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Volumn 120, Issue 1, 2015, Pages 419-426

Water structure and elastin-like peptide aggregation: A differential calorimetric approach

Author keywords

Clathrate; Differential scanning calorimetry; Elastin; Hydrophilic hydration; Hydrophobic hydration

Indexed keywords

CALORIMETERS; DIFFERENTIAL SCANNING CALORIMETRY; GLYCOPROTEINS; HYDRATES; HYDRATION; HYDROXYPROLINE; PEPTIDES; TEMPERATURE;

EID: 84938725054     PISSN: 13886150     EISSN: 15882926     Source Type: Journal    
DOI: 10.1007/s10973-014-4254-9     Document Type: Article
Times cited : (19)

References (55)
  • 1
    • 77950609823 scopus 로고    scopus 로고
    • Structural disorder and dynamics of elastin
    • 1:CAS:528:DC%2BC3cXjs1egs7k%3D
    • Muiznieks LD, Weiss AS, Keeley FW. Structural disorder and dynamics of elastin. Biochem Cell Biol. 2010;88:239-50.
    • (2010) Biochem Cell Biol , vol.88 , pp. 239-250
    • Muiznieks, L.D.1    Weiss, A.S.2    Keeley, F.W.3
  • 2
    • 0033006918 scopus 로고    scopus 로고
    • Elastin: Molecular description and function
    • 1:CAS:528:DyaK1MXhvFehsbY%3D
    • Debelle L, Tamburro AM. Elastin: molecular description and function. Int J Biochem Cell Biol. 1999;31:261-72.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 261-272
    • Debelle, L.1    Tamburro, A.M.2
  • 5
    • 0242499494 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Exon-by-exon chemical synthesis and related conformational studies
    • 1:CAS:528:DC%2BD3sXotlOksL0%3D
    • Tamburro AM, Bochicchio B, Pepe A. Dissection of human tropoelastin: exon-by-exon chemical synthesis and related conformational studies. Biochemistry. 2003;42:13347-62.
    • (2003) Biochemistry , vol.42 , pp. 13347-13362
    • Tamburro, A.M.1    Bochicchio, B.2    Pepe, A.3
  • 6
    • 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
    • 1:CAS:528:DyaK1cXkvVymur4%3D
    • Bisaccia F, Castiglione-Morelli MA, Spisani S, Ostuni A, Serafini-Fracassini A, Bavoso A, et al. 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. 1998;37:11128-35.
    • (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
  • 7
    • 33747084768 scopus 로고    scopus 로고
    • Localizing alpha-helices in human tropoelastin: Assembly of the elastin "puzzle"
    • 1:CAS:528:DC%2BD28XmvFWiurc%3D
    • Tamburro AM, Pepe A, Bochicchio B. Localizing alpha-helices in human tropoelastin: assembly of the elastin "puzzle". Biochemistry. 2006;45:9518-30.
    • (2006) Biochemistry , vol.45 , pp. 9518-9530
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3
  • 8
    • 3142687653 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Solution structure, dynamics and self-assembly of the exon 5 peptide
    • 1:CAS:528:DC%2BD2cXlvVKiu7g%3D
    • Bochicchio B, Floquet N, Pepe A, Alix AJP, Tamburro AM. Dissection of human tropoelastin: solution structure, dynamics and self-assembly of the exon 5 peptide. Chemistry. 2004;10:3166-76.
    • (2004) Chemistry , vol.10 , pp. 3166-3176
    • Bochicchio, B.1    Floquet, N.2    Pepe, A.3    Alix, A.J.P.4    Tamburro, A.M.5
  • 9
    • 84984621304 scopus 로고
    • Temperature of polypeptide inverse temperature depends on mean residue hydrophobicity
    • 1:CAS:528:DyaK3MXit12gtbs%3D
    • Urry DW, Luan CH, Parker TM, Gowda D, Prasad K, Reid MC, et al. Temperature of polypeptide inverse temperature depends on mean residue hydrophobicity. J Am Chem Soc. 1991;113:4346-8.
    • (1991) J Am Chem Soc , vol.113 , pp. 4346-4348
    • Urry, D.W.1    Luan, C.H.2    Parker, T.M.3    Gowda, D.4    Prasad, K.5    Reid, M.C.6
  • 10
    • 0032538330 scopus 로고    scopus 로고
    • Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: Implications for protein engineering
    • 1:CAS:528:DyaK1cXmvVOku7k%3D
    • Reiersen H, Clarke AR, Rees A. Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: implications for protein engineering. J Mol Biol. 1998;283:255-64.
    • (1998) J Mol Biol , vol.283 , pp. 255-264
    • Reiersen, H.1    Clarke, A.R.2    Rees, A.3
  • 11
    • 14644431361 scopus 로고    scopus 로고
    • Dissection of human tropoelastin: Supramolecular organization of polypeptide sequences coded by particular exons
    • 1:CAS:528:DC%2BD2MXktVOjsLk%3D
    • Pepe A, Guerra D, Bochicchio B, Quaglino D, Gheduzzi D, Pasquali Ronchetti I, et al. Dissection of human tropoelastin: supramolecular organization of polypeptide sequences coded by particular exons. Matrix Biol. 2005;24:96-109.
    • (2005) Matrix Biol , vol.24 , pp. 96-109
    • Pepe, A.1    Guerra, D.2    Bochicchio, B.3    Quaglino, D.4    Gheduzzi, D.5    Pasquali Ronchetti, I.6
  • 12
    • 34648850062 scopus 로고    scopus 로고
    • Molecular and supramolecular structural studies on human tropoelastin sequences
    • 1:CAS:528:DC%2BD2sXht12js7%2FM
