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Volumn 175-176, Issue , 2013, Pages 47-53

The structure of poly-L-lysine in different solvents

Author keywords

Alpha helix; ATR infrared spectroscopy; Beta conformation; DFT calculation; DMSO; Ethylene glycol; PII; Poly l lysine; TFE; Water

Indexed keywords

AMIDE; ETHYLENE GLYCOL; POLYLYSINE; SOLVENT; WATER;

EID: 84875160964     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.02.004     Document Type: Article
Times cited : (61)

References (55)
  • 1
    • 0014227144 scopus 로고
    • New chain conformations of poly(glutamic acid) and polylysine
    • M.L. Tiffany, and S. Krimm New chain conformations of poly(glutamic acid) and polylysine Biopolymers 6 1968 1379 1382
    • (1968) Biopolymers , vol.6 , pp. 1379-1382
    • Tiffany, M.L.1    Krimm, S.2
  • 2
    • 0037120758 scopus 로고    scopus 로고
    • Effect of secondary structure on the potential of mean force for poly-l-lysine in the alpha-helix and beta-sheet conformations
    • J.J. Grigsby, H.W. Blanch, and J.M. Prausnitz Effect of secondary structure on the potential of mean force for poly-l-lysine in the alpha-helix and beta-sheet conformations Biophysical Chemistry 99 2002 107 116
    • (2002) Biophysical Chemistry , vol.99 , pp. 107-116
    • Grigsby, J.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 3
    • 0017225725 scopus 로고
    • Solution conformation of poly(l-lysine) - Raman and infrared spectroscopic study
    • P.C. Painter, and J.L. Koenig Solution conformation of poly(l-lysine) - Raman and infrared spectroscopic study Biopolymers 15 1976 229 240
    • (1976) Biopolymers , vol.15 , pp. 229-240
    • Painter, P.C.1    Koenig, J.L.2
  • 4
    • 0016788526 scopus 로고
    • Nmr-studies of mixtures of poly-l-lysine hydrobromide with water
    • A. Darke, and E.G. Finer Nmr-studies of mixtures of poly-l-lysine hydrobromide with water Biopolymers 14 1975 441 455
    • (1975) Biopolymers , vol.14 , pp. 441-455
    • Darke, A.1    Finer, E.G.2
  • 5
    • 0006117467 scopus 로고
    • A nuclear magnetic resonance study of the helix coil transition of poly L lysine in methanol water solvents
    • F.J. Joubert, N. Lotan, and H.A. Scheraga A nuclear magnetic resonance study of the helix coil transition of poly L lysine in methanol water solvents Physiological Chemistry and Physics 1 1969 348
    • (1969) Physiological Chemistry and Physics , vol.1 , pp. 348
    • Joubert, F.J.1    Lotan, N.2    Scheraga, H.A.3
  • 6
    • 6244223777 scopus 로고
    • Nmr and electron-spin-resonance study of the conformations and dynamical properties of poly(l-lysine) in aqueous-solutions
    • B. Perly, Y. Chevalier, and C. Chachaty Nmr and electron-spin-resonance study of the conformations and dynamical properties of poly(l-lysine) in aqueous-solutions Macromolecules 14 1981 969 975
    • (1981) Macromolecules , vol.14 , pp. 969-975
    • Perly, B.1    Chevalier, Y.2    Chachaty, C.3
  • 8
    • 0034118337 scopus 로고    scopus 로고
    • Solution structure and dynamics of biomolecules from Ramam optical activity
    • DOI 10.1016/S0079-6107(99)00017-6, PII S0079610799000176
    • L.D. Barron, L. Hecht, E.W. Blanch, and A.F. Bell Solution structure and dynamics of biomolecules from Raman optical activity Progress in Biophysics and Molecular Biology 73 2000 1 49 (Pubitemid 30252105)
    • (2000) Progress in Biophysics and Molecular Biology , vol.73 , Issue.1 , pp. 1-49
    • Barron, L.D.1    Hecht, L.2    Blanch, E.W.3    Bell, A.F.4
  • 10
    • 0033018671 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectroscopy of selected oligopeptide conformations
    • DOI 10.1016/S0968-0896(98)00217-X, PII S096808969800217X
    • T.A. Keiderling, R.A.G.D. Silva, G. Yoder, and R.K. Dukor Vibrational circular dichroism spectroscopy of selected oligopeptide conformations Bioorganic & Medicinal Chemistry 7 1999 133 141 (Pubitemid 29097701)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.1 , pp. 133-141
    • Keiderling, T.A.1    Silva, R.A.G.D.2    Yoder, G.3    Dukor, R.K.4
  • 11
    • 0024318673 scopus 로고
