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Volumn 23, Issue 5-6, 2002, Pages 561-573

Molecular basis for the extensibility of elastin

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ELASTIN; GLYCINE; LYSINE; PROLINE; PROTEIN PRECURSOR; TROPOELASTIN; VALINE; WATER;

EID: 0037569589     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023474909980     Document Type: Review
Times cited : (125)

References (130)
  • 1
    • 0019142643 scopus 로고
    • Optical properties of single elastin fibres indicate random protein conformation
    • Aaron BB and Gosline JM (1980) Optical properties of single elastin fibres indicate random protein conformation. Nature 287: 865-867.
    • (1980) Nature , vol.287 , pp. 865-867
    • Aaron, B.B.1    Gosline, J.M.2
  • 2
    • 0019490755 scopus 로고
    • Elastin as a random-network elastomer: A mechanical and optical analysis of single elastin fibers
    • Aaron BB and Gosline JM (1981) Elastin as a random-network elastomer: a mechanical and optical analysis of single elastin fibers. Biopolymers 20: 1247-1260.
    • (1981) Biopolymers , vol.20 , pp. 1247-1260
    • Aaron, B.B.1    Gosline, J.M.2
  • 4
    • 0031965674 scopus 로고    scopus 로고
    • Molecular dynamics simulations of hydrophobic collapse of ubiquitin
    • Alonso DOV and Daggett V (1998) Molecular dynamics simulations of hydrophobic collapse of ubiquitin. Protein Sci 7: 860-874.
    • (1998) Protein Sci , vol.7 , pp. 860-874
    • Alonso, D.O.V.1    Daggett, V.2
  • 5
    • 84985715920 scopus 로고
    • Thermoelasticity of swollen elastin networks at constant composition
    • Andrady AL and Mark JE (1980) Thermoelasticity of swollen elastin networks at constant composition. Biopolymers 19: 849-855.
    • (1980) Biopolymers , vol.19 , pp. 849-855
    • Andrady, A.L.1    Mark, J.E.2
  • 6
    • 0025297435 scopus 로고
    • Depsipeptide analogues of elastin repeating sequences: Conformational analysis
    • Arad O and Goodman M (1990) Depsipeptide analogues of elastin repeating sequences: conformational analysis. Biopolymers 29: 1652-1668.
    • (1990) Biopolymers , vol.29 , pp. 1652-1668
    • Arad, O.1    Goodman, M.2
  • 7
  • 9
    • 0038305379 scopus 로고    scopus 로고
    • A microscopic view of the solvation of peptides and proteins
    • in press
    • Beck DAC, Alonso DOV and Daggett V (2002) A microscopic view of the solvation of peptides and proteins. Biophys Chem, in press.
    • (2002) Biophys Chem
    • Beck, D.A.C.1    Alonso, D.O.V.2    Daggett, V.3
  • 10
    • 0038644308 scopus 로고
    • Spectroscopic studies of connective tissues - Native and hydrated elastin
    • Bertoluzza A, Bonora S, Fini G and Morelli MA (1989) Spectroscopic studies of connective tissues - native and hydrated elastin. Can J Spectrosc 34: 13-14.
    • (1989) Can J Spectrosc , vol.34 , pp. 13-14
    • Bertoluzza, A.1    Bonora, S.2    Fini, G.3    Morelli, M.A.4
  • 11
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best RB, Li B, Steward A, Daggett V and Clarke J (2001) Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J 81: 2344-2356.
    • (2001) Biophys J , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 12
    • 0032483056 scopus 로고    scopus 로고
    • The amino acid sequence coded by the rarely expressed exon 26A of human elastin contains a stable beta-turn with chemotactic activity for monocytes
    • Bisaccia F, Castiglione-Morelli MA, Spisani S, Ostuni A, Serafini-Fracassini A, Bavoso A and Tamburro AM (1998) The amino acid sequence coded by the rarely expressed exon 26A of human elastin contains a stable beta-turn with chemotactic activity for monocytes. Biochemistry 37: 11,128-11,135.
    • (1998) Biochemistry , vol.37 , pp. 11128-11135
    • Bisaccia, F.1    Castiglione-Morelli, M.A.2    Spisani, S.3    Ostuni, A.4    Serafini-Fracassini, A.5    Bavoso, A.6    Tamburro, A.M.7
  • 13
    • 0012811428 scopus 로고
    • Identification of beta, beta-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism
    • Brahms S, Brahms J, Spach G and Brack A (1977) Identification of beta, beta-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism. Proc Natl Acad Sci USA 74: 3208-3212.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3208-3212
    • Brahms, S.1    Brahms, J.2    Spach, G.3    Brack, A.4
  • 14
    • 0023663346 scopus 로고
    • Repeating structure of chick tropoelastin revealed by complementary DNA cloning
    • Bressan GM, Argos P and Stanley KK (1987) Repeating structure of chick tropoelastin revealed by complementary DNA cloning. Biochemistry 26: 1497-1503.
    • (1987) Biochemistry , vol.26 , pp. 1497-1503
    • Bressan, G.M.1    Argos, P.2    Stanley, K.K.3
  • 15
    • 0029967225 scopus 로고    scopus 로고
    • Conformational and electrostatic properties of V-G-G-V-G, a typical sequence of the glycine-rich regions of elastin. An ab initio quantum molecular study
    • Broch H, Moulabbi M, Vasilescu D and Tamburro AM (1996) Conformational and electrostatic properties of V-G-G-V-G, a typical sequence of the glycine-rich regions of elastin. An ab initio quantum molecular study. Int J Pept Protein Res 47: 394-404.
    • (1996) Int J Pept Protein Res , vol.47 , pp. 394-404
    • Broch, H.1    Moulabbi, M.2    Vasilescu, D.3    Tamburro, A.M.4
  • 16
    • 0031860996 scopus 로고    scopus 로고
    • Quantum molecular modeling of the elastinic tetrapeptide Val-Pro-Gly-Gly
    • Broch H, Moulabbi M, Vasilescu D and Tamburro AM (1998) Quantum molecular modeling of the elastinic tetrapeptide Val-Pro-Gly-Gly. J Biomol Struct Dyn 15: 1073-1091.
