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Volumn 7, Issue 10, 2012, Pages

Raman Spectroscopy Adds Complementary Detail to the High-Resolution X-Ray Crystal Structure of Photosynthetic PsbP from Spinacia oleracea

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN CYANOP; PROTEIN PSBP; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 84867174766     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0046694     Document Type: Article
Times cited : (21)

References (61)
  • 1
    • 0033578748 scopus 로고    scopus 로고
    • Raman spectroscopy, the sleeping giant in structural biology, awakes
    • Carey PR, (1999) Raman spectroscopy, the sleeping giant in structural biology, awakes. J Biol Chem 274: 26625-26628.
    • (1999) J Biol Chem , vol.274 , pp. 26625-26628
    • Carey, P.R.1
  • 2
    • 2442668918 scopus 로고    scopus 로고
    • Vibrational spectroscopy and computer modeling of proteins: solving structure of human α1-acid glycoprotein
    • Kopecký V Jr, Ettrich R, Hofbauerová K, Baumruk V, (2004) Vibrational spectroscopy and computer modeling of proteins: solving structure of human α1-acid glycoprotein. Spectrosc-Int J 18: 323-330.
    • (2004) Spectrosc-Int J , vol.18 , pp. 323-330
    • Kopecký Jr., V.1    Ettrich, R.2    Hofbauerová, K.3    Baumruk, V.4
  • 3
    • 3142658015 scopus 로고    scopus 로고
    • Following ligand binding and ligand reactions in proteins via Raman crystallography
    • Carey PR, Dong J, (2004) Following ligand binding and ligand reactions in proteins via Raman crystallography. Biochemistry 43: 8885-8893.
    • (2004) Biochemistry , vol.43 , pp. 8885-8893
    • Carey, P.R.1    Dong, J.2
  • 4
    • 78149444302 scopus 로고    scopus 로고
    • Raman-assisted crystallography suggests a mechanism of X-ray-induced disulfide radical formation and reparation
    • Carpentier P, Royant A, Weik M, Bourgeois D, (2010) Raman-assisted crystallography suggests a mechanism of X-ray-induced disulfide radical formation and reparation. Structure 18: 1410-1419.
    • (2010) Structure , vol.18 , pp. 1410-1419
    • Carpentier, P.1    Royant, A.2    Weik, M.3    Bourgeois, D.4
  • 5
    • 79955846688 scopus 로고    scopus 로고
    • Raman-assisted crystallography of biomolecules at the synchrotron: Instrumentation, methods and applications
    • McGeehan JE, Bourgeois D, Royant A, Carpentier P, (2011) Raman-assisted crystallography of biomolecules at the synchrotron: Instrumentation, methods and applications. Biochim Biophys Acta 1814: 750-759.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 750-759
    • McGeehan, J.E.1    Bourgeois, D.2    Royant, A.3    Carpentier, P.4
  • 6
    • 69749094630 scopus 로고    scopus 로고
    • Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis
    • Lafaye C, Iwema T, Carpentier P, Jullian-Binard C, Kroll JS, et al. (2009) Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis. J Mol Biol 392: 952-966.
    • (2009) J Mol Biol , vol.392 , pp. 952-966
    • Lafaye, C.1    Iwema, T.2    Carpentier, P.3    Jullian-Binard, C.4    Kroll, J.S.5
  • 7
    • 0016389125 scopus 로고
    • Comparison of protein structure in crystals, in lyophilized state, and in solution by laser Raman scattering. 3. α-Lactalbumin
    • Yu N-T, (1974) Comparison of protein structure in crystals, in lyophilized state, and in solution by laser Raman scattering. 3. α-Lactalbumin. J Am Chem Soc 96: 4664-4668.
    • (1974) J Am Chem Soc , vol.96 , pp. 4664-4668
    • Yu, N.-T.1
  • 8
    • 0026773101 scopus 로고
    • Conformations, interactions, and thermostabilities of RNA and proteins in bean pod mottle virus: investigation of solution and crystal structures by laser Raman spectroscopy
    • Li T, Chen Z, Johnson JE, Thomas GJ Jr, (1992) Conformations, interactions, and thermostabilities of RNA and proteins in bean pod mottle virus: investigation of solution and crystal structures by laser Raman spectroscopy. Biochemistry 31: 6673-6682.