    • UV resonance Raman studies of peptide conformation in poly(L-lysine), poly(L-glutamic acid), an model complexes: The basis for protein secondary structure determinations
    • DOI 10.1021/ja00194a022
    • S. Song, and S.A. Asher UV resonance Raman studies of peptide conformation in poly(l-lysine), poly(l-glutamic acid), and model complexes: the basis for protein secondary structure determinations Journal of the American Chemical Society 111 1989 4295 4305 (Pubitemid 19156932)
    • (1989) Journal of the American Chemical Society , vol.111 , Issue.12 , pp. 4295-4305
    • Song, S.1    Asher, S.A.2
  • 12
    • 12044258309 scopus 로고
    • UVRR spectroscopy of the peptide bond. 2. Carbonyl H-bond effects on the ground- and excited-state structures of N-methylacetamide
    • Y. Wang, R. Purrello, S. Georgiou, and T.G. Spiro UVRR spectroscopy of the peptide bond. 2. Carbonyl H-bond effects on the ground- and excited-state structures of N-methylacetamide Journal of the American Chemical Society 113 1991 6368 6377
    • (1991) Journal of the American Chemical Society , vol.113 , pp. 6368-6377
    • Wang, Y.1    Purrello, R.2    Georgiou, S.3    Spiro, T.G.4
  • 13
    • 30144436601 scopus 로고    scopus 로고
    • Intermediacy of Poly(L-proline) II and β-strand conformations in poly(L-lysine) β-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy
    • DOI 10.1021/bi051507v
    • R.D. JiJi, G. Balakrishnan, Y. Hu, and T.G. Spiro Intermediacy of poly(l-proline) II and β-strand conformations in poly(l-lysine) β-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy Biochemistry 45 2005 34 41 (Pubitemid 43054080)
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 34-41
    • Jiji, R.D.1    Balakrishnan, G.2    Hu, Y.3    Spiro, T.G.4
  • 14
    • 19744362700 scopus 로고    scopus 로고
    • 1-helix, and β-sheet ψ angle energy landscape in poly-L-lysine and poly-L-glutamic acid
    • DOI 10.1021/ja044636s
    • A.V. Mikhonin, N.S. Myshakina, S.V. Bykov, and S.A. Asher UV resonance Raman determination of polyproline II, extended 2.5(1)-helix, and beta-sheet Psi angle energy landscape in poly-l-lysine and poly-l-glutamic acid Journal of the American Chemical Society 127 2005 7712 7720 (Pubitemid 40745960)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.21 , pp. 7712-7720
    • Mikhonin, A.V.1    Myshakina, N.S.2    Bykov, S.V.3    Asher, S.A.4
  • 15
    • 80051596185 scopus 로고    scopus 로고
    • Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol
    • S. Toal, O. Amidi, and R. Schweitzer-Stenner Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol Journal of the American Chemical Society 133 2011 12728 12739
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 12728-12739
    • Toal, S.1    Amidi, O.2    Schweitzer-Stenner, R.3
  • 16
    • 0036784642 scopus 로고    scopus 로고
    • A simple model for polyproline II structure in unfolded states of alanine-based peptides
    • R.V. Pappu, and G.D. Rose A simple model for polyproline II structure in unfolded states of alanine-based peptides Protein Science 11 2002 2437 2455
    • (2002) Protein Science , vol.11 , pp. 2437-2455
    • Pappu, R.V.1    Rose, G.D.2
  • 17
    • 1542366657 scopus 로고    scopus 로고
    • Role of Solvent in Determining Conformational Preferences of Alanine Dipeptide in Water
    • DOI 10.1021/ja039051x
    • A.N. Drozdov, A. Grossfield, and R.V. Pappu Role of solvent in determining conformational preferences of alanine dipeptide in water Journal of the American Chemical Society 126 2004 2574 2581 (Pubitemid 38295738)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.8 , pp. 2574-2581
    • Drozdov, A.N.1    Grossfield, A.2    Pappu, R.V.3
  • 18
    • 0036399145 scopus 로고    scopus 로고
    • Unfolded proteins studied by Raman optical activity
    • DOI 10.1016/S0065-3233(02)62005-4
    • L.D. Barron, E.W. Blanch, and L. Hecht Unfolded proteins studied by Raman optical activity Unfolded Proteins 62 2002 51 90 (Pubitemid 35204868)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 51-90
    • Barron, L.D.1    Blanch, E.W.2    Hecht, L.3
  • 19
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • DOI 10.1016/S0065-3233(02)62008-X