    • (1998) J Biomol Struct Dyn , vol.15 , pp. 1073-1091
    • Broch, H.1    Moulabbi, M.2    Vasilescu, D.3    Tamburro, A.M.4
  • 17
    • 0026641004 scopus 로고
    • The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket
    • Brown PL, Mecham L, Tisdale C and Mecham RP (1992) The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket. Biochem Biophys Res Commun 186: 549-555.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 549-555
    • Brown, P.L.1    Mecham, L.2    Tisdale, C.3    Mecham, R.P.4
  • 19
    • 0029811144 scopus 로고    scopus 로고
    • Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly
    • Brown-Augsburger P, Broekelmann T, Rosenbloom J and Mecham RP (1996) Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly. Biochem J 318 (Pt 1): 149-155.
    • (1996) Biochem J , vol.318 , Issue.PART 1 , pp. 149-155
    • Brown-Augsburger, P.1    Broekelmann, T.2    Rosenbloom, J.3    Mecham, R.P.4
  • 20
    • 0029051024 scopus 로고
    • Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly
    • Brown-Augsburger P, Tisdale C, Broekelmann T, Sloan C and Mecham RP (1995) Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly. J Biol Chem 270: 17,778-17,783.
    • (1995) J Biol Chem , vol.270 , pp. 17778-17783
    • Brown-Augsburger, P.1    Tisdale, C.2    Broekelmann, T.3    Sloan, C.4    Mecham, R.P.5
  • 23
    • 84988073226 scopus 로고
    • Polypentapeptide of elastin damping of internal chain dynamics on extension
    • Chang DK and Urry DW (1989) Polypentapeptide of elastin damping of internal chain dynamics on extension. J Comput Chem 10: 850-855.
    • (1989) J Comput Chem , vol.10 , pp. 850-855
    • Chang, D.K.1    Urry, D.W.2
  • 24
    • 0024519055 scopus 로고
    • Nuclear overhauser effect and computational characterization of the beta-spiral of the polypentapeptide of elastin
    • Chang DK, Venkatachalam CM, Prasad KU and Urry DW (1989) Nuclear overhauser effect and computational characterization of the beta-spiral of the polypentapeptide of elastin. J Biomol Struct Dyn 6: 851-858.
    • (1989) J Biomol Struct Dyn , vol.6 , pp. 851-858
    • Chang, D.K.1    Venkatachalam, C.M.2    Prasad, K.U.3    Urry, D.W.4
  • 25
    • 0000154289 scopus 로고
    • Crystal structure and conformation of the cyclic trimer of a repeat pentapeptide of elastin, cyclo-(L-valyl-L-prolyglycyl-L-valylglycyl)3
    • Cook WJ, Einspahr H, Trapane TL, Urry DW and Bugg CE (1980) Crystal structure and conformation of the cyclic trimer of a repeat pentapeptide of elastin, cyclo-(L-valyl-L-prolyglycyl-L-valylglycyl)3. J Am Chem Soc 102: 5502-5505.
    • (1980) J Am Chem Soc , vol.102 , pp. 5502-5505
    • Cook, W.J.1    Einspahr, H.2    Trapane, T.L.3    Urry, D.W.4    Bugg, C.E.5
  • 26
    • 0024307263 scopus 로고
    • Electron microscopic evidence for elastin-like supramolecular organization in synthetic polytripeptides
    • Daga Gordini D, Guantieri V and Tamburro AM (1989) Electron microscopic evidence for elastin-like supramolecular organization in synthetic polytripeptides. Connect Tissue Res 19: 27-34.
    • (1989) Connect Tissue Res , vol.19 , pp. 27-34
    • Daga Gordini, D.1    Guantieri, V.2    Tamburro, A.M.3
  • 27
    • 0012605164 scopus 로고
    • A molecular-dynamics simulation of the C-terminal fragment of the L7/L12 ribosomal-protein in solution
    • Daggett V and Levitt M (1991) A molecular-dynamics simulation of the C-terminal fragment of the L7/L12 ribosomal-protein in solution. Chem Phys Lett 158: 501-512.
    • (1991) Chem Phys Lett , vol.158 , pp. 501-512
    • Daggett, V.1    Levitt, M.2
  • 28
    • 0032751580 scopus 로고    scopus 로고
    • The structures of elastins and their function
    • Debelle L and Alix AJ (1999) The structures of elastins and their function. Biochimie 81: 981-994.
    • (1999) Biochimie , vol.81 , pp. 981-994
    • Debelle, L.1    Alix, A.J.2
  • 29
    • 0028874868 scopus 로고
    • Bovine elastin and kappa-elastin secondary structure determination by optical spectroscopies
    • Debelle L, Alix AJ, Jacob MP, Huvenne JP, Berjot M, Sombret B and Legrand P (1995) Bovine elastin and kappa-elastin secondary structure determination by optical spectroscopies. J Biol Chem 270: 26,099-26,103.
    • (1995) J Biol Chem , vol.270 , pp. 26099-26103
    • Debelle, L.1    Alix, A.J.2    Jacob, M.P.3    Huvenne, J.P.4    Berjot, M.5    Sombret, B.6    Legrand, P.7
  • 31
    • 0017075586 scopus 로고
    • Nuclear spin-relaxation studies of hydrated elastin
    • Ellis GE and Packer KJ (1976) Nuclear spin-relaxation studies of hydrated elastin. Biopolymers 15: 813-832.
    • (1976) Biopolymers , vol.15 , pp. 813-832
    • Ellis, G.E.1    Packer, K.J.2
  • 32
    • 0018869702 scopus 로고
    • Characterization of molecular motions in 13C-labeled aortic elastin by 13C-1H magnetic double resonance
    • Fleming WW, Sullivan CE and Torchia DA (1980) Characterization of molecular motions in 13C-labeled aortic elastin by 13C-1H magnetic double resonance. Biopolymers 19: 597-617.
