. Identification in pea seed mitochondria of a late-embryogenesis abundant protein able to protect enzymes from drying. Plant Physiol. 2005, 137 (1), 157-167. (Pubitemid 43034298)
    • (2005) Plant Physiology , vol.137 , Issue.1 , pp. 157-167
    • Grelet, J.1    Benamar, A.2    Teyssier, E.3    Avelange-Macherel, M.-H.4    Grunwald, D.5    Macherel, D.6
  • 18
    • 22544488409 scopus 로고    scopus 로고
    • Dehydration-regulated processing of late embryogenesis abundant protein in a desiccation-tolerant nematode
    • DOI 10.1016/j.febslet.2005.06.036, PII S0014579305007672
    • Goyal, K.; Pinelli, C.; Maslen, S. L.; Rastogi, R. K.; Stephens, E.; Tunnacliffe, A. Dehydration-regulated processing of late embryogenesis abundant protein in a desiccation-tolerant nematode. FEBS Lett. 2005, 579 (19), 4093-4098 (Pubitemid 41021796)
    • (2005) FEBS Letters , vol.579 , Issue.19 , pp. 4093-4098
    • Goyal, K.1    Pinelli, C.2    Maslen, S.L.3    Rastogi, R.K.4    Stephens, E.5    Tunnacliffe, A.6
  • 20
    • 0742323272 scopus 로고    scopus 로고
    • POPP the question: What do LEA proteins do?
    • DOI 10.1016/j.tplants.2003.10.012
    • Wise, M. J.; Tunnacliffe, A. POPP the question: what do LEA proteins do. Trends Plant Sci. 2004, 9 (1), 13-17 (Pubitemid 38157641)
    • (2004) Trends in Plant Science , vol.9 , Issue.1 , pp. 13-17
    • Wise, M.J.1    Tunnacliffe, A.2
  • 21
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • DOI 10.1007/s00114-007-0254-y
    • Tunnacliffe, A.; Wise, M. J. The continuing conundrum of the LEA proteins. Naturwissenschaften 2007, 94 (10), 791-812. (Pubitemid 47367664)
    • (2007) Naturwissenschaften , vol.94 , Issue.10 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 23
    • 0031195261 scopus 로고    scopus 로고
    • Cytoplasmic vitrification and survival of anhydrobiotic organisms
    • DOI 10.1016/S0300-9629(96)00271-X, PII S030096299600271X
    • Sun, W. Q.; Leopold, A. C. Cytoplasmic vitrification acid survival of anhydrobiotic organisms. Comp. Biochem. Physiol., Part A: Mol. Integr. Physiol. 1997, 117 (3), 327-333. (Pubitemid 27236695)
    • (1997) Comparative Biochemistry and Physiology - a Physiology , vol.117 , Issue.3 , pp. 327-333
    • Sun, W.Q.1    Leopold, A.C.2
  • 25
    • 24144463133 scopus 로고    scopus 로고
    • A putative LEA protein, but no trehalose, is present in anhydrobiotic bdelloid rotifers
    • DOI 10.1007/s10750-005-4239-6
    • Tunnacliffe, A.; Lapinski, J.; McGee, B. A putative LEA protein, but no trehalose, is present in anhydrobiotic bdelloid rotifers. Hydrobiologia 2005, 546, 315-321. (Pubitemid 41239968)
    • (2005) Hydrobiologia , vol.546 , Issue.1 , pp. 315-321
    • Tunnacliffe, A.1    Lapinski, J.2    McGee, B.3
  • 26
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • DOI 10.1074/jbc.M212007200
    • Goyal, K.; Tisi, L.; Basran, A.; Browne, J.; Burnell, A.; Zurdo, J.; Tunnacliffe, A. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 2003, 278 (15), 12977-12984. (Pubitemid 36800064)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6    Tunnacliffe, A.7
  • 27
    • 0027564435 scopus 로고
    • A repeating 11-mer amino acid motif and plant desiccation
    • Dure, L., 3rd. A repeating 11-mer amino acid motif and plant desiccation. Plant J. 1993, 3 (3), 363-369 (Pubitemid 223002519)
    • (1993) Plant Journal , vol.3 , Issue.3 , pp. 363-369
    • Dure III, L.1
  • 28
    • 1842296918 scopus 로고    scopus 로고
    • Purification, characterization, and structural analysis of a plant low-temperature-induced protein
    • Boothe, J. G.; Sonnichsen, F. D.; deBeus, M. D.; JohnsonFlanagan, A. M. Purification, characterization, and structural analysis of a plant low-temperature-induced protein. Plant Physiol. 1997, 113 (2), 367-376.
