메뉴 건너뛰기




Volumn 1834, Issue 6, 2013, Pages 977-988

Dynamics of uncrystallized water and protein in hydrated elastin studied by thermal and dielectric techniques

Author keywords

Amino acid; Dielectric relaxation; Glass transition; Hydrated elastin; Hydrophobic hydration; Uncrystallized water

Indexed keywords

ELASTIN; PROTEIN; WATER;

EID: 84878115983     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.03.015     Document Type: Article
Times cited : (26)

References (69)
  • 1
    • 0016354473 scopus 로고
    • The properties of water in biological systems
    • R. Cooke, and I.D. Kuntz The properties of water in biological systems Annu. Rev. Biophys. Bioeng. 3 1974 95 126
    • (1974) Annu. Rev. Biophys. Bioeng. , vol.3 , pp. 95-126
    • Cooke, R.1    Kuntz, I.D.2
  • 3
    • 0015504345 scopus 로고
    • Dielectric relaxation spectra of water absorbed on lysozyme
    • S.C. Harvey, and P. Hoekstra Dielectric relaxation spectra of water absorbed on lysozyme J. Phys. Chem. 76 1972 2987 2994
    • (1972) J. Phys. Chem. , vol.76 , pp. 2987-2994
    • Harvey, S.C.1    Hoekstra, P.2
  • 4
    • 0025107856 scopus 로고
    • Fluctuations, exchange processes, and water diffusion in aqueous protein systems, a study of bovine serum albumin by diverse NMR techniques
    • R. Kimmich, T. Gneiting, K. Kotitschke, and G. Schnur Fluctuations, exchange processes, and water diffusion in aqueous protein systems, a study of bovine serum albumin by diverse NMR techniques Biophys. J. 58 1990 1183 1197
    • (1990) Biophys. J. , vol.58 , pp. 1183-1197
    • Kimmich, R.1    Gneiting, T.2    Kotitschke, K.3    Schnur, G.4
  • 6
    • 71649087577 scopus 로고    scopus 로고
    • 13C NMR studies on the temperature dependent water and protein dynamics in hydrated elastin, myoglobin and collagen
    • 13C NMR studies on the temperature dependent water and protein dynamics in hydrated elastin, myoglobin and collagen Biochim. Biophys. Acta 1804 2010 41 48
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 41-48
    • Lusceac, S.A.1    Vogel, M.R.2    Herbers, C.R.3
  • 7
    • 84859974245 scopus 로고    scopus 로고
    • Water and protein dynamics in bovine serum albumin-water mixtures over wide ranges of composition
    • A. Panagopoulou, A. Kyritsis, N. Shinyashiki, and P. Pissis Water and protein dynamics in bovine serum albumin-water mixtures over wide ranges of composition J. Phys. Chem. B 116 2012 4593 4602
    • (2012) J. Phys. Chem. B , vol.116 , pp. 4593-4602
    • Panagopoulou, A.1    Kyritsis, A.2    Shinyashiki, N.3    Pissis, P.4
  • 8
    • 70349295517 scopus 로고    scopus 로고
    • Dielectric response of deeply supercooled hydration water in the connective tissue proteins collagen and elastin
    • C. Gainaru, A. Fillmer, and R. Böhmer Dielectric response of deeply supercooled hydration water in the connective tissue proteins collagen and elastin J. Phys. Chem. B 113 2009 12628 12631
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12628-12631
    • Gainaru, C.1    Fillmer, A.2    Böhmer, R.3
  • 13
    • 71649095681 scopus 로고    scopus 로고
    • The protein glass transition as measured by dielectric spectroscopy and differential scanning calorimetry
    • H. Jansson, and J. Swenson The protein glass transition as measured by dielectric spectroscopy and differential scanning calorimetry Biochim. Biophys. Acta 1804 2010 20 26