    • (1980) Biopolymers , vol.19 , pp. 597-617
    • Fleming, W.W.1    Sullivan, C.E.2    Torchia, D.A.3
  • 33
    • 0000964680 scopus 로고
    • Effect of volume exclusion on the dimensions of polymer chains
    • Flory PJ and Fisk S (1966) Effect of volume exclusion on the dimensions of polymer chains. J Chem Phys 44: 2243-2248.
    • (1966) J Chem Phys , vol.44 , pp. 2243-2248
    • Flory, P.J.1    Fisk, S.2
  • 34
    • 0015935408 scopus 로고
    • Isolation and amino acid sequences of tropoelastin peptides
    • Foster JA, Bruenger E, Gray WR and Sandberg LB (1973) Isolation and amino acid sequences of tropoelastin peptides. J Biol Chem 248: 2876-2879.
    • (1973) J Biol Chem , vol.248 , pp. 2876-2879
    • Foster, J.A.1    Bruenger, E.2    Gray, W.R.3    Sandberg, L.B.4
  • 36
    • 0016630191 scopus 로고
    • Raman scattering of collagen, gelatin, and elastin
    • Frushour BG and Koenig JL (1975) Raman scattering of collagen, gelatin, and elastin. Biopolymers 14: 379-391.
    • (1975) Biopolymers , vol.14 , pp. 379-391
    • Frushour, B.G.1    Koenig, J.L.2
  • 38
    • 0024521529 scopus 로고
    • The protein components of the 12-nanometer microfibrils of elastic and nonelastic tissues
    • Gibson MA, Kumaratilake JS and Cleary EG (1989) The protein components of the 12-nanometer microfibrils of elastic and nonelastic tissues. J Biol Chem 264: 4590-4598.
    • (1989) J Biol Chem , vol.264 , pp. 4590-4598
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 39
    • 0025887137 scopus 로고
    • Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils
    • Gibson MA, Sandberg LB, Grosso LE and Cleary EG (1991) Complementary DNA cloning establishes microfibril-associated glycoprotein (MAGP) to be a discrete component of the elastin-associated microfibrils. J Biol Chem 266: 7596-7601.
    • (1991) J Biol Chem , vol.266 , pp. 7596-7601
    • Gibson, M.A.1    Sandberg, L.B.2    Grosso, L.E.3    Cleary, E.G.4
  • 40
    • 0017849526 scopus 로고
    • Hydrophobic interaction and a model for the elasticity of elastin
    • Gosline JM (1978a) Hydrophobic interaction and a model for the elasticity of elastin. Biopolymers 17: 677-695.
    • (1978) Biopolymers , vol.17 , pp. 677-695
    • Gosline, J.M.1
  • 41
    • 0017818044 scopus 로고
    • The temperature-dependent swelling of elastin
    • Gosline JM (1978b) The temperature-dependent swelling of elastin. Biopolymers 17: 697-707.
    • (1978) Biopolymers , vol.17 , pp. 697-707
    • Gosline, J.M.1
  • 42
    • 0018294163 scopus 로고
    • Dynamic mechanical properties of elastin
    • Gosline JM and French CJ (1979) Dynamic mechanical properties of elastin. Biopolymers 18: 2091-2103.
    • (1979) Biopolymers , vol.18 , pp. 2091-2103
    • Gosline, J.M.1    French, C.J.2
  • 43
    • 0016718521 scopus 로고
    • Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis
    • Gosline JM, Yew FF and Weis-fogh T (1975) Reversible structural changes in a hydrophobic protein, elastin, as indicated by fluorescence probe analysis. Biopolymers 14: 1811-1826.
    • (1975) Biopolymers , vol.14 , pp. 1811-1826
    • Gosline, J.M.1    Yew, F.F.2    Weis-fogh, T.3
  • 44
    • 2042480091 scopus 로고
    • Some structural aspects of elastin revealed by X-ray diffraction and other physical methods
    • Gotte L, Mammi M and Pezzin G (1977) Some structural aspects of elastin revealed by X-ray diffraction and other physical methods. Adv Exp Med Biol 79: 236-245.
    • (1977) Adv Exp Med Biol , vol.79 , pp. 236-245
    • Gotte, L.1    Mammi, M.2    Pezzin, G.3
  • 46
    • 0015932437 scopus 로고
    • Molecular model for elastin structure and function
    • Gray WR, Sandberg LB and Foster JA (1973) Molecular model for elastin structure and function. Nature 246: 461-466.
    • (1973) Nature , vol.246 , pp. 461-466
    • Gray, W.R.1    Sandberg, L.B.2    Foster, J.A.3
  • 47
    • 0023143335 scopus 로고
    • Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro)
    • Guantieri V, Tamburro AM, Cabrol D, Broch H and Vasilescu D (1987) Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro). Int J Pept Protein Res 29: 216-230.
    • (1987) Int J Pept Protein Res , vol.29 , pp. 216-230
    • Guantieri, V.1    Tamburro, A.M.2    Cabrol, D.3    Broch, H.4    Vasilescu, D.5
  • 48
    • 0001001748 scopus 로고
    • Dielectric relaxation studies demonstrate a peptide librational mode in the polypentapeptide of elastin
    • Henze R and Urry DW (1985) Dielectric relaxation studies demonstrate a peptide librational mode in the polypentapeptide of elastin. J Am Chem Soc 107: 2991-2993.
    • (1985) J Am Chem Soc , vol.107 , pp. 2991-2993
    • Henze, R.1    Urry, D.W.2
  • 49
    • 0030983421 scopus 로고    scopus 로고
    • Expression of a synthetic protein-based polymer (elastomer) gene in Aspergillus nidulans
    • Herzog RW, Singh NK, Urry DW and Daniell H (1997) Expression of a synthetic protein-based polymer (elastomer) gene in Aspergillus nidulans. Appl Microbiol Biotechnol 47: 368-372.