    • (1997) Plant Physiol. , vol.113 , Issue.2 , pp. 367-376
    • Boothe, J.G.1    Sonnichsen, F.D.2    DeBeus, M.D.3    JohnsonFlanagan, A.M.4
  • 29
    • 0036006031 scopus 로고    scopus 로고
    • Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean
    • DOI 10.1104/pp.010521
    • Soulages, J. L.; Kim, K.; Walters, C.; Cushman, J. C. Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. Plant Physiol. 2002, 128 (3), 822-832. (Pubitemid 34243820)
    • (2002) Plant Physiology , vol.128 , Issue.3 , pp. 822-832
    • Soulages, J.L.1    Kim, K.2    Walters, C.3    Cushman, J.C.4
  • 30
    • 0029805280 scopus 로고    scopus 로고
    • The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state
    • Lisse, T.; Bartels, D.; Kalbitzer, H. R.; Jaenicke, R. The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. Biol. Chem. 1996, 377 (9), 555-561. (Pubitemid 26383818)
    • (1996) Biological Chemistry , vol.377 , Issue.9 , pp. 555-561
    • Lisse, T.1    Bartels, D.2    Kalbitzer, H.R.3    Jaenicke, R.4
  • 31
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- And temperature-induced protein aggregation
    • Dong, A.; Prestrelski, S. J.; Allison, S. D.; Carpenter, J. F. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharm. Sci. 1995, 84 (4), 415-424
    • (1995) J. Pharm. Sci. , vol.84 , Issue.4 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 32
    • 18044380883 scopus 로고    scopus 로고
    • High-temperature unfolding of a trp-cage miniprotein: A molecular dynamics simulation study
    • Seshasayee, A. S. High-temperature unfolding of a trp-cage miniprotein: a molecular dynamics simulation study. Theor. Biol. Med. Modell. 2005, 2, 7.
    • (2005) Theor. Biol. Med. Modell. , vol.2 , pp. 7
    • Seshasayee, A.S.1
  • 34
    • 0026525048 scopus 로고
    • Molecular dynamics simulations of helix denaturation
    • Daggett, V.; Levitt, M. Molecular dynamics simulations of helix denaturation. J. Mol. Biol. 1992, 223 (4), 1121-1138
    • (1992) J. Mol. Biol. , vol.223 , Issue.4 , pp. 1121-1138
    • Daggett, V.1    Levitt, M.2
  • 36
    • 0017474001 scopus 로고
    • Hypothesis about mechanism of protein folding
    • Tanaka, S.; Scheraga, H. A. Hypothesis about mechanism of protein folding. Macromolecules 1977, 10 (2), 291-304.