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 20-26
    • Jansson, H.1    Swenson, J.2
  • 15
    • 30744469866 scopus 로고    scopus 로고
    • Dynamics of proteins in hydrated state and in solution as studied by dielectric relaxation spectroscopy
    • J. Mijović, Y. Bian, R.A. Gross, and B. Chen Dynamics of proteins in hydrated state and in solution as studied by dielectric relaxation spectroscopy Macromolecules 38 2005 10812 10819
    • (2005) Macromolecules , vol.38 , pp. 10812-10819
    • Mijović, J.1    Bian, Y.2    Gross, R.A.3    Chen, B.4
  • 17
    • 33646170638 scopus 로고    scopus 로고
    • Hydration dependence of conformational dielectric relaxation of lysozyme
    • J. Knab, J.-Y. Chen, and A. Markelz Hydration dependence of conformational dielectric relaxation of lysozyme Biophys. J. 90 2006 2576 2581
    • (2006) Biophys. J. , vol.90 , pp. 2576-2581
    • Knab, J.1    Chen, J.-Y.2    Markelz, A.3
  • 18
    • 34249867927 scopus 로고    scopus 로고
    • Hydration of gluten: A dielectric, calorimetric and fourier transform infrared study
    • A. Almutawah, S.A. Barker, and P.S. Belton Hydration of gluten: A dielectric, calorimetric and fourier transform infrared study Biomacromolecules 8 2007 1601 1606
    • (2007) Biomacromolecules , vol.8 , pp. 1601-1606
    • Almutawah, A.1    Barker, S.A.2    Belton, P.S.3
  • 19
    • 84856869626 scopus 로고    scopus 로고
    • Origin and influence of water-induced chain relaxation phenomena in chitosan biopolymers
    • M. Al Kobaisi, P. Murugaraj, and D.E. Mainwaring Origin and influence of water-induced chain relaxation phenomena in chitosan biopolymers J. Polym. Sci., Part B: Polym. Phys. 50 2012 403 414
    • (2012) J. Polym. Sci., Part B: Polym. Phys. , vol.50 , pp. 403-414
    • Al Kobaisi, M.1    Murugaraj, P.2    Mainwaring, D.E.3
  • 20
    • 79959277520 scopus 로고    scopus 로고
    • Hydrated elastin: Dynamics of water and protein followed by dielectric spectroscopies
    • V. Samouillan, D. Tintar, and C. Lacabanne Hydrated elastin: Dynamics of water and protein followed by dielectric spectroscopies Chem. Phys. 385 2011 19 26
    • (2011) Chem. Phys. , vol.385 , pp. 19-26
    • Samouillan, V.1    Tintar, D.2    Lacabanne, C.3
  • 21
    • 0042861647 scopus 로고    scopus 로고
    • Translational hydration water dynamics drives the protein glass transition
    • A.L. Tournier, J. Xu, and J.C. Smith Translational hydration water dynamics drives the protein glass transition Biophys. J. 85 2003 1871 1875
    • (2003) Biophys. J. , vol.85 , pp. 1871-1875
    • Tournier, A.L.1    Xu, J.2    Smith, J.C.3
  • 22
    • 0031793174 scopus 로고    scopus 로고
    • Cooperative charge fluctuations by migrating protons in globular proteins
    • G. Careri Cooperative charge fluctuations by migrating protons in globular proteins Prog. Biophys. Mol. Biol. 70 1998 223 249
    • (1998) Prog. Biophys. Mol. Biol. , vol.70 , pp. 223-249
    • Careri, G.1
  • 24
    • 0141560454 scopus 로고    scopus 로고
    • The 'glass transition' in protein dynamics: What it is, why it occurs, and how to exploit it
    • D. Ringe, and G.A. Petsko The 'glass transition' in protein dynamics: What it is, why it occurs, and how to exploit it Biophys. Chem. 105 2003 667 680