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 368-372
    • Herzog, R.W.1    Singh, N.K.2    Urry, D.W.3    Daniell, H.4
  • 50
    • 0002688989 scopus 로고    scopus 로고
    • Elastic properties of poly(ethylene-glycol) studied by molecular dynamic stretching simulation
    • Heymann B and Grubmuller H (1999) Elastic properties of poly(ethylene-glycol) studied by molecular dynamic stretching simulation. Chem Phys Lett 307: 425-432.
    • (1999) Chem Phys Lett , vol.307 , pp. 425-432
    • Heymann, B.1    Grubmuller, H.2
  • 51
    • 0027396755 scopus 로고
    • The ductus arteriosus migratory smooth muscle cell phenotype processes tropoelastin to a 52-kDa product associated with impaired assembly of elastic laminae
    • Hinek A and Rabinovitch M (1993) The ductus arteriosus migratory smooth muscle cell phenotype processes tropoelastin to a 52-kDa product associated with impaired assembly of elastic laminae. J Biol Chem 268: 1405-1413.
    • (1993) J Biol Chem , vol.268 , pp. 1405-1413
    • Hinek, A.1    Rabinovitch, M.2
  • 52
    • 0016168148 scopus 로고
    • The elastic properties of elastin
    • Hoeve CA and Flory PJ (1974) The elastic properties of elastin. Biopolymers 13: 677-686.
    • (1974) Biopolymers , vol.13 , pp. 677-686
    • Hoeve, C.A.1    Flory, P.J.2
  • 53
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology; University College, London
    • Hubbard SJ and Thorton JM (1993) NACCESS, Computer Program. Department of Biochemistry and Molecular Biology; University College, London.
    • (1993) NACCESS, Computer Program
    • Hubbard, S.J.1    Thorton, J.M.2
  • 55
    • 0023062132 scopus 로고
    • Structure of the 3′ region of the human elastin gene: Great abundance of Alu repetitive sequences and few coding sequences
    • Indik Z, Yoon K, Morrow SD, Cicila G, Rosenbloom J and Ornstein-Goldstein N (1987b) Structure of the 3′ region of the human elastin gene: great abundance of Alu repetitive sequences and few coding sequences. Connect Tissue Res 16: 197-211.
    • (1987) Connect Tissue Res , vol.16 , pp. 197-211
    • Indik, Z.1    Yoon, K.2    Morrow, S.D.3    Cicila, G.4    Rosenbloom, J.5    Ornstein-Goldstein, N.6
  • 57
    • 0030568435 scopus 로고    scopus 로고
    • Testing the modified hydration-shell hydrogen-bond model of hydrophobic effects using molecular dynamics simulation
    • Laidig KE and Daggett V (1996) Testing the modified hydration-shell hydrogen-bond model of hydrophobic effects using molecular dynamics simulation. J Phys Chem 100: 5616-5619.
    • (1996) J Phys Chem , vol.100 , pp. 5616-5619
    • Laidig, K.E.1    Daggett, V.2
  • 58
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B and Richards FM (1971) The interpretation of protein structures: estimation of static accessibility. J Mol Biol 55: 379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 59
    • 0034894236 scopus 로고    scopus 로고
    • Elastomeric polypentapeptides cross-linked into matrices and fibers
    • Lee J, Macosko CW and Urry DW (2001) Elastomeric polypentapeptides cross-linked into matrices and fibers. Biomacromolecules 2: 170-179.
    • (2001) Biomacromolecules , vol.2 , pp. 170-179
    • Lee, J.1    Macosko, C.W.2    Urry, D.W.3
  • 60
    • 0026566808 scopus 로고
    • Molecular dynamics study of the conformational behavior of a representative elastin building block: Boc-Gly-Val-Gly-Gly-Leu-OMe
    • Lelj F, Tamburro AM, Villani V, Grimaldi P and Guantieri V (1992) Molecular dynamics study of the conformational behavior of a representative elastin building block: Boc-Gly-Val-Gly-Gly-Leu-OMe. Biopolymers 32: 161-172.
    • (1992) Biopolymers , vol.32 , pp. 161-172
    • Lelj, F.1    Tamburro, A.M.2    Villani, V.3    Grimaldi, P.4    Guantieri, V.5
  • 61
    • 0035814373 scopus 로고    scopus 로고
    • Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers
    • Li B, Alonso DOV, Bennion BJ and Daggett V (2001b) Hydrophobic hydration is an important source of elasticity in elastin-based biopolymers. J Am Chem Soc 123: 11,991-11,998.
    • (2001) J Am Chem Soc , vol.123 , pp. 11991-11998
    • Li, B.1    Alonso, D.O.V.2    Bennion, B.J.3    Daggett, V.4
  • 62
    • 0035910282 scopus 로고    scopus 로고
    • The molecular basis for the inverse temperature transition of elastin
    • Li B, Alonso DOV and Daggett V (2001a) The molecular basis for the inverse temperature transition of elastin. J Mol Biol 305: 581-592.
    • (2001) J Mol Biol , vol.305 , pp. 581-592
    • Li, B.1    Alonso, D.O.V.2    Daggett, V.3
  • 63
    • 0025325403 scopus 로고
    • The effects of hydration on the dynamic mechanical properties of elastin
    • Lillie MA and Gosline JM (1990) The effects of hydration on the dynamic mechanical properties of elastin. Biopolymers 29: 1147-1160.
    • (1990) Biopolymers , vol.29 , pp. 1147-1160
    • Lillie, M.A.1    Gosline, J.M.2
  • 65
    • 84990714230 scopus 로고
    • On the source of entropic elastomeric force in polypeptides and proteins: Backbone configurational vs. side-chain solvational entropy
    • Luan C, Jaggard J, Harris D and Urry DW (1989) On the source of entropic elastomeric force in polypeptides and proteins: backbone configurational vs. side-chain solvational entropy. Int J Quant Chem: Quant Biol Symp 16: 235-244.
    • (1989) Int J Quant Chem: Quant Biol Symp , vol.16 , pp. 235-244
    • Luan, C.1    Jaggard, J.2    Harris, D.3    Urry, D.W.4
  • 66
    • 0026924813 scopus 로고
    • Hydrophobicity of amino acid residues: Differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin
    • Luan CH, Parker TM, Gowda DC and Urry DW (1992) Hydrophobicity of amino acid residues: differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin. Biopolymers 32: 1251-1261.