    • (1992) Biochemistry , vol.31 , pp. 6673-6682
    • Li, T.1    Chen, Z.2    Johnson, J.E.3    Thomas Jr., G.J.4
  • 9
    • 0024550631 scopus 로고
    • Environmentally induced conformational changes in B-type DNA: comparison of the conformation of the oligonucleotide d(TCGCGAATTCGCG) in solution and in its crystalline complex with the restriction nuclease EcoRI
    • Thomas GA, Kubasek WL, Greene P, Grable J, Rosenberg JM, (1989) Environmentally induced conformational changes in B-type DNA: comparison of the conformation of the oligonucleotide d(TCGCGAATTCGCG) in solution and in its crystalline complex with the restriction nuclease EcoRI. Biochemistry 28: 2001-2009.
    • (1989) Biochemistry , vol.28 , pp. 2001-2009
    • Thomas, G.A.1    Kubasek, W.L.2    Greene, P.3    Grable, J.4    Rosenberg, J.M.5
  • 10
    • 0035853151 scopus 로고    scopus 로고
    • Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy
    • Altose MD, Zheng Y, Dong J, Palfey BA, Carey PR, (2001) Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy. Proc Natl Acad Sci USA 98: 3006-3011.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3006-3011
    • Altose, M.D.1    Zheng, Y.2    Dong, J.3    Palfey, B.A.4    Carey, P.R.5
  • 12
    • 33750061923 scopus 로고    scopus 로고
    • Proline zwitterion dynamics in solution, glass, and crystalline state
    • Kapitán J, Baumruk V, Kopecký V Jr, Pohl R, Bouř P, (2006) Proline zwitterion dynamics in solution, glass, and crystalline state. J Am Chem Soc 128: 13451-13462.
    • (2006) J Am Chem Soc , vol.128 , pp. 13451-13462
    • Kapitán, J.1    Baumruk, V.2    Kopecký Jr., V.3    Pohl, R.4    Bouř, P.5
  • 13
    • 33750941544 scopus 로고    scopus 로고
    • Structure of the ring in drop coating deposited proteins and its implication for Raman spectroscopy of biomolecules
    • Kopecký V Jr, Baumruk V, (2006) Structure of the ring in drop coating deposited proteins and its implication for Raman spectroscopy of biomolecules. Vib Spectrosc 42: 184-187.
    • (2006) Vib Spectrosc , vol.42 , pp. 184-187
    • Kopecký Jr., V.1    Baumruk, V.2
  • 14
    • 0030732736 scopus 로고    scopus 로고
    • Capillary flow as the cause of ring stains from dried liquid drops
    • Deegan RD, Bakajin O, Dupot TF, Huber G, Gel SR, et al. (1997) Capillary flow as the cause of ring stains from dried liquid drops. Nature 389: 827-829.
    • (1997) Nature , vol.389 , pp. 827-829
    • Deegan, R.D.1    Bakajin, O.2    Dupot, T.F.3    Huber, G.4    Gel, S.R.5
  • 15
    • 33646843580 scopus 로고    scopus 로고
    • Validation of the drop coating deposition Raman method for protein analysis
    • Ortiz C, Zhang D, Xie Y, Ribbe AE, Ben-Amotz D, (2006) Validation of the drop coating deposition Raman method for protein analysis. Anal Biochem 353: 157-166.
    • (2006) Anal Biochem , vol.353 , pp. 157-166
    • Ortiz, C.1    Zhang, D.2    Xie, Y.3    Ribbe, A.E.4    Ben-Amotz, D.5
  • 16
    • 0037295369 scopus 로고    scopus 로고
    • Photosystem II: the engine of life
    • Barber J, (2003) Photosystem II: the engine of life. Q Rev Biophys 36: 71-89.
    • (2003) Q Rev Biophys , vol.36 , pp. 71-89
    • Barber, J.1
  • 17
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of photosystem II
    • Seidler A, (1996) The extrinsic polypeptides of photosystem II. Biochim Biophys Acta 1277: 35-60.