    • (2003) Biophys. Chem. , vol.105 , pp. 667-680
    • Ringe, D.1    Petsko, G.A.2
  • 25
    • 5144223810 scopus 로고    scopus 로고
    • Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions
    • P.W. Fenimore, H. Frauenfelder, B.H. McMahon, and R.D. Young Bulk-solvent and hydration-shell fluctuations, similar to α- and β-fluctuations in glasses, control protein motions and functions Proc. Natl. Acad. Sci. 101 2004 14408 14413
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 14408-14413
    • Fenimore, P.W.1    Frauenfelder, H.2    Mcmahon, B.H.3    Young, R.D.4
  • 26
    • 0034189981 scopus 로고    scopus 로고
    • Dielectric relaxations of collagen and elastin in the dehydrated state
    • V. Samouillan, A. Lamure, and C. Lacabanne Dielectric relaxations of collagen and elastin in the dehydrated state Chem. Phys. 255 2000 259 271
    • (2000) Chem. Phys. , vol.255 , pp. 259-271
    • Samouillan, V.1    Lamure, A.2    Lacabanne, C.3
  • 27
    • 84855198895 scopus 로고    scopus 로고
    • Thermodynamics of meat proteins
    • R.G.M. Van der Sman Thermodynamics of meat proteins Food Hydrocoll. 27 2012 529 535
    • (2012) Food Hydrocoll. , vol.27 , pp. 529-535
    • Van Der Sman, R.G.M.1
  • 30
    • 0032751580 scopus 로고    scopus 로고
    • The structures of elastins and their function
    • L. Debelle, and A.J.P. Alix The structures of elastins and their function Biochimie 81 1999 981 994
    • (1999) Biochimie , vol.81 , pp. 981-994
    • Debelle, L.1    Alix, A.J.P.2
  • 32
    • 0016168148 scopus 로고
    • The elastic properties of elastin
    • C. Hoeve, and P. Flory The elastic properties of elastin Biopolymers 13 1974 677 686
    • (1974) Biopolymers , vol.13 , pp. 677-686
    • Hoeve, C.1    Flory, P.2
  • 34
    • 0001728735 scopus 로고
    • Protein elasticity based on conformations of sequential polypeptides: The biological elastic fiber
    • D. Urry Protein elasticity based on conformations of sequential polypeptides: The biological elastic fiber J. Protein Chem. 3 1984 403 436
    • (1984) J. Protein Chem. , vol.3 , pp. 403-436
    • Urry, D.1
  • 35
    • 0242499494 scopus 로고    scopus 로고
    • Dissection of human tropoelastexon-by-exon chemical synthesis and related conformational studies
    • A. Tamburro, B. Bochicchio, and A. Pepe Dissection of human tropoelastexon-by-exon chemical synthesis and related conformational studies Biochemistry 42 2003 13347 13362
    • (2003) Biochemistry , vol.42 , pp. 13347-13362
    • Tamburro, A.1    Bochicchio, B.2    Pepe, A.3
  • 36
    • 33747084768 scopus 로고    scopus 로고
    • Localizing alpha-helices in human tropoelastin: Assembly of the elastin "puzzle"
    • A. Tamburro, A. Pepe, and B. Bochicchio Localizing alpha-helices in human tropoelastin: Assembly of the elastin "puzzle" Biochemistry 45 2006 9518 9530
    • (2006) Biochemistry , vol.45 , pp. 9518-9530
    • Tamburro, A.1    Pepe, A.2    Bochicchio, B.3
  • 37
    • 0037569589 scopus 로고    scopus 로고
    • Molecular basis for the extensibility of elastin
    • B. Li, and V. Daggett Molecular basis for the extensibility of elastin J. Muscle Res. Cell Motil. 23 2002 561 573
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , pp. 561-573
    • Li, B.1    Daggett, V.2
  • 38
    • 18144374871 scopus 로고    scopus 로고