    • (1992) Biopolymers , vol.32 , pp. 1251-1261
    • Luan, C.H.1    Parker, T.M.2    Gowda, D.C.3    Urry, D.W.4
  • 67
    • 0016724586 scopus 로고
    • Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data
    • Lyerla JR Jr and Torchia DA (1975) Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data. Biochemistry 14: 5175-5183.
    • (1975) Biochemistry , vol.14 , pp. 5175-5183
    • Lyerla J.R., Jr.1    Torchia, D.A.2
  • 68
    • 0014431328 scopus 로고
    • Evidence for order in the structure of alpha-elastin
    • Mammi M, Gotte L and Pezzin G (1968) Evidence for order in the structure of alpha-elastin. Nature 220: 371-373.
    • (1968) Nature , vol.220 , pp. 371-373
    • Mammi, M.1    Gotte, L.2    Pezzin, G.3
  • 69
    • 0014960152 scopus 로고
    • Comparison of soluble and native elastin conformations by far-ultraviolet circular dichroism
    • Mammi M, Gotte L and Pezzin G (1970) Comparison of soluble and native elastin conformations by far-ultraviolet circular dichroism. Nature 225: 380-381.
    • (1970) Nature , vol.225 , pp. 380-381
    • Mammi, M.1    Gotte, L.2    Pezzin, G.3
  • 71
    • 0026892823 scopus 로고
    • Production and purification of a recombinant elastomeric polypeptide, G-(VPGVG)19-VPGV, from Escherichia coli
    • McPherson DT, Morrow C, Minehan DS, Wu J, Hunter E and Urry DW (1992) Production and purification of a recombinant elastomeric polypeptide, G-(VPGVG)19-VPGV, from Escherichia coli. Biotechnol Prog 8: 347-352.
    • (1992) Biotechnol Prog , vol.8 , pp. 347-352
    • McPherson, D.T.1    Morrow, C.2    Minehan, D.S.3    Wu, J.4    Hunter, E.5    Urry, D.W.6
  • 75
    • 0001832838 scopus 로고    scopus 로고
    • Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water
    • Oesterhelt F, Rief M and Gaub HE (1999) Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water. New J Phys 1: 6.1-6.11.
    • (1999) New J Phys , vol.1 , pp. 61-611
    • Oesterhelt, F.1    Rief, M.2    Gaub, H.E.3
  • 78
    • 0025130777 scopus 로고
    • Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning
    • Pierce RA, Deak SB, Stolle CA and Boyd CD (1990) Heterogeneity of rat tropoelastin mRNA revealed by cDNA cloning. Biochemistry 29: 9677-9683.
    • (1990) Biochemistry , vol.29 , pp. 9677-9683
    • Pierce, R.A.1    Deak, S.B.2    Stolle, C.A.3    Boyd, C.D.4
  • 79
    • 0002573220 scopus 로고
    • Greehalgh RM and Marrick JA (eds). W.B. Saunders, London
    • Powell JT (1990) In: Greehalgh RM and Marrick JA (eds) The cause and Management of Aneurysms (pp. 89-96) W.B. Saunders, London.
    • (1990) The Cause and Management of Aneurysms , pp. 89-96
    • Powell, J.T.1
  • 80
    • 0023353716 scopus 로고
    • Raman spectrum and structure of elastin in relation to type-II beta-turns
    • Prescott B, Renugopalakrishnan V and Thomas GJ Jr (1987) Raman spectrum and structure of elastin in relation to type-II beta-turns. Biopolymers 26: 934-936.
    • (1987) Biopolymers , vol.26 , pp. 934-936
    • Prescott, B.1    Renugopalakrishnan, V.2    Thomas G.J., Jr.3
  • 81
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • Raju K and Anwar RA (1987a) Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. J Biol Chem 262: 5755-5762.
    • (1987) J Biol Chem , vol.262 , pp. 5755-5762
    • Raju, K.1    Anwar, R.A.2
  • 82
    • 0023664380 scopus 로고
    • Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones
    • Raju K and Anwar RA (1987b) Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. J Biol Chem 262: 5755-5762.
    • (1987) J Biol Chem , vol.262 , pp. 5755-5762
    • Raju, K.1    Anwar, R.A.2
  • 83
    • 0026643352 scopus 로고
    • Enzymatic and nonenzymatic cross-linking of collagen and elastin
    • Reiser K, McCormick RJ and Rucker RB (1992) Enzymatic and nonenzymatic cross-linking of collagen and elastin. FASEB J 6: 2439-2449.
    • (1992) FASEB J , vol.6 , pp. 2439-2449
    • Reiser, K.1    McCormick, R.J.2    Rucker, R.B.3
  • 84
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • Rosenbloom J, Abrams WR and Mecham R (1993) Extracellular matrix 4: the elastic fiber. Faseb J 7: 1208-1218.
    • (1993) Faseb J , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 85
    • 0001237577 scopus 로고
    • Phase transition behavior of the isolated polymer chain
    • Sanchez IC (1979) Phase transition behavior of the isolated polymer chain. Macromolecules 12: 980-988.
    • (1979) Macromolecules , vol.12 , pp. 980-988
    • Sanchez, I.C.1
  • 87
    • 0024230245 scopus 로고
    • Nucleation and accretion of bioelastomeric fibers at biological temperatures and low concentrations
    • Sciortino F, Palma MU, Urry DW and Prasad KU (1988) Nucleation and accretion of bioelastomeric fibers at biological temperatures and low concentrations. Biochem Biophys Res Commun 157: 1061-1066.
    • (1988) Biochem Biophys Res Commun , vol.157 , pp. 1061-1066
    • Sciortino, F.1    Palma, M.U.2    Urry, D.W.3    Prasad, K.U.4
  • 88
    • 0016893216 scopus 로고
    • The macromolecular organization of the elastin fibril
    • Serafini-Fracassini A, Field JM and Spina M (1976) The macromolecular organization of the elastin fibril. J Mol Biol 100: 73-84.
