메뉴 건너뛰기




Volumn 1808, Issue 7, 2011, Pages 1879-1887

Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes

Author keywords

CD spectroscopy; Desiccation; FTIR spectroscopy; LEA protein; Protein secondary structure; Protein membrane interactions

Indexed keywords

HEAT SHOCK PROTEIN; LIPOSOME; PROTEIN LEA7; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 79955802057     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.03.009     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 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
    • L. Dure, S.C. Greenway, and G.A. Galau Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis Biochemistry 20 1981 4162 4168
    • (1981) Biochemistry , vol.20 , pp. 4162-4168
    • Dure, L.1    Greenway, S.C.2    Galau, G.A.3
  • 2
    • 0032765202 scopus 로고    scopus 로고
    • Water content, raffinose, and dehydrins in the induction of desiccation tolerance in immature wheat embryos
    • M. Black, F. Corbineau, H. Gee, and D. Come Water content, raffinose, and dehydrins in the induction of desiccation tolerance in immature wheat embryos Plant Physiol. 120 1999 463 471 (Pubitemid 29388190)
    • (1999) Plant Physiology , vol.120 , Issue.2 , pp. 463-471
    • Black, M.1    Corbineau, F.2    Gee, H.3    Come, D.4
  • 3
    • 0344710956 scopus 로고
    • Maturation proteins associated with desiccation tolerance in soybean
    • S.A. Blackman, S.H. Wettlaufer, R.L. Obendorf, and A.C. Leopold Maturation proteins associated with desiccation tolerance in soybean Plant Physiol. 96 1991 868 874 (Pubitemid 21914096)
    • (1991) Plant Physiology , vol.96 , Issue.3 , pp. 868-874
    • Blackman, S.A.1    Wettlaufer, S.H.2    Obendorf, R.L.3    Leopold, A.C.4
  • 4
    • 42149115630 scopus 로고    scopus 로고
    • LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana
    • M. Hundertmark, and D.K. Hincha LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana BMC Genomics 9 2008 118
    • (2008) BMC Genomics , vol.9 , pp. 118
    • Hundertmark, M.1    Hincha, D.K.2
  • 5
    • 0036189582 scopus 로고    scopus 로고
    • Inactivation of two homologues of proteins presumed to be involved in the desiccation tolerance of plants sensitizes Deinococcus radiodurans R1 to desiccation
    • J.R. Battista, M.-J. Park, and A.E. McLemore Inactivation of two homologues of proteins presumed to be involved in the desiccation tolerance of plants sensitizes Deinococcus radiodurans R1 to desiccation Cryobiology 43 2001 133 139 (Pubitemid 33780252)
    • (2001) Cryobiology , vol.43 , Issue.2 , pp. 133-139
    • Battista, J.R.1    Park, M.-J.2    McLemore, A.E.3
  • 6
    • 0037034885 scopus 로고    scopus 로고
    • Anhydrobiosis: Plant desiccation gene found in a nematode
    • DOI 10.1038/416038a
    • J. Browne, A. Tunnacliffe, and A. Burnell Plant desiccation gene found in a nematode Nature 416 2002 38 (Pubitemid 34215392)
    • (2002) Nature , vol.416 , Issue.6876 , pp. 38
    • Browne, J.1    Tunnacliffe, A.2    Burnell, A.3
  • 9
    • 0027552602 scopus 로고
    • An osmotic stress protein of cyanobacteria is immunologically related to plant dehydrins
    • T.J. Close, and P.J. Lammers An osmotic stress protein of cyanobacteria is immunologically related to plant dehydrins Plant Physiol. 101 1993 773 779
    • (1993) Plant Physiol. , vol.101 , pp. 773-779
    • Close, T.J.1    Lammers, P.J.2
  • 10
    • 42149111687 scopus 로고    scopus 로고
    • Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana
    • N. Bies-Etheve, P. Gaubier-Comella, A. Debures, E. Lasserre, E. Jobet, M. Raynal, R. Cooke, and M. Delseny Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana Plant Mol. Biol. 67 2008 107 124
    • (2008) Plant Mol. Biol. , vol.67 , pp. 107-124
    • Bies-Etheve, N.1    Gaubier-Comella, P.2    Debures, A.3    Lasserre, E.4    Jobet, E.5    Raynal, M.6    Cooke, R.7    Delseny, M.8
  • 11
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208 (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of LEA proteins
    • A. Tunnacliffe, and M.J. Wise The continuing conundrum of LEA proteins Naturwissenschaften 94 2007 791 812
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 15
    • 77949398001 scopus 로고    scopus 로고
    • MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins
    • V. Boucher, J. Buitink, X. Lin, J. Boudet, F.A. Hoekstra, M. Hundertmark, D. Renard, and O. Leprince MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins Plant Cell Environ. 33 2010 418 430
    • (2010) Plant Cell Environ. , vol.33 , pp. 418-430
    • Boucher, V.1    Buitink, J.2    Lin, X.3    Boudet, J.4    Hoekstra, F.A.5    Hundertmark, M.6    Renard, D.7    Leprince, O.8
  • 17
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • DOI 10.1042/BJ20041931
    • K. Goyal, L.J. Walton, and A. Tunnacliffe LEA proteins prevent protein aggregation due to water stress Biochem. J. 388 2005 151 157 (Pubitemid 40732942)
    • (2005) Biochemical Journal , vol.388 , Issue.1 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 18
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • DOI 10.1104/pp.108.118208
    • D. Kovacs, E. Kalmar, Z. Torok, and P. Tompa Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins Plant Physiol. 147 2008 381 390 (Pubitemid 352844363)
    • (2008) Plant Physiology , vol.147 , Issue.1 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 19
    • 33745476713 scopus 로고    scopus 로고
    • Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance
    • DOI 10.1104/pp.105.074039
    • J. Boudet, J. Buitink, F.A. Hoekstra, H. Rogniaux, C. Larre, P. Satour, and O. Leprince Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance Plant Physiol. 140 2006 1418 1436 (Pubitemid 43956226)
    • (2006) Plant Physiology , vol.140 , Issue.4 , pp. 1418-1436
    • Boudet, J.1    Buitink, J.2    Hoekstra, F.A.3    Rogniaux, H.4    Larre, C.5    Satour, P.6    Leprince, O.7
  • 20
    • 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
    • K. Goyal, L. Tisi, A. Basran, J. Browne, A. Burnell, J. Zurdo, and A. Tunnacliffe Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein J. Biol. Chem. 278 2003 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
  • 24
    • 77954658735 scopus 로고    scopus 로고
    • Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state
    • A. Thalhammer, M. Hundertmark, A.V. Popova, R. Seckler, and D.K. Hincha Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state Biochim. Biophys. Acta 1798 2010 1812 1820
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1812-1820
    • Thalhammer, A.1    Hundertmark, M.2    Popova, A.V.3    Seckler, R.4    Hincha, D.K.5
  • 25
    • 77955652628 scopus 로고    scopus 로고
    • A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state
    • D. Tolleter, D.K. Hincha, and D. Macherel A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state Biochim. Biophys. Acta 1798 2010 1926 1933
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1926-1933
    • Tolleter, D.1    Hincha, D.K.2    MacHerel, D.3
  • 26
    • 0027140360 scopus 로고
    • Molecular responses to water deficit
    • E.A. Bray Molecular responses to water deficit Plant Physiol. 103 1993 1035 1040 (Pubitemid 2027436)
    • (1993) Plant Physiology , vol.103 , Issue.4 , pp. 1035-1040
    • Bray, E.A.1
  • 29
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • DOI 10.1006/abio.2000.4879
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 287 2000 243 251 (Pubitemid 32006233)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Yu.2    Woody, R.W.3
  • 31
    • 0036239562 scopus 로고    scopus 로고
    • Specific effects of fructo- and gluco-oligosaccharides in the preservation of liposomes during drying
    • D.K. Hincha, E. Zuther, E.M. Hellwege, and A.G. Heyer Specific effects of fructo- and gluco-oligosaccharides in the preservation of liposomes during drying Glycobiology 12 2002 103 110 (Pubitemid 34428933)
    • (2002) Glycobiology , vol.12 , Issue.2 , pp. 103-110
    • Hincha, D.K.1    Zuther, E.2    Hellwege, E.M.3    Heyer, A.G.4
  • 32
    • 0041320844 scopus 로고    scopus 로고
    • Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: A fourier transform infrared spectroscopy study
    • A.V. Popova, and D.K. Hincha Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: a Fourier-transform infrared spectroscopy study Biophys. J. 85 2003 1682 1690 (Pubitemid 37052251)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1682-1690
    • Popova, A.V.1    Hincha, D.K.2
  • 33
    • 34548290371 scopus 로고    scopus 로고
    • Effects of cholesterol on dry bilayers: Interactions between phosphatidylcholine unsaturation and glycolipid or free sugar
    • DOI 10.1529/biophysj.107.108886