    • The hydrophobic domain 26 in human tropoelastin is unstructured in solution
    • J. Mackay, L. Muiznieks, A. Toonkool, and A. Weiss The hydrophobic domain 26 in human tropoelastin is unstructured in solution J. Struct. Biol. 150 2005 154 162
    • (2005) J. Struct. Biol. , vol.150 , pp. 154-162
    • Mackay, J.1    Muiznieks, L.2    Toonkool, A.3    Weiss, A.4
  • 39
    • 77049239749 scopus 로고
    • The chemistry of connective tissues 2. Soluble proteins derived from partial hydrolysis of elastin
    • S.M. Partridge, H.F. Davies, and G.S. Adair The chemistry of connective tissues 2. Soluble proteins derived from partial hydrolysis of elastin Biochem. J. 61 1955 11 21
    • (1955) Biochem. J. , vol.61 , pp. 11-21
    • Partridge, S.M.1    Davies, H.F.2    Adair, G.S.3
  • 40
    • 0017942478 scopus 로고
    • The glass point of elastin as a function of diluent concentration
    • C. Hoeve, and M. Hoeve The glass point of elastin as a function of diluent concentration Polym. Eng. Sci. 20 1980 290 293
    • (1980) Polym. Eng. Sci. , vol.20 , pp. 290-293
    • Hoeve, C.1    Hoeve, M.2
  • 42
    • 0023953406 scopus 로고
    • Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics
    • D.W. Urry Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics J. Protein Chem. 7 1988 1 34
    • (1988) J. Protein Chem. , vol.7 , pp. 1-34
    • Urry, D.W.1
  • 43
    • 68949129479 scopus 로고    scopus 로고
    • Influence of the amino-acid sequence on the inverse temperature transition of elastin-like polymers
    • A. Ribeiro, F. Javier Arias, J. Reguera, M. Alonso, and J.C. Rodríquez-Cabello Influence of the amino-acid sequence on the inverse temperature transition of elastin-like polymers Biophys. J. 97 1 2009 312 320
    • (2009) Biophys. J. , vol.97 , Issue.1 , pp. 312-320
    • Ribeiro, A.1    Javier Arias, F.2    Reguera, J.3    Alonso, M.4    Rodríquez-Cabello, J.C.5
  • 44
    • 77956620478 scopus 로고    scopus 로고
    • Investigation of the dynamical properties of water in elastin by deuterium double quantum filtered NMR
    • C. Sun, and G.S. Boutis Investigation of the dynamical properties of water in elastin by deuterium double quantum filtered NMR J. Magn. Reson. 205 2010 86 92
    • (2010) J. Magn. Reson. , vol.205 , pp. 86-92
    • Sun, C.1    Boutis, G.S.2
  • 45
    • 79952254253 scopus 로고    scopus 로고
    • Measurement of the exchange rate of waters of hydration in elastin by 2D T2-T2 correlation nuclear magnetic resonance spectroscopy
    • C. Sun, and G.S. Boutis Measurement of the exchange rate of waters of hydration in elastin by 2D T2-T2 correlation nuclear magnetic resonance spectroscopy New J. Phys. 13 2011 025026 025042
    • (2011) New J. Phys. , vol.13 , pp. 025026-025042
    • Sun, C.1    Boutis, G.S.2
  • 46
    • 0017437920 scopus 로고
    • Humidity fixed points of binary saturated aqueous solutions
    • L. Greenspan Humidity fixed points of binary saturated aqueous solutions J. Res. Natl. Bur. Stand. A Phys. Chem. 81A 1977 89 96
    • (1977) J. Res. Natl. Bur. Stand. A Phys. Chem. , vol.81 A , pp. 89-96
    • Greenspan, L.1
  • 47
    • 0002947095 scopus 로고
    • G.M. Sessler, Topics in Applied Physics Springer Berlin
    • J. van Turnhout G.M. Sessler, Electrets Topics in Applied Physics vol. 33 1980 Springer Berlin 81 215
    • (1980) Electrets , vol.33 VOL. , pp. 81-215