    • (1977) Macromolecules , vol.10 , Issue.2 , pp. 291-304
    • Tanaka, S.1    Scheraga, H.A.2
  • 39
  • 40
    • 33744827386 scopus 로고    scopus 로고
    • Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology
    • DOI 10.1016/j.physa.2006.01.062, PII S0378437106001014
    • Higman, V. A.; Greene, L. H. Elucidation of conserved long-range interaction networks in proteins and their significance in determining protein topology. Phys. A (Amsterdam, Neth.) 2006, 368 (2), 595-606. (Pubitemid 43831508)
    • (2006) Physica A: Statistical Mechanics and Its Applications , vol.368 , Issue.2 , pp. 595-606
    • Higman, V.A.1    Greene, L.H.2
  • 41
    • 0031926859 scopus 로고    scopus 로고
    • Structural cassette mutagenesis in a de novo designed protein: Proof of a novel concept for examining protein folding and stability
    • DOI 10.1002/(SICI)1097-0282(1998)47:1<101::AID-BIP11>3.0.CO;2-L
    • Kwok, S. C.; Tripet, B.; Man, J. H.; Chana, M. S.; Lavigne, P.; Mant, C. T.; Hodges, R. S. Structural cassette mutagenesis in a de novo designed protein: proof of a novel concept for examining protein folding and stability. Biopolymers 1998, 47 (1), 101-123 (Pubitemid 28354761)
    • (1998) Biopolymers - Peptide Science Section , vol.47 , Issue.1 , pp. 101-123
    • Kwok, S.C.1    Tripet, B.2    Man, J.H.3    Chana, M.S.4    Lavigne, P.5    Mant, C.T.6    Hodges, R.S.7
  • 42
    • 0142184268 scopus 로고    scopus 로고
    • How can free energy component analysis explain the difference in protein stability caused by amino acid substitutions? Effect of three hydrophobic mutations at the 56th residue on the stability of human lysozyme
    • Funahashi, J.; Sugita, Y.; Kitao, A.; Yutani, K. How can free energy component analysis explain the difference in protein stability caused by amino acid substitutions? Effect of three hydrophobic mutations at the 56th residue on the stability of human lysozyme. Protein Eng. 2003, 16 (9), 665-671 (Pubitemid 37314394)
    • (2003) Protein Engineering , vol.16 , Issue.9 , pp. 665-671
    • Funahashi, J.1    Sugita, Y.2    Kitao, A.3    Yutani, K.4
  • 43
    • 33747198476 scopus 로고    scopus 로고
    • The side chain interaction index as a tool for predicting fast-folding elements and the structure and stability of engineered peptides
    • DOI 10.1016/j.ab.2006.06.021, PII S0003269706004453
    • Gehenn, K.; Stege, J.; Reed, J. The side chain interaction index as a tool for predicting fast-folding elements and the structure and stability of engineered peptides. Anal. Biochem. 2006, 356 (1), 12-17 (Pubitemid 44232740)
    • (2006) Analytical Biochemistry , vol.356 , Issue.1 , pp. 12-17
    • Gehenn, K.1    Stege, J.2    Reed, J.3
  • 44
    • 47749136312 scopus 로고    scopus 로고
    • Roles of beta-turns in protein folding: From peptide models to protein engineering
    • Marcelino, A. M. C.; Gierasch, L. M. Roles of beta-turns in protein folding: From peptide models to protein engineering. Biopolymers 2008, 89 (5), 380-391.
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 380-391
    • Marcelino, A.M.C.1    Gierasch, L.M.2
  • 45
    • 47149089463 scopus 로고    scopus 로고
    • Role of structural water molecule in HIV protease-inhibitor complexes: A QM/MM study
    • Suresh, C. H.; Vargheese, A. M.; Vijayalakshmi, K. P.; Mohan, N.; Koga, N. Role of structural water molecule in HIV protease-inhibitor complexes: A QM/MM study. J. Comput. Chem. 2008, 29 (11), 1840-1849.