    • Z.S. Shi, R.W. Woody, and N.R. Kallenbach Is polyproline II a major backbone conformation in unfolded proteins? Unfolded Proteins 62 2002 163 240 (Pubitemid 35204871)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 20
    • 0034636977 scopus 로고    scopus 로고
    • Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme
    • E.W. Blanch, L.A. Morozova-Roche, D.A. Cochran, A.J. Doig, L. Hecht, and L.D. Barron Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme Journal of Molecular Biology 301 2000 553 563
    • (2000) Journal of Molecular Biology , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 23
    • 0036746917 scopus 로고    scopus 로고
    • ATR-FTIR spectroscopy: Its advantages and limitations
    • J. Grdadolnik ATR-FTIR spectroscopy: its advantages and limitations Acta Chimica Slovenica 49 2002 631 642
    • (2002) Acta Chimica Slovenica , vol.49 , pp. 631-642
    • Grdadolnik, J.1
  • 25
    • 16344363078 scopus 로고    scopus 로고
    • Production of nonclassical inclusion bodies from which correctly folded protein can be extracted
    • DOI 10.1021/bp0497839
    • S. Jevsevar, V. Gaberc-Porekar, I. Fonda, B. Podobnik, J. Grdadolnik, and V. Menart Production of nonclassical inclusion bodies from which correctly folded protein can be extracted Biotechnology Progress 21 2005 632 639 (Pubitemid 40466443)
    • (2005) Biotechnology Progress , vol.21 , Issue.2 , pp. 632-639
    • Jevsevar, S.1    Gaberc-Porekar, V.2    Fonda, I.3    Podobnik, B.4    Grdadolnik, J.5    Menart, V.6
  • 26
    • 17444390052 scopus 로고    scopus 로고
    • A conformational α-helix to β-sheet transition accompanies racemic self-assembly of polylysine: An FT-IR spectroscopic study
    • DOI 10.1016/j.bpc.2005.01.003
    • W. Dzwolak, and V. Smirnovas A conformational α-helix to β-sheet transition accompanies racemic self-assembly of polylysine: an FT-IR spectroscopic study Biophysical Chemistry 115 2005 49 54 (Pubitemid 40543106)
    • (2005) Biophysical Chemistry , vol.115 , Issue.1 , pp. 49-54
    • Dzwolak, W.1    Smirnovas, V.2
  • 27
    • 35948936905 scopus 로고    scopus 로고
    • Cross-strand coupling of a β-hairpin peptide stabilized with an Aib-Gly turn studied using isotope-edited IR spectroscopy
    • DOI 10.1021/ja0736414
    • R. Huang, V. Setnicka, M.A. Etienne, J. Kim, J. Kubelka, R.P. Hammer, and T.A. Keiderling Cross-strand coupling of a β-hairpin peptide stabilized with an Aib-Gly turn studied using isotope-edited IR spectroscopy Journal of the American Chemical Society 129 2007 13592 13603 (Pubitemid 350071788)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.44 , pp. 13592-13603
    • Huang, R.1    Setnicka, V.2    Etienne, M.A.3    Kim, J.4    Kubelka, J.5    Hammer, R.P.6    Keiderling, T.A.7
  • 31
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • C. Lee, W. Yang, and R.G. Parr Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Physical Review B 37 1988 785 789
    • (1988) Physical Review B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 32
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • A.D. Becke Density-functional exchange-energy approximation with correct asymptotic behavior Physical Review A 38 1988 3098 3100
    • (1988) Physical Review A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 33
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • A.D. Becke Density-functional thermochemistry. III. The role of exact exchange Journal of Chemical Physics 98 1993 5648 5652
    • (1993) Journal of Chemical Physics , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 34
    • 0002058203 scopus 로고
    • Ultraviolet resonance Raman studies of proteins and related model compounds
    • Wiley & Sons Ltd. New York
    • J.C. Austin, T. Jordan, and T.G. Spiro Ultraviolet resonance Raman studies of proteins and related model compounds Biomolecular Spectroscopy 1993 Wiley & Sons Ltd. New York
    • (1993) Biomolecular Spectroscopy
    • Austin, J.C.1    Jordan, T.2    Spiro, T.G.3
  • 35
    • 0038281274 scopus 로고    scopus 로고
    • Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins
    • E. Vass, M. Hollosi, F. Besson, and R. Buchet Vibrational spectroscopic detection of beta- and gamma-turns in synthetic and natural peptides and proteins Chemical Reviews 103 2003 1917 1954