    • (1996) Biochim Biophys Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 18
    • 33644855090 scopus 로고    scopus 로고
    • PsbR, a missing link in the assembly of the oxygen-evolving complex of plant photosystem II
    • Suorsa M, Sirpio S, Allahverdiyeva Y, Paakkarinen V, Mamedov F, et al. (2006) PsbR, a missing link in the assembly of the oxygen-evolving complex of plant photosystem II. J Biol Chem 281: 145-150.
    • (2006) J Biol Chem , vol.281 , pp. 145-150
    • Suorsa, M.1    Sirpio, S.2    Allahverdiyeva, Y.3    Paakkarinen, V.4    Mamedov, F.5
  • 19
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of Photosystem II
    • Seidler A, (1996) The extrinsic polypeptides of Photosystem II. Biochim Biophys Acta 1277: 35-60.
    • (1996) Biochim Biophys Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 20
    • 30344437393 scopus 로고    scopus 로고
    • PsbP protein, but not PsbQ protein is essential for the regulation and stabilization of photosystem II in higher plants
    • Ifuku K, Yamamoto Y, Ono TA, Ishihara S, Sato F, (2005) PsbP protein, but not PsbQ protein is essential for the regulation and stabilization of photosystem II in higher plants. Plant Physiol 193: 1175-1184.
    • (2005) Plant Physiol , vol.193 , pp. 1175-1184
    • Ifuku, K.1    Yamamoto, Y.2    Ono, T.A.3    Ishihara, S.4    Sato, F.5
  • 21
    • 23444439654 scopus 로고    scopus 로고
    • Structure and function of the PsbP protein of photosystem II from higher plants
    • Ifuku K, Nakatsu T, Shimamoto R, Yamamoto Y, Ishihara S, et al. (2005) Structure and function of the PsbP protein of photosystem II from higher plants. Photosyn Res 84: 251-255.
    • (2005) Photosyn Res , vol.84 , pp. 251-255
    • Ifuku, K.1    Nakatsu, T.2    Shimamoto, R.3    Yamamoto, Y.4    Ishihara, S.5
  • 22
    • 34548297894 scopus 로고    scopus 로고
    • The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana
    • Yi X, Hargett SR, Liu H, Frankel LK, Bricker TM, (2007) The PsbP protein is required for photosystem II complex assembly/stability and photoautotrophy in Arabidopsis thaliana. J Biol Chem 282: 24833-24841.
    • (2007) J Biol Chem , vol.282 , pp. 24833-24841
    • Yi, X.1    Hargett, S.R.2    Liu, H.3    Frankel, L.K.4    Bricker, T.M.5
  • 23
    • 34249803219 scopus 로고    scopus 로고
    • Oxygen-evolving extrinsic proteins (PsbO, P, Q, R): Bioinformatics and functional analysis
    • De Las Rivas J, Heredia P, Roman A, (2007) Oxygen-evolving extrinsic proteins (PsbO, P, Q, R): Bioinformatics and functional analysis. Biochim Biophys Acta 1767: 575-582.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 575-582
    • de Las Rivas, J.1    Heredia, P.2    Roman, A.3
  • 24
    • 0037177852 scopus 로고    scopus 로고
    • Three dimensional cryo-EM study of extrinsic domains of the oxygen-evolving complex of spinach: assignment of the PsbO protein
    • Nield J, Balsera M, De Las Rivas J, Barber J, (2002) Three dimensional cryo-EM study of extrinsic domains of the oxygen-evolving complex of spinach: assignment of the PsbO protein. J Biol Chem 277: 15006-15012.
    • (2002) J Biol Chem , vol.277 , pp. 15006-15012
    • Nield, J.1    Balsera, M.2    de Las Rivas, J.3    Barber, J.4
  • 25
    • 0041875132 scopus 로고    scopus 로고
    • Electron microscopy in structural studies of photosystem II
    • Bumba L, Vacha FE, (2003) Electron microscopy in structural studies of photosystem II. Photosynth Res 77: 1-19.
    • (2003) Photosynth Res , vol.77 , pp. 1-19
    • Bumba, L.1    Vacha, F.E.2
  • 26
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • Caffarri S, Kouril R, Kerei{dotless}che S, Boekema EJ, Croce R, (2009) Functional architecture of higher plant photosystem II supercomplexes. EMBO J 28: 3052-3063.