    • Van Turnhout, J.1
  • 49
    • 51149207143 scopus 로고
    • Dispersion and absorption in dielectrics II. Direct current characteristics
    • R.H. Cole, and K.S. Cole Dispersion and absorption in dielectrics II. Direct current characteristics J. Chem. Phys. 10 1942 98 105
    • (1942) J. Chem. Phys. , vol.10 , pp. 98-105
    • Cole, R.H.1    Cole, K.S.2
  • 50
    • 84878112518 scopus 로고    scopus 로고
    • http:/grafitylabs.com
  • 52
    • 37049074769 scopus 로고
    • A BET-like three sorption stage isotherm
    • E.O. Timmermann A BET-like three sorption stage isotherm J. Chem. Soc. Faraday Trans. 1 85 1989 1631 1645
    • (1989) J. Chem. Soc. Faraday Trans. , vol.1 , Issue.85 , pp. 1631-1645
    • Timmermann, E.O.1
  • 53
    • 79952636175 scopus 로고    scopus 로고
    • Appearance of a Debye process at the conductivity relaxation frequency of a viscous liquid
    • R. Richert, A. Agapov, and A.P. Sokolov Appearance of a Debye process at the conductivity relaxation frequency of a viscous liquid J. Chem. Phys. 134 2011 104508 104514
    • (2011) J. Chem. Phys. , vol.134 , pp. 104508-104514
    • Richert, R.1    Agapov, A.2    Sokolov, A.P.3
  • 54
    • 34848865925 scopus 로고    scopus 로고
    • An infrared spectroscopic study of the conformational transition of elastin-like polypeptides
    • V. Serrano, W. Liu, and S. Franzen An infrared spectroscopic study of the conformational transition of elastin-like polypeptides Biophys. J. 93 2007 2429 2435
    • (2007) Biophys. J. , vol.93 , pp. 2429-2435
    • Serrano, V.1    Liu, W.2    Franzen, S.3
  • 55
    • 5644229523 scopus 로고    scopus 로고
    • Elastic effects behind cooperative bonding in beta-sheets
    • J. Rosmmeisl, J.K. Nørskov, and K.W. Jakobsen Elastic effects behind cooperative bonding in beta-sheets J. Am. Chem. Soc. 126 2004 13140 13143
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13140-13143
    • Rosmmeisl, J.1    Nørskov, J.K.2    Jakobsen, K.W.3
  • 56
    • 0023407692 scopus 로고
    • A study of casein hydration by the thermally stimulated depolarisation currents method
    • A. Anagnostopoulou-Konsta, and P. Pissis A study of casein hydration by the thermally stimulated depolarisation currents method J. Phys. D: Appl. Phys. 20 1987 1168 1174
    • (1987) J. Phys. D: Appl. Phys. , vol.20 , pp. 1168-1174
    • Anagnostopoulou-Konsta, A.1    Pissis, P.2
  • 57
    • 0022123547 scopus 로고
    • A study of sorbed water on cellulose by the thermally stimulated depolarization technique
    • P. Pissis A study of sorbed water on cellulose by the thermally stimulated depolarization technique J. Phys. D: Appl. Phys. 18 1985 1897 1908
    • (1985) J. Phys. D: Appl. Phys. , vol.18 , pp. 1897-1908
    • Pissis, P.1
  • 58
    • 0000577108 scopus 로고
    • Depolarization thermocurrents in frozen aqueous solutions of mono- and di-saccharides
    • D. Daoukaki-Diamanti, P. Pissis, and G. Boudouris Depolarization thermocurrents in frozen aqueous solutions of mono- and di-saccharides Chem. Phys. 91 1984 315 325
    • (1984) Chem. Phys. , vol.91 , pp. 315-325
    • Daoukaki-Diamanti, D.1    Pissis, P.2    Boudouris, G.3
  • 59
    • 0031169621 scopus 로고    scopus 로고
    • Water binding to biopolymers in different cereals and legumes: Proton NMR relaxation, dielectric and water imbibition studies