    • A.V. Popova, and D.K. Hincha Effects of cholesterol on dry bilayers: interactions between phosphatidylcholine unsaturation and glycolopid or free sugar Biophys. J. 93 2007 1204 1214 (Pubitemid 47330900)
    • (2007) Biophysical Journal , vol.93 , Issue.4 , pp. 1204-1214
    • Popova, A.V.1    Hincha, D.K.2
  • 34
    • 0031205005 scopus 로고    scopus 로고
    • Stabilization of Dry Membranes by Mixtures of Hydroxyethyl Starch and Glucose: The Role of Vitrification
    • J.H. Crowe, A.E. Oliver, F.A. Hoekstra, and L.M. Crowe Stabilization of dry membranes by mixtures of hydroxyethyl starch and glucose: the role of vitrification Cryobiology 35 1997 20 30 (Pubitemid 127434057)
    • (1997) Cryobiology , vol.35 , Issue.1 , pp. 20-30
    • Crowe, J.H.1    Oliver, A.E.2    Hoekstra, F.A.3    Crowe, L.M.4
  • 35
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • C. Geourjon, and G. Deleage SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments Comput. Appl. Biosci. 11 1995 681 684 (Pubitemid 26032758)
    • (1995) Computer Applications in the Biosciences , vol.11 , Issue.6 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 36
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 37
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • DOI 10.1016/j.bbabio.2007.06.004, PII S0005272807001375
    • A. Barth Infrared spectroscopy of proteins Biochim. Biophys. Acta 1767 2007 1073 1101 (Pubitemid 47313388)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.9 , pp. 1073-1101
    • Barth, A.1
  • 38
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 39
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • J.L.R. Arrondo, A. Muga, J. Castresana, and F.M. Goni Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy Progr. Biophys. Mol. Biol. 59 1993 26 56
    • (1993) Progr. Biophys. Mol. Biol. , vol.59 , pp. 26-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 40
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra
    • H. Susi, and D.M. Byler Protein structure by Fourier transform infrared spectroscopy: second derivative spectra Biochem. Biophys. Res. Comm. 115 1983 391 397
    • (1983) Biochem. Biophys. Res. Comm. , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 41
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • H. Susi, and M. Byler Resolution-enhanced Fourier transform infrared spectroscopy of enzymes Meth. Enzymol. 130 1986 290 311
    • (1986) Meth. Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, M.2
  • 43
    • 0018890321 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins. V. Normal vibrations of β-turns
    • S. Krimm, and J. Bandekar Vibrational analysis of peptides, polypeptides, and proteins. V. Normal vibrations of β-turns Biopolymers 19 1980 1 29
    • (1980) Biopolymers , vol.19 , pp. 1-29
    • Krimm, S.1    Bandekar, J.2
  • 44
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • J.L.R. Arrondo, and F.M. Goni Structure and dynamics of membrane proteins as studied by infrared spectroscopy Prog. Biophys. Mol. Biol. 72 1999 367 405
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 45
    • 0032528558 scopus 로고    scopus 로고
    • Intermolecular β-sheet results from trifluoroethanol-induced nonnative α-helical structure in β-sheet predominant proteins: Infrared and circular dichroism spectroscopic study
    • DOI 10.1006/abbi.1998.0718
    • A. Dong, J. Matsuura, M.C. Manning, and J.F. Carpenter Intermolecular β-sheet results from trifluoroethanol-induced nonnative α-helical structure in β-sheet predominant proteins: infrared and circular dichroism spectroscopic study Arch. Biochem. Biophys. 355 1998 275 281 (Pubitemid 28364380)
    • (1998) Archives of Biochemistry and Biophysics , vol.355 , Issue.2 , pp. 275-281
    • Dong, A.1    Matsuura, J.2    Manning, M.C.3    Carpenter, J.F.4
  • 46
    • 0037054839 scopus 로고    scopus 로고
    • Hydration, slaving and protein function
    • DOI 10.1016/S0301-4622(02)00083-2, PII S0301462202000832
    • H. Frauenfelder, P.W. Fenimore, and B.H. McMahon Hydration, slaving and protein function Biophys. Chem. 98 2002 35 48 (Pubitemid 34785980)
    • (2002) Biophysical Chemistry , vol.98 , Issue.1-2 , pp. 35-48
    • Frauenfelder, H.1    Fenimore, P.W.2    McMahon, B.H.3
  • 47
    • 0026070508 scopus 로고
    • Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy
    • H.H. Mantsch, and R.N. McElhaney Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy Chem. Phys. Lipids 57 1991 213 226
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 213-226
    • Mantsch, H.H.1    McElhaney, R.N.2
  • 48
    • 0001603906 scopus 로고
    • High-pressure infrared spectroscopic evidence of water binding sites in 1,2-diacyl phospholipids
    • P.T.T. Wong, and H.H. Mantsch High-pressure infrared spectroscopic evidence of water binding sites in 1,2-diacyl phospholipids Chem. Phys. Lipids 46 1988 213 224
    • (1988) Chem. Phys. Lipids , vol.46 , pp. 213-224
    • Wong, P.T.T.1    Mantsch, H.H.2
  • 49
    • 33646179170 scopus 로고    scopus 로고
    • Low amounts of sucrose are sufficient to depress the phase transition temperature of dry phosphatidylcholine, but not for lyoprotection of liposomes
    • C. Cacela, and D.K. Hincha Low amounts of sucrose are sufficient to depress the phase transition temperature of dry phosphatidylcholine, but not for lyoprotection of liposomes Biophys. J. 90 2006 2831 2842
    • (2006) Biophys. J. , vol.90 , pp. 2831-2842
    • Cacela, C.1    Hincha, D.K.2
  • 50
    • 0348150694 scopus 로고    scopus 로고
    • The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity
    • DOI 10.1104/pp.011171
    • M.-C. Koag, R.D. Fenton, S. Wilkens, and T.J. Close The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity Plant Physiol. 131 2003 309 316 (Pubitemid 36141227)
    • (2003) Plant Physiology , vol.131 , Issue.1 , pp. 309-316
    • Koag, M.-C.1    Fenton, R.D.2    Wilkens, S.3    Close, T.J.4
  • 51
    • 67650175436 scopus 로고    scopus 로고
    • The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes
    • M.-C. Koag, S. Wilkens, R.D. Fenton, J. Resnik, E. Vo, and T.J. Close The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes Plant Physiol. 150 2009 1503 1514
    • (2009) Plant Physiol. , vol.150 , pp. 1503-1514
    • Koag, M.-C.1    Wilkens, S.2    Fenton, R.D.3    Resnik, J.4    Vo, E.5    Close, T.J.6
  • 52
    • 78649301049 scopus 로고    scopus 로고
    • Interactions of intrinsically disordered Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 with membranes-synergistic effects of lipid composition and temperature on secondary structure
    • L.N. Rahman, L. Chen, S. Nazim, V.V. Bamm, M.W. Yaish, B.A. Moffatt, J.R. Dutcher, and G. Harauz Interactions of intrinsically disordered Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 with membranes-synergistic effects of lipid composition and temperature on secondary structure Biochem. Cell Biol. 88 2010 791 807
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 791-807
    • Rahman, L.N.1    Chen, L.2    Nazim, S.3    Bamm, V.V.4    Yaish, M.W.5    Moffatt, B.A.6    Dutcher, J.R.7    Harauz, G.8
  • 53
    • 0028360934 scopus 로고
    • Interactions ofsynthtic peptide analogs of the class A amphipathic helix with lipids
    • V.K. Mishra, M.N. Palgunachari, J.P. Segrest, and G.M. Anantharamaiah Interactions ofsynthtic peptide analogs of the class A amphipathic helix with lipids J. Biol. Chem. 289 1994 7185 7191
    • (1994) J. Biol. Chem. , vol.289 , pp. 7185-7191
    • Mishra, V.K.1    Palgunachari, M.N.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 55
    • 47149091098 scopus 로고    scopus 로고
    • Methyl group dynamics and the onset of anharmonicity in myoglobin
    • M. Krishnan, V. Kurkal-Siebert, and J.C. Smith Methyl group dynamics and the onset of anharmonicity in myoglobin J. Phys. Chem. B 112 2008 5522 5533
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5522-5533
    • Krishnan, M.1    Kurkal-Siebert, V.2    Smith, J.C.3
  • 57
    • 0033747018 scopus 로고    scopus 로고
    • Molecular dynamics of solid-state lysozyme as affected by glycerol and water: A neutron scattering study
    • A.M. Tsai, D.A. Neumann, and L.N. Bell Molecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study Biophys. J. 79 2000 2728 2732
    • (2000) Biophys. J. , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 58
    • 0033780562 scopus 로고    scopus 로고
    • Infrared spectroscopy of enzyme reaction intermediates
    • C.W. Wharton Infrared spectroscopy of enzyme reaction intermediates Nat. Prod. Rep. 17 2000 447 453
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 447-453
    • Wharton, C.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.