    • (2009) EMBO J , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Kereiche, S.3    Boekema, E.J.4    Croce, R.5
  • 27
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A, Witt HT, Kern J, Fromme P, Krauss N, et al. (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409: 739-43.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5
  • 28
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution
    • Kamiya N, Shen JR, (2003) Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc Natl Acad Sci USA 100: 98-102.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 98-102
    • Kamiya, N.1    Shen, J.R.2
  • 29
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II
    • Loll B, Cern J, Saenger W, Zouni A, Biesiadka J, (2005) Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438: 1040-1044.
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Cern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 30
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9 Å resolution and the role of quinones, lipids, channels and chloride
    • Guskov A, Kern J, Gabdullkhakov A, Broser M, Zouni A, et al. (2009) Cyanobacterial photosystem II at 2.9 Å resolution and the role of quinones, lipids, channels and chloride. Nature Struc Mol Biol 16: 334-341.
    • (2009) Nature Struc Mol Biol , vol.16 , pp. 334-341
    • Guskov, A.1    Kern, J.2    Gabdullkhakov, A.3    Broser, M.4    Zouni, A.5
  • 31
    • 57849168295 scopus 로고    scopus 로고
    • Structure, function and evolution of the PsbP protein family in higher plants
    • Ifuku K, Ishihara S, Shimamoto R, Ido K, Sato F, (2008) Structure, function and evolution of the PsbP protein family in higher plants. Photosyn Res 98: 427-437.
    • (2008) Photosyn Res , vol.98 , pp. 427-437
    • Ifuku, K.1    Ishihara, S.2    Shimamoto, R.3    Ido, K.4    Sato, F.5
  • 32
    • 21744439800 scopus 로고    scopus 로고
    • The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region
    • Balsera M, Arellano JB, Revuelta JL, De Las Rivas J, Hermoso JA, (2005) The 1.49 Å resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region. J Mol Biol 350: 1051-1060.
    • (2005) J Mol Biol , vol.350 , pp. 1051-1060
    • Balsera, M.1    Arellano, J.B.2    Revuelta, J.L.3    de Las Rivas, J.4    Hermoso, J.A.5
  • 33
    • 2442543556 scopus 로고    scopus 로고
    • Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
    • Ifuku K, Nakatsu T, Kato H, Sato F, (2004) Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum. EMBO Rep 5: 362-367.
    • (2004) EMBO Rep , vol.5 , pp. 362-367
    • Ifuku, K.1    Nakatsu, T.2    Kato, H.3    Sato, F.4
  • 34
    • 77956154786 scopus 로고    scopus 로고
    • Structure of CyanoP at 2.8 Å: implications for the evolution and function of the PsbP subunit of photosystem II
    • Michoux F, Takasaka K, Boehm M, Nixon P, Murray JW, (2010) Structure of CyanoP at 2.8 Å: implications for the evolution and function of the PsbP subunit of photosystem II. Biochemistry 49: 7411-741.
    • (2010) Biochemistry , vol.49 , pp. 7411-7741
    • Michoux, F.1    Takasaka, K.2    Boehm, M.3    Nixon, P.4    Murray, J.W.5
  • 35
    • 59749085061 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia olerace
    • Kohoutová J, Kuta Smatanová I, Brynda J, Lapkouski M, Revuelta JL, et al. (2009) Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia olerace. Acta Cryst F65: 111-115.
    • (2009) Acta Cryst , vol.F65 , pp. 111-115
    • Kohoutová, J.1    Kuta Smatanová, I.2    Brynda, J.3    Lapkouski, M.4    Revuelta, J.L.5
  • 36
    • 79958002353 scopus 로고    scopus 로고
    • Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex
    • Ifuku K, Ido K, Sato F, (2011) Molecular functions of PsbP and PsbQ proteins in the photosystem II supercomplex. J Photochem Photobiol 104: 158-164.
    • (2011) J Photochem Photobiol , vol.104 , pp. 158-164
    • Ifuku, K.1    Ido, K.2    Sato, F.3
  • 37
    • 84988158466 scopus 로고
    • Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation
    • Miura T, Takeuchi H, Harada I, (1989) Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation. J Raman Spectrosc 20: 667-671.