    • S. Ratkovic, and P. Pissis Water binding to biopolymers in different cereals and legumes: Proton NMR relaxation, dielectric and water imbibition studies J. Mater. Sci. 32 1997 3061 3068
    • (1997) J. Mater. Sci. , vol.32 , pp. 3061-3068
    • Ratkovic, S.1    Pissis, P.2
  • 60
    • 2042447908 scopus 로고
    • The dielectric relaxation of water in plant tissue
    • P. Pissis The dielectric relaxation of water in plant tissue J. Exp. Bot. 41 1990 677 684
    • (1990) J. Exp. Bot. , vol.41 , pp. 677-684
    • Pissis, P.1
  • 62
    • 0035814373 scopus 로고    scopus 로고
    • Hydrophobic hydration is an important source of elasticity in elastin-based polymers
    • B.L. Darwin, O.V. Alonso, B.J. Bennion, and V. Daggett Hydrophobic hydration is an important source of elasticity in elastin-based polymers J. Am. Chem. Soc. 123 2001 11991 11998
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11991-11998
    • Darwin, B.L.1    Alonso, O.V.2    Bennion, B.J.3    Daggett, V.4
  • 63
    • 79956104665 scopus 로고    scopus 로고
    • Resolving the ambiguity of the dynamics of water and clarifying its role in hydrated proteins
    • K.L. Ngai, S. Capaccioli, S. Ancherbak, and N. Shinyashiki Resolving the ambiguity of the dynamics of water and clarifying its role in hydrated proteins Philos. Mag. 91 2011 1809 1835
    • (2011) Philos. Mag. , vol.91 , pp. 1809-1835
    • Ngai, K.L.1    Capaccioli, S.2    Ancherbak, S.3    Shinyashiki, N.4
  • 65
    • 0000119222 scopus 로고
    • The law of the relationship between viscosity of liquids and the temperature
    • H. Vogel The law of the relationship between viscosity of liquids and the temperature Phys. Z. 22 1921 645 646
    • (1921) Phys. Z. , vol.22 , pp. 645-646
    • Vogel, H.1
  • 66
    • 0036039010 scopus 로고    scopus 로고
    • Structural characteristics in protein hydration investigated by cryogenic X-ray crystal structure analyses
    • M. Nakasako Structural characteristics in protein hydration investigated by cryogenic X-ray crystal structure analyses J. Biol. Phys. 28 2002 129 137
    • (2002) J. Biol. Phys. , vol.28 , pp. 129-137
    • Nakasako, M.1
  • 67
    • 34249856305 scopus 로고    scopus 로고
    • Glass transitions of ordinary and heavy water within silica-gel nanopores
    • M. Oguni, S. Maruyama, K. Wakabayashi, and A. Nagoe Glass transitions of ordinary and heavy water within silica-gel nanopores Chem. Asian J. 2 4 2007 514 520
    • (2007) Chem. Asian J. , vol.2 , Issue.4 , pp. 514-520
    • Oguni, M.1    Maruyama, S.2    Wakabayashi, K.3    Nagoe, A.4
  • 68
    • 0023061930 scopus 로고
    • Structure and dynamics of water surrounding biomolecules
    • W. Saenger Structure and dynamics of water surrounding biomolecules Annu. Rev. Biophys. Chem. 16 1987 93 114
    • (1987) Annu. Rev. Biophys. Chem. , vol.16 , pp. 93-114
    • Saenger, W.1
  • 69
    • 0019841713 scopus 로고
    • Free water in hair keratin? A depolarization thermal current study
    • J.L. Leveque, J.C. Carson, P. Pissis, and G. Boudouris Free water in hair keratin? A depolarization thermal current study Biopolymers 20 1981 2649 2656
    • (1981) Biopolymers , vol.20 , pp. 2649-2656
    • Leveque, J.L.1    Carson, J.C.2    Pissis, P.3    Boudouris, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.