    • (1976) J Mol Biol , vol.100 , pp. 73-84
    • Serafini-Fracassini, A.1    Field, J.M.2    Spina, M.3
  • 89
    • 0019482068 scopus 로고
    • Elastin: Molecular and supramolecular structure
    • Tamburro AM (1981) Elastin: molecular and supramolecular structure. Prog Clin Biol Res 54: 45-62.
    • (1981) Prog Clin Biol Res , vol.54 , pp. 45-62
    • Tamburro, A.M.1
  • 90
    • 0022384546 scopus 로고
    • Poly(Pro-Nle-Gly): Can an amorphus polypeptide take up a supramolecular elastinlike structure?
    • Tamburro AM and Daga Gordini D (1985) Poly(Pro-Nle-Gly): can an amorphus polypeptide take up a supramolecular elastinlike structure? Biopolymers 24: 1853-1861.
    • (1985) Biopolymers , vol.24 , pp. 1853-1861
    • Tamburro, A.M.1    Daga Gordini, D.2
  • 91
  • 93
    • 0018264857 scopus 로고
    • Concentration-dependent conformational transition of alpha-elastin in aqueous solution
    • Tamburro AM, Guantieri V, Daga-Gordini D and Abatangelo G (1978) Concentration-dependent conformational transition of alpha-elastin in aqueous solution. J Biol Chem 253: 2893-2894.
    • (1978) J Biol Chem , vol.253 , pp. 2893-2894
    • Tamburro, A.M.1    Guantieri, V.2    Daga-Gordini, D.3    Abatangelo, G.4
  • 94
    • 0027068138 scopus 로고
    • Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly)
    • Tamburro AM, Guantieri V and Gordini DD (1992) Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly). J Biomol Struct Dyn 10: 441-454.
    • (1992) J Biomol Struct Dyn , vol.10 , pp. 441-454
    • Tamburro, A.M.1    Guantieri, V.2    Gordini, D.D.3
  • 95
    • 0025944530 scopus 로고
    • Polypeptide models of elastin: CD and NMR studies on synthetic poly(X-Gly-Gly)
    • Tamburro AM, Guantieri V, Scopa A and Drabble JM (1991) Polypeptide models of elastin: CD and NMR studies on synthetic poly(X-Gly-Gly). Chirality 3: 318-323.
    • (1991) Chirality , vol.3 , pp. 318-323
    • Tamburro, A.M.1    Guantieri, V.2    Scopa, A.3    Drabble, J.M.4
  • 96
    • 0001554681 scopus 로고
    • Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin
    • Teeter MM (1984) Water structure of a hydrophobic protein at atomic resolution: pentagon rings of water molecules in crystals of crambin. Proc Natl Acad Sci USA 81: 6014-6018.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6014-6018
    • Teeter, M.M.1
  • 97
    • 0001371421 scopus 로고
    • Partial structure of two degradation products from the cross-linkages in elastin
    • Thomas JM, Elsden DF and Partridge SM (1963) Partial structure of two degradation products from the cross-linkages in elastin. Nature 200: 651-652.
    • (1963) Nature , vol.200 , pp. 651-652
    • Thomas, J.M.1    Elsden, D.F.2    Partridge, S.M.3
  • 98
    • 0023354464 scopus 로고
    • Raman amide bands of type-lI beta-turns in cyclo-(VPGVG)3 and poly-(VPGVG), and implications for protein secondary-structure analysis
    • Thomas GJ Jr, Prescott B and Urry DW (1987) Raman amide bands of type-lI beta-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 G.J., Jr.1    Prescott, B.2    Urry, D.W.3
  • 99
    • 0015935567 scopus 로고
    • Mobility of elastin chains as determined by 13C nuclear magnetic resonance
    • Torchia DA and Piez KA (1973) Mobility of elastin chains as determined by 13C nuclear magnetic resonance. J Mol Biol 76: 419-424.
    • (1973) J Mol Biol , vol.76 , pp. 419-424
    • Torchia, D.A.1    Piez, K.A.2
  • 100
    • 0034111432 scopus 로고    scopus 로고
    • The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin
    • Trask BC, Trask TM, Broekelmann T and Mecham RP (2000a) The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Mol Biol Cell 11: 1499-1507.
    • (2000) Mol Biol Cell , vol.11 , pp. 1499-1507
    • Trask, B.C.1    Trask, T.M.2    Broekelmann, T.3    Mecham, R.P.4
  • 101
    • 0034637534 scopus 로고    scopus 로고
    • Interaction of tropoelastin with the amino-terminal domains of fibrillin-1 and fibrillin-2 suggests a role for the fibrillins in elastic fiber assembly
    • Trask TM, Trask BC, Ritty TM, Abrams WR, Rosenbloom J and Mecham RP (2000b) Interaction of tropoelastin with the amino-terminal domains of fibrillin-1 and fibrillin-2 suggests a role for the fibrillins in elastic fiber assembly. J Biol Chem 275: 24,400-24,406.
    • (2000) J Biol Chem , vol.275 , pp. 24400-24406
    • Trask, T.M.1    Trask, B.C.2    Ritty, T.M.3    Abrams, W.R.4    Rosenbloom, J.5    Mecham, R.P.6
  • 102
    • 0020021572 scopus 로고
    • Cunningham LW and Frederiksen DW, (eds). Academic Press, New york
    • Urry DW (1982) In: Cunningham LW and Frederiksen DW, (eds) Methods in Enzymology (pp. 673-716) Academic Press, New york.
    • (1982) Methods in Enzymology , pp. 673-716
    • Urry, D.W.1
  • 103
    • 0020554865 scopus 로고
    • What is elastin; what is not
    • Urry DW (1983) What is elastin; what is not. Ultrastruct Pathol 4: 227-251.