    • (2003) Chemical Reviews , vol.103 , pp. 1917-1954
    • Vass, E.1    Hollosi, M.2    Besson, F.3    Buchet, R.4
  • 36
    • 0035814332 scopus 로고    scopus 로고
    • Differentiation of β-sheet-forming structures: Ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets
    • DOI 10.1021/ja0116627
    • J. Kubelka, and T.A. Keiderling Differentiation of beta-sheet-forming structures: Ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein beta-sheets Journal of the American Chemical Society 123 2001 12048 12058 (Pubitemid 33135036)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.48 , pp. 12048-12058
    • Kubelka, J.1    Keiderling, T.A.2
  • 37
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • J. Bandekar Amide modes and protein conformation Biochimica et Biophysica Acta 1120 1992 123 143
    • (1992) Biochimica et Biophysica Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 38
    • 0031213772 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectra of proteins in the amide III region: Measurement and correlation of bandshape to secondary structure
    • DOI 10.1006/abio.1997.2221
    • B.I. Baello, P. Pancoska, and T.A. Keiderling Vibrational circular dichroism spectra of proteins in the amide III region: measurement and correlation of bandshape to secondary structure Analytical Biochemistry 250 1997 212 221 (Pubitemid 27319099)
    • (1997) Analytical Biochemistry , vol.250 , Issue.2 , pp. 212-221
    • Baello, B.I.1    Pancoska, P.2    Keiderling, T.A.3
  • 39
    • 0028539766 scopus 로고
    • Secondary structure estimation of proteins using the amide-III region of Fourier-transform infrared-spectroscopy - Application to analyze calcium binding-induced structural-changes in calsequestrin
    • F.N. Fu, D.B. Deoliveira, W.R. Trumble, H.K. Sarkar, and B.R. Singh Secondary structure estimation of proteins using the amide-III region of Fourier-transform infrared-spectroscopy - application to analyze calcium binding-induced structural-changes in calsequestrin Applied Spectroscopy 48 1994 1432 1441
    • (1994) Applied Spectroscopy , vol.48 , pp. 1432-1441
    • Fu, F.N.1    Deoliveira, D.B.2    Trumble, W.R.3    Sarkar, H.K.4    Singh, B.R.5
  • 41
    • 84863414548 scopus 로고    scopus 로고
    • Structure and vibrational motion of insulin from Raman optical activity spectra
    • S. Yamamoto, J. Kaminský, and P. Bouř Structure and vibrational motion of insulin from Raman optical activity spectra Analytical Chemistry 84 2012 2440 2451
    • (2012) Analytical Chemistry , vol.84 , pp. 2440-2451
    • Yamamoto, S.1    Kaminský, J.2    Bouř, P.3
  • 42
    • 0001443463 scopus 로고    scopus 로고
    • Effects of Hydration on the Structure, Vibrational Wavenumbers, Vibrational Force Field and Resonance Raman Intensities of N-Methylacetamide
    • H. Torii, T. Tatsumi, and M. Tasumi Effects of hydration on the structure, vibrational wavenumbers, vibrational force field and resonance Raman intensities of N-methylacetamide Journal of Raman Spectroscopy 29 1998 537 546 (Pubitemid 128477609)
    • (1998) Journal of Raman Spectroscopy , vol.29 , Issue.6 , pp. 537-546
    • Torii, H.1    Tatsumi, T.2    Tasumit, M.3
  • 43
    • 3142754280 scopus 로고    scopus 로고
    • UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations
    • DOI 10.1021/ja049518j
    • S.A. Asher, A.V. Mikhonin, and S. Bykov UV Raman demonstrates that alpha-helical polyalanine peptides melt to polyproline II conformations Journal of the American Chemical Society 126 2004 8433 8440 (Pubitemid 38917966)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.27 , pp. 8433-8440
    • Asher, S.A.1    Mikhonin, A.V.2    Bykov, S.3
  • 44
    • 10844246340 scopus 로고    scopus 로고
    • Assignments and conformational dependencies of the amide III peptide backbone UV resonance Raman bands
    • DOI 10.1021/jp045959d
    • A.V. Mikhonin, Z. Ahmed, A. Ianoul, and S.A. Asher Assignments and conformational dependencies of the amide III peptide backbone UV resonance Raman bands The Journal of Physical Chemistry. B 108 2004 19020 19028 (Pubitemid 40003265)