    • (2008) J. Comput. Chem. , vol.29 , Issue.11 , pp. 1840-1849
    • Suresh, C.H.1    Vargheese, A.M.2    Vijayalakshmi, K.P.3    Mohan, N.4    Koga, N.5
  • 47
    • 28544438211 scopus 로고    scopus 로고
    • Molecular dynamics simulation of barnacle cement
    • DOI 10.1016/j.msea.2005.05.107, PII S092150930500780X
    • Yin, J.; Zhao, Y. P.; Zhu, R. Z. Molecular dynamics simulation of barnacle cement. Mater. Sci. Eng., A 2005, 409 (1-2), 160-166. (Pubitemid 41742299)
    • (2005) Materials Science and Engineering a , vol.409 , Issue.1-2 , pp. 160-166
    • Yin, J.1    Zhao, Y.-P.2    Zhu, R.-Z.3
  • 48
    • 49449124722 scopus 로고
    • Determination of vibrational level spacings of van der Waals molecules from Lennard-Jones potential
    • Shin, H. K. Determination of vibrational level spacings of van der Waals molecules from Lennard-Jones potential. Chem. Phys. Lett. 1977, 47 (2), 225-230.
    • (1977) Chem. Phys. Lett. , vol.47 , Issue.2 , pp. 225-230
    • Shin, H.K.1
  • 49
    • 33748269908 scopus 로고    scopus 로고
    • The thermodynamics of folding of a beta hairpin peptide probed through replica exchange molecular dynamics simulations
    • DOI 10.1007/s00214-005-0041-9
    • Baumketner, A.; Shea, J. E. The thermodynamics of folding of a beta hairpin peptide probed through replica exchange molecular dynamics simulations. Theor. Chem. Acc. 2006, 116 (1-3), 262-273. (Pubitemid 44318430)
    • (2006) Theoretical Chemistry Accounts , vol.116 , Issue.1-3 , pp. 262-273
    • Baumketner, A.1    Shea, J.-E.2
  • 50
    • 34248215206 scopus 로고    scopus 로고
    • On the applicability of mathematical constants and sequences in intermolecular potential energy functions
    • Lim, T. C. On the applicability of mathematical constants and sequences in intermolecular potential energy functions. J. Math. Chem. 2007, 41 (4), 381-391.
    • (2007) J. Math. Chem. , vol.41 , Issue.4 , pp. 381-391
    • Lim, T.C.1
  • 51
    • 0033106945 scopus 로고    scopus 로고
    • A homology modeling method of an icosahedral viral capsid: Inclusion of surrounding protein structures
    • Yoneda, T.; Yoneda, S.; Takayama, N.; Kitazawa, M.; Umeyama, H. A homology modeling method of an icosahedral viral capsid: Inclusion of surrounding protein structures. J. Mol. Graphics Modell. 1999, 17 (2), 114.
    • (1999) J. Mol. Graphics Modell. , vol.17 , Issue.2 , pp. 114
    • Yoneda, T.1    Yoneda, S.2    Takayama, N.3    Kitazawa, M.4    Umeyama, H.5
  • 52
    • 0027185404 scopus 로고
    • A method to configure protein side-chains from the main-chain trace in homology modelling
    • DOI 10.1006/jmbi.1993.1331
    • Eisenmenger, F.; Argos, P.; Abagyan, R. A method to configure protein side-chains from the main-chain trace in homology modeling. J. Mol. Biol. 1993, 231 (3), 849-860. (Pubitemid 23211319)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.3 , pp. 849-860
    • Eisenmenger, F.1    Argos, P.2    Abagyan, R.3
  • 55
    • 57749111581 scopus 로고    scopus 로고
    • Mimicking the plant cell interior under water stress by macromolecular crowding: Disordered dehydrin proteins are highly resistant to structural collapse
    • DOI 10.1104/pp.108.124099
    • Mouillon, J. M.; Eriksson, S. K.; Harryson, P. Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse. Plant Physiol. 2008, 148 (4), 1925-1937. (Pubitemid 352847470)
    • (2008) Plant Physiology , vol.148 , Issue.4 , pp. 1925-1937
    • Mouillon, J.-M.1    Eriksson, S.K.2    Harryson, P.3
  • 56
    • 34547909602 scopus 로고    scopus 로고
    • Assortative mixing in protein contact networks and protein folding kinetics
    • DOI 10.1093/bioinformatics/btm257
    • Bagler, G.; Sinha, S. Assortative mixing in Protein Contact Networks and protein folding kinetics. Bioinformatics 2007, 23 (14), 1760-1767 (Pubitemid 47250308)