    • (1983) Ultrastruct Pathol , vol.4 , pp. 227-251
    • Urry, D.W.1
  • 104
    • 0026468684 scopus 로고
    • Free energy transduction in polypeptides and proteins based on inverse temperature transitions
    • Urry DW (1992) Free energy transduction in polypeptides and proteins based on inverse temperature transitions. Prog Biophys Mol Biol 57: 23-57.
    • (1992) Prog Biophys Mol Biol , vol.57 , pp. 23-57
    • Urry, D.W.1
  • 105
    • 33748232872 scopus 로고
    • Molecular machines - How motion and other functions of living organisms can result from reversible chemical-changes
    • Urry DW (1993) Molecular machines - how motion and other functions of living organisms can result from reversible chemical-changes. Angew Chem-Int Edition English 32: 819-841.
    • (1993) Angew Chem-Int Edition English , vol.32 , pp. 819-841
    • Urry, D.W.1
  • 106
    • 84990716086 scopus 로고
    • A librational entropy mechanism for elastimers with repeating peptide sequences in helical array
    • Urry DW and Venkatachalam CM (1983) A librational entropy mechanism for elastimers with repeating peptide sequences in helical array. Int J Quant Chem: Quant Biol Syrup 10: 81-93.
    • (1983) Int J Quant Chem: Quant Biol Syrup , vol.10 , pp. 81-93
    • Urry, D.W.1    Venkatachalam, C.M.2
  • 107
    • 0024508521 scopus 로고
    • Two-dimensional proton NMR studies on poly(VPGVG) and its cyclic conformational correlate, cyclo(VPGVG)3
    • Urry DW, Chang DK, Krishna NR, Huang DH, Trapane TL and Prasad KU (1989) Two-dimensional proton NMR studies on poly(VPGVG) and its cyclic conformational correlate, cyclo(VPGVG)3. Biopolymers 28: 819-833.
    • (1989) Biopolymers , vol.28 , pp. 819-833
    • Urry, D.W.1    Chang, D.K.2    Krishna, N.R.3    Huang, D.H.4    Trapane, T.L.5    Prasad, K.U.6
  • 108
    • 0024289981 scopus 로고
    • pK shift of functional group in mechanochemical coupling due to hydrophobic effect: Evidence for an apolar-polar repulsion free energy in water
    • Urry DW, Chang DK, Zhang H and Prasad KU (1988) pK shift of functional group in mechanochemical coupling due to hydrophobic effect: evidence for an apolar-polar repulsion free energy in water. Biochem Biophys Res Commun 153: 832-839.
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 832-839
    • Urry, D.W.1    Chang, D.K.2    Zhang, H.3    Prasad, K.U.4
  • 109
    • 0023021294 scopus 로고
    • Polytetrapeptide of elastin. Temperature-correlated elastomeric force and structure development
    • Urry DW, Harris RD, Long MM and Prasad KU (1986a) Polytetrapeptide of elastin. Temperature-correlated elastomeric force and structure development. Int J Pept Protein Res 28: 649-660.
    • (1986) Int J Pept Protein Res , vol.28 , pp. 649-660
    • Urry, D.W.1    Harris, R.D.2    Long, M.M.3    Prasad, K.U.4
  • 110
    • 0022903476 scopus 로고
    • Temperature dependence of length of elastin and its polypentapeptide
    • Urry DW, Haynes B and Harris RD (1986b) Temperature dependence of length of elastin and its polypentapeptide. Biochem Biophys Res Commun 141: 749-755.
    • (1986) Biochem Biophys Res Commun , vol.141 , pp. 749-755
    • Urry, D.W.1    Haynes, B.2    Harris, R.D.3
  • 111
    • 0029443219 scopus 로고
    • Molecular biophysics of elastin structure, function and pathology
    • Urry DW, Luan CH and Peng SQ (1995) Molecular biophysics of elastin structure, function and pathology. Ciba Found Symp 192: 4-22.
    • (1995) Ciba Found Symp , vol.192 , pp. 4-22
    • Urry, D.W.1    Luan, C.H.2    Peng, S.Q.3
  • 112
    • 0016698904 scopus 로고
    • Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin
    • Urry DW, Mitchell LW, Ohnishi T and Long MM (1975) Proton and carbon magnetic resonance studies of the synthetic polypentapeptide of elastin. J Mol Biol 96: 101-117.
    • (1975) J Mol Biol , vol.96 , pp. 101-117
    • Urry, D.W.1    Mitchell, L.W.2    Ohnishi, T.3    Long, M.M.4
  • 113
    • 0031030332 scopus 로고    scopus 로고
    • Characterization of waters of hydrophobic hydration by microwave dielectric relaxation
    • Urry DW, Peng S, Xu J and McPherson DT (1997) Characterization of waters of hydrophobic hydration by microwave dielectric relaxation. J Am Chem Soc 119: 1161-1162.
    • (1997) J Am Chem Soc , vol.119 , pp. 1161-1162
    • Urry, D.W.1    Peng, S.2    Xu, J.3    McPherson, D.T.4
  • 114
    • 0026848928 scopus 로고
    • Hydrophobicity-induced pK shifts in elastin protein-based polymers
    • Urry DW, Peng SQ and Parker TM (1992) Hydrophobicity-induced pK shifts in elastin protein-based polymers. Biopolymers 32: 373-379.
    • (1992) Biopolymers , vol.32 , pp. 373-379
    • Urry, D.W.1    Peng, S.Q.2    Parker, T.M.3
  • 115
    • 0022263575 scopus 로고
    • Polypentapeptide of elastin: Temperature dependence of ellipticity and correlation with elastomeric force
    • Urry DW, Shaw RG and Prasad KU (1985a) Polypentapeptide of elastin: temperature dependence of ellipticity and correlation with elastomeric force. Biochem Biophys Res Commun 130: 50-57.
    • (1985) Biochem Biophys Res Commun , vol.130 , pp. 50-57
    • Urry, D.W.1    Shaw, R.G.2    Prasad, K.U.3
  • 116
    • 0014689359 scopus 로고
    • Coacervation of solubilized elastin effects a notable conformational change
    • Urry DW, Starcher B and Partridge SM (1969) Coacervation of solubilized elastin effects a notable conformational change. Nature 222: 795-796.