    • (1989) J Raman Spectrosc , vol.20 , pp. 667-671
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 38
    • 0033616633 scopus 로고    scopus 로고
    • Raman markers of nonaromatic side chains in an α-helix assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val residues of phage fd subunits
    • Overman SA, Thomas GJ Jr, (1999) Raman markers of nonaromatic side chains in an α-helix assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val residues of phage fd subunits. Biochemistry 38: 4018-4027.
    • (1999) Biochemistry , vol.38 , pp. 4018-4027
    • Overman, S.A.1    Thomas Jr., G.J.2
  • 39
    • 18444419164 scopus 로고    scopus 로고
    • Raman spectroscopy of proteins: from peptides to large assemblies
    • Tuma R, (2005) Raman spectroscopy of proteins: from peptides to large assemblies. J Raman Spectrosc 36: 307-319.
    • (2005) J Raman Spectrosc , vol.36 , pp. 307-319
    • Tuma, R.1
  • 42
    • 0022503458 scopus 로고
    • The secondary structure analysis using Raman amide I and amide III spectra
    • Williams RW, (1986) The secondary structure analysis using Raman amide I and amide III spectra. Methods Enzymol 130: 311-331.
    • (1986) Methods Enzymol , vol.130 , pp. 311-331
    • Williams, R.W.1
  • 43
    • 84986759513 scopus 로고
    • Determination of the secondary structure of proteins from the Raman amide I band: the reference intensity profiles method
    • Berjot M, Marx J, Alix AJP, (1987) Determination of the secondary structure of proteins from the Raman amide I band: the reference intensity profiles method. J Raman Spectrosc 18: 289-300.
    • (1987) J Raman Spectrosc , vol.18 , pp. 289-300
    • Berjot, M.1    Marx, J.2    Alix, A.J.P.3
  • 44
    • 0023354464 scopus 로고
    • Raman amide bands of type-II β-turns in cyclo-(VPGVG)3 and poly-(VPGVG), and implications for protein secondary-structure analysis
    • Thomas GJ Jr, Prescott B, Urry DW, (1987) Raman amide bands of type-II β-turns in cyclo-(VPGVG)3 and poly-(VPGVG), and implications for protein secondary-structure analysis. Biopolymers 26: 921-934.
    • (1987) Biopolymers , vol.26 , pp. 921-934
    • Thomas Jr., G.J.1    Prescott, B.2    Urry, D.W.3
  • 45
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG, (1997) The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 46
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comaprison with experimental scales
    • Munoz V, Serrano L, (1994) Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comaprison with experimental scales. Proteins 20: 301-311.
    • (1994) Proteins , vol.20 , pp. 301-311
    • Munoz, V.1    Serrano, L.2
  • 48
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie AGW (1992) Recent changes to the MOSFLM package for processing film and image plate data. Jnt CCP4/ESF-EACBM Newsl Protein Crystallogr 26.
    • (1992) Jnt CCP4/ESF-EACBM Newsl Protein Crystallogr , vol.26
    • Leslie, A.G.W.1
  • 49
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) Acta Cryst D50: 760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 50
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW, (1968) Solvent content of protein crystals. J Mol Biol 33: 491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 52
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Cryst D60: 2126-2132.
    • (2004) Acta Cryst , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 53
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A, (1997) MOLREP: an Automated Program for Molecular Replacement. J Appl Cryst 30: 1022-1025.
    • (1997) J Appl Cryst , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 54
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali A, Overington JH, (1994) Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci 3: 1582-1596.
    • (1994) Protein Sci , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.H.2
  • 55
  • 56
    • 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, (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. JCTC 4: 435-447.
    • (2008) JCTC , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 58
    • 33645941402 scopus 로고
    • The OPLS force field for proteins. Energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen WL, Tirado-Rives J, (1988) The OPLS force field for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J Am Chem Soc 110: 1657-1666.
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 60
    • 0001585978 scopus 로고    scopus 로고
    • Improving efficiency of large time-scale molecular dynamics of hydrogen-rich systems
    • Feenstra KA, Hess B, Berendsen HJC, (1999) Improving efficiency of large time-scale molecular dynamics 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.