    • (2004) Journal of Physical Chemistry B , vol.108 , Issue.49 , pp. 19020-19028
    • Mikhonin, A.V.1    Ahmed, Z.2    Ianoul, A.3    Asher, S.A.4
  • 45
    • 78449233764 scopus 로고    scopus 로고
    • Polycyano derivatives of some organic tri- and hexacyclic molecules are powerful super- and hyperacids in the gas phase and DMSO: Computational study by DFT approach
    • R. Vianello, and Z.B. Maksić Polycyano derivatives of some organic tri- and hexacyclic molecules are powerful super- and hyperacids in the gas phase and DMSO: computational study by DFT approach Journal of Organic Chemistry 75 2010 7670 7681
    • (2010) Journal of Organic Chemistry , vol.75 , pp. 7670-7681
    • Vianello, R.1    Maksić, Z.B.2
  • 48
    • 0030730455 scopus 로고    scopus 로고
    • Specificity of helix-induction by 2,2,2-trifluoroethanol in polypeptides
    • DOI 10.1016/S0141-8130(97)00064-0, PII S0141813097000640
    • A.I. Arunkumar, T.K.S. Kumar, and C. Yu Specificity of helix-induction by 2,2,2-trifluoroethanol in polypeptides International Journal of Biological Macromolecules 21 1997 223 230 (Pubitemid 27462553)
    • (1997) International Journal of Biological Macromolecules , vol.21 , Issue.3 , pp. 223-230
    • Arunkumar, A.I.1    Kumar, T.K.S.2    Yu, C.3
  • 49
    • 77957300060 scopus 로고    scopus 로고
    • Inter-residue coupling and equilibrium unfolding of PM helical peptides. Vibrational spectra enhanced with C-13 isotopic labeling
    • H. Chi, A. Lakhani, A. Roy, M. Nakaema, and T.A. Keiderling Inter-residue coupling and equilibrium unfolding of PM helical peptides. Vibrational spectra enhanced with C-13 isotopic labeling The Journal of Physical Chemistry. B 114 2010 12744 12753
    • (2010) The Journal of Physical Chemistry. B , vol.114 , pp. 12744-12753
    • Chi, H.1    Lakhani, A.2    Roy, A.3    Nakaema, M.4    Keiderling, T.A.5
  • 50
    • 77950949985 scopus 로고    scopus 로고
    • Circular dichroism and UV resonance Raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide
    • K. Xiong, and S.A. Asher Circular dichroism and UV resonance Raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide Biochemistry 49 2010 3336 3342
    • (2010) Biochemistry , vol.49 , pp. 3336-3342
    • Xiong, K.1    Asher, S.A.2
  • 52
    • 49149094036 scopus 로고    scopus 로고
    • Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO
    • A.M.S. Duarte, C.P.M. van Mierlo, and M.A. Hemminga Molecular dynamics study of the solvation of an alpha-helical transmembrane peptide by DMSO The Journal of Physical Chemistry. B 112 2008 8664 8671
    • (2008) The Journal of Physical Chemistry. B , vol.112 , pp. 8664-8671
    • Duarte, A.M.S.1    Van Mierlo, C.P.M.2    Hemminga, M.A.3
  • 53
    • 0038245117 scopus 로고    scopus 로고
    • An electronic effect on protein structure
    • DOI 10.1110/ps.0241903
    • M.P. Hinderaker, and R.T. Raines An electronic effect on protein structure Protein Science 12 2003 1188 1194 (Pubitemid 36597505)
    • (2003) Protein Science , vol.12 , Issue.6 , pp. 1188-1194
    • Hinderaker, M.P.1    Raines, R.T.2
  • 54
    • 79954518426 scopus 로고    scopus 로고
    • Optimizing protein-solvent force fields to reproduce intrinsic conformational preferences of model peptides
    • P.S. Nerenberg, and T. Head-Gordon Optimizing protein-solvent force fields to reproduce intrinsic conformational preferences of model peptides Journal of Chemical Theory and Computation 7 2011 1220 1230
    • (2011) Journal of Chemical Theory and Computation , vol.7 , pp. 1220-1230
    • Nerenberg, P.S.1    Head-Gordon, T.2
  • 55
    • 73849143569 scopus 로고    scopus 로고
    • The relationship between water bridges and the polyproline II conformation: A large-scale analysis of molecular dynamics simulations and crystal structures
    • P.B. Law, and V. Daggett The relationship between water bridges and the polyproline II conformation: a large-scale analysis of molecular dynamics simulations and crystal structures Protein Engineering, Design & Selection 23 2010 27 33
    • (2010) Protein Engineering, Design & Selection , vol.23 , pp. 27-33
    • Law, P.B.1    Daggett, V.2


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