    • (1969) Nature , vol.222 , pp. 795-796
    • Urry, D.W.1    Starcher, B.2    Partridge, S.M.3
  • 117
    • 0021998703 scopus 로고
    • Carbon-13 NMR relaxation studies demonstrate an inverse temperature transition in the elastin polypentapeptide
    • Urry DW, Trapane TL, Iqbal M, Venkatachalam CM and Prasad KU (1985b) Carbon-13 NMR relaxation studies demonstrate an inverse temperature transition in the elastin polypentapeptide. Biochemistry 24: 5182-5189.
    • (1985) Biochemistry , vol.24 , pp. 5182-5189
    • Urry, D.W.1    Trapane, T.L.2    Iqbal, M.3    Venkatachalam, C.M.4    Prasad, K.U.5
  • 118
    • 0022993480 scopus 로고
    • Nitrogen-15 NMR relaxation study of inverse temperature transitions in elastin polypentapeptide and its crosslinked elastomer
    • Urry DW, Trapane TL, McMichens RB, Iqbal M, Harris RD and Prasad KU (1986c) Nitrogen-15 NMR relaxation study of inverse temperature transitions in elastin polypentapeptide and its crosslinked elastomer. Biopolymers 25: S209-S228.
    • (1986) Biopolymers , vol.25
    • Urry, D.W.1    Trapane, T.L.2    McMichens, R.B.3    Iqbal, M.4    Harris, R.D.5    Prasad, K.U.6
  • 119
    • 0000646591 scopus 로고
    • Sequential polypeptides of elastin: Cyclic conformational correlates of the linear polypentapeptide
    • Urry DW, Trapane TL, Sugano H and Prasad KU (1981) Sequential polypeptides of elastin: cyclic conformational correlates of the linear polypentapeptide. J Am Chem Soc 103: 2080-2089.
    • (1981) J Am Chem Soc , vol.103 , pp. 2080-2089
    • Urry, D.W.1    Trapane, T.L.2    Sugano, H.3    Prasad, K.U.4
  • 121
    • 0019517690 scopus 로고
    • Nuclear magnetic resonance and conformational energy calculations of repeat peptides of elastin. Conformational characterization of cyclopentadecapeptide cyclo-(L-Val-L-Pro-Gly-L-Val-Gly)3
    • Venkatachalam CM, Khaled MA, Sugano KH and Urry DW (1981) Nuclear magnetic resonance and conformational energy calculations of repeat peptides of elastin. Conformational characterization of cyclopentadecapeptide cyclo-(L-Val-L-Pro-Gly-L-Val-Gly)3. J Am Chem Soc 103: 2372-2379.
    • (1981) J Am Chem Soc , vol.103 , pp. 2372-2379
    • Venkatachalam, C.M.1    Khaled, M.A.2    Sugano, K.H.3    Urry, D.W.4
  • 122
    • 0029048088 scopus 로고
    • Conformational modeling of elastin tetrapeptide Boc-Gly-Leu-Gly-Gly-NMe by molecular dynamics simulations with improvements to the thermalization procedure
    • Villani V and Tamburro AM (1995) Conformational modeling of elastin tetrapeptide Boc-Gly-Leu-Gly-Gly-NMe by molecular dynamics simulations with improvements to the thermalization procedure. J Biomol Struct Dyn 12: 1173-1202.
    • (1995) J Biomol Struct Dyn , vol.12 , pp. 1173-1202
    • Villani, V.1    Tamburro, A.M.2
  • 123
    • 0032796605 scopus 로고    scopus 로고
    • Conformational chaos of an elastin-related peptide in aqueous solution
    • Villani V and Tamburro AM (1999) Conformational chaos of an elastin-related peptide in aqueous solution. Ann NY Acad Sci 879: 284-287.
    • (1999) Ann NY Acad Sci , vol.879 , pp. 284-287
    • Villani, V.1    Tamburro, A.M.2
  • 124
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • Vrhovski B and Weiss AS (1998) Biochemistry of tropoelastin. Eur J Biochem 258: 1-18.
    • (1998) Eur J Biochem , vol.258 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 125
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • Vrhovski B, Jensen S and Weiss AS (1997) Coacervation characteristics of recombinant human tropoelastin. Eur J Biochem 250: 92-98.
    • (1997) Eur J Biochem , vol.250 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 126
    • 0025334699 scopus 로고
    • A molecular dynamics investigation of the elastomeric restoring force in elastin
    • Wasserman ZR and Salemme FR (1990) A molecular dynamics investigation of the elastomeric restoring force in elastin. Biopolymers 29: 1613-1631.
    • (1990) Biopolymers , vol.29 , pp. 1613-1631
    • Wasserman, Z.R.1    Salemme, F.R.2
  • 127
    • 0014949231 scopus 로고
    • New molecular model for the long-range elasticity of elastin
    • Weis-Fogh T and Anderson SO (1970) New molecular model for the long-range elasticity of elastin. Nature 227: 718-721.
    • (1970) Nature , vol.227 , pp. 718-721
    • Weis-Fogh, T.1    Anderson, S.O.2
  • 128
    • 0032508370 scopus 로고    scopus 로고
    • Barstar has a highly dynamic hydrophobic core: Evidence from molecular dynamics simulations and nuclear magnetic resonance relaxation data
    • Wong KB and Daggett V (1998) Barstar has a highly dynamic hydrophobic core: evidence from molecular dynamics simulations and nuclear magnetic resonance relaxation data. Biochemistry 37: 11,182-11,192.
    • (1998) Biochemistry , vol.37 , pp. 11182-11192
    • Wong, K.B.1    Daggett, V.2
  • 130
    • 0028267099 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices
    • Zhang H, Apfelroth SD, Hu W, Davis EC, Sanguineti C, Bonadio J, Mecham RP and Ramirez F (1994) Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices. J Cell Biol 124: 855-863.
    • (1994) J Cell Biol , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, W.3    Davis, E.C.4    Sanguineti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8


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