    • (2007) Bioinformatics , vol.23 , Issue.14 , pp. 1760-1767
    • Bagler, G.1    Sinha, S.2
  • 57
    • 36749050344 scopus 로고    scopus 로고
    • Repeat-protein folding: New insights into origins of cooperativity, stability, and topology
    • DOI 10.1016/j.abb.2007.08.034, PII S0003986107004511, Highlight Issue: Protein Folding
    • Kloss, E.; Courtemanche, N.; Barrick, D. Repeat-protein folding: New insights into origins of cooperativity, stability, and topology. Arch. Biochem. Biophys. 2008, 469 (1), 83-99. (Pubitemid 350212850)
    • (2008) Archives of Biochemistry and Biophysics , vol.469 , Issue.1 , pp. 83-99
    • Kloss, E.1    Courtemanche, N.2    Barrick, D.3
  • 59
    • 0035425883 scopus 로고    scopus 로고
    • An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase
    • Schuler, L. D.; Daura, X.; Van Gunsteren, W. F. An improved GROMOS96 force field for aliphatic hydrocarbons in the condensed phase. J. Comput. Chem. 2001, 22 (11), 1205-1218.
    • (2001) J. Comput. Chem. , vol.22 , Issue.11 , pp. 1205-1218
    • Schuler, L.D.1    Daura, X.2    Van Gunsteren, W.F.3
  • 60
    • 0034237485 scopus 로고    scopus 로고
    • Molecular dynamics simulation of hen egg white lysozyme: A test of the GROMOS96 force field against nuclear magnetic resonance data
    • Stocker, U.; van Gunsteren, W. F. Molecular dynamics simulation of hen egg white lysozyme: A test of the GROMOS96 force field against nuclear magnetic resonance data. Proteins: Struct., Funct., Genet. 2000, 40 (1), 145-153. (Pubitemid 30368590)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.1 , pp. 145-153
    • Stocker, U.1    Van Gunsteren, W.F.2
  • 63
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An N.Log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald - an N.Log(N) method for Ewald sums in large systems. J. Chem. Phys. 1993, 98 (12), 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , Issue.12 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 66
    • 0003242622 scopus 로고
    • Transport properties computed by linear response through weak coupling to a bath
    • Meyer, M., Pontikis, V., Eds.; Kluwer: Norwell, MA
    • Berendsen, H. J. C. Transport properties computed by linear response through weak coupling to a bath. In Computer Simulations in Material Science; Meyer, M., Pontikis, V., Eds.; Kluwer: Norwell, MA, 1991; pp 139-155.
    • (1991) Computer Simulations in Material Science , pp. 139-155
    • Berendsen, H.J.C.1
  • 67
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure - Pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22 (12), 2577-2637.
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 68
    • 0021097529 scopus 로고
    • How good are predictions of protein secondary structure
    • Kabsch, W.; Sander, C. How good are predictions of protein secondary structure. FEBS Lett. 1983, 155 (2), 179-182.
    • (1983) FEBS Lett. , vol.155 , Issue.2 , pp. 179-182
    • Kabsch, W.1    Sander, C.2
  • 69
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theor. Comput. 2008, 4 (3), 435-447.
    • (2008) J. Chem. Theor. Comput. , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 70
    • 46449113031 scopus 로고    scopus 로고
    • Similar chemistry, but different bond preferences in inter versus intra-protein interactions
    • DOI 10.1002/prot.21960
    • Cohen, M.; Reichmann, D.; Neuvirth, H.; Schreiber, G. Similar chemistry, but different bond preferences in inter versus intra-protein interactions. Proteins: Struct., Funct., Bioinf. 2008, 72 (2), 741-753. (Pubitemid 351928526)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.2 , pp. 741-753
    • Cohen, M.1    Reichmann, D.2    Neuvirth, H.3    Schreiber, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.