    • Ostuni A, Bochicchio B, Armentano MF, Bisaccia F, Tamburro AM. Molecular and supramolecular structural studies on human tropoelastin sequences. Biophys J. 2007;93:3640-51.
    • (2007) Biophys J , vol.93 , pp. 3640-3651
    • Ostuni, A.1    Bochicchio, B.2    Armentano, M.F.3    Bisaccia, F.4    Tamburro, A.M.5
  • 13
    • 36649020438 scopus 로고    scopus 로고
    • Investigating the amyloidogenic nanostructured sequences of elastin: Sequence encoded by exon 28 of human tropoelastin gene
    • 1:CAS:528:DC%2BD2sXhtFGisr3F
    • Bochicchio B, Pepe A, Flamia R, Lorusso M, Tamburro AM. Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene. Biomacromolecules. 2007;8:3478-86.
    • (2007) Biomacromolecules , vol.8 , pp. 3478-3486
    • Bochicchio, B.1    Pepe, A.2    Flamia, R.3    Lorusso, M.4    Tamburro, A.M.5
  • 15
    • 0026143166 scopus 로고
    • Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin-based
    • 1:CAS:528:DyaK3MXks1OjsLs%3D
    • Luan CH, Parker TM, Prasad KU, Urry DW. Differential scanning calorimetry studies of NaCl effect on the inverse temperature transition of some elastin-based. Biopolymers. 1991;31:465-75.
    • (1991) Biopolymers , vol.31 , pp. 465-475
    • Luan, C.H.1    Parker, T.M.2    Prasad, K.U.3    Urry, D.W.4
  • 16
    • 0026924813 scopus 로고
    • Hydrophobicity of amino acid residues: Differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin
    • 1:CAS:528:DyaK38XmsFWkt78%3D
    • Luan CH, Parker TM, Gowda DC, Urry DW. Hydrophobicity of amino acid residues: differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin. Biopolymers. 1992;32:1251-61.
    • (1992) Biopolymers , vol.32 , pp. 1251-1261
    • Luan, C.H.1    Parker, T.M.2    Gowda, D.C.3    Urry, D.W.4
  • 18
    • 68949129479 scopus 로고    scopus 로고
    • Influence of the amino-acid sequence on the inverse temperature transition of elastin-like polymers
    • 1:CAS:528:DC%2BD1MXpsFOmurw%3D
    • Ribeiro A, Arias FJ, Reguera J, Alonso M, Rodríguez-Cabello JC. Influence of the amino-acid sequence on the inverse temperature transition of elastin-like polymers. Biophys J. 2009;97:312-20.
    • (2009) Biophys J , vol.97 , pp. 312-320
    • Ribeiro, A.1    Arias, F.J.2    Reguera, J.3    Alonso, M.4    Rodríguez-Cabello, J.C.5
  • 19
    • 78650061689 scopus 로고    scopus 로고
    • Proline periodicity modulates the self-assembly properties of elastin-like polypeptides
    • 1:CAS:528:DC%2BC3cXhsFCht7fL
    • Muiznieks LD, Keeley FW. Proline periodicity modulates the self-assembly properties of elastin-like polypeptides. J Biol Chem. 2010;285:39779-89.
    • (2010) J Biol Chem , vol.285 , pp. 39779-39789
    • Muiznieks, L.D.1    Keeley, F.W.2
  • 20
    • 84876743882 scopus 로고    scopus 로고
    • Effect of proline analogues on the conformation of elastin peptides
    • 1:CAS:528:DC%2BC3sXmtlWgt7g%3D
    • Pepe A, Crudele MA, Bochicchio B. Effect of proline analogues on the conformation of elastin peptides. New J Chem. 2013;37:1326.
    • (2013) New J Chem , vol.37 , pp. 1326
    • Pepe, A.1    Crudele, M.A.2    Bochicchio, B.3
  • 21
    • 80055006040 scopus 로고    scopus 로고
    • Structural requirements essential for elastin coacervation: Favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n
    • 1:CAS:528:DC%2BC3MXhtFGltbfI
    • Maeda I, Fukumoto Y, Nose T, Shimohigashi Y, Nezu T, Terada Y, et al. Structural requirements essential for elastin coacervation: favorable spatial arrangements of valine ridges on the three-dimensional structure of elastin-derived polypeptide (VPGVG)n. J Pept Sci. 2011;17:735-43.
    • (2011) J Pept Sci , vol.17 , pp. 735-743
    • Maeda, I.1    Fukumoto, Y.2    Nose, T.3    Shimohigashi, Y.4    Nezu, T.5    Terada, Y.6
  • 22
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • 1:CAS:528:DyaK2sXnslGgtrY%3D
    • Vrhovski B, Jensen S, Weiss AS. Coacervation characteristics of recombinant human tropoelastin. Eur J Biochem. 1997;250:92-8.
    • (1997) Eur J Biochem , vol.250 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 23
    • 33847253510 scopus 로고    scopus 로고
    • Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer
    • 1:CAS:528:DC%2BD2sXmt1ymtQ%3D%3D
    • Reguera J, Urry DW, Parker TM, McPherson DT, Rodríguez-Cabello JC. Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer. Biomacromolecules. 2007;8:354-8.
    • (2007) Biomacromolecules , vol.8 , pp. 354-358
    • Reguera, J.1    Urry, D.W.2    Parker, T.M.3    McPherson, D.T.4    Rodríguez-Cabello, J.C.5
  • 24
    • 84890333312 scopus 로고    scopus 로고
    • Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides
    • 1:CAS:528:DC%2BC3sXhs1WltLnM
    • Bochicchio B, Laurita A, Heinz A, Schmelzer CEH, Pepe A. Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides. Biomacromolecules. 2013;14:4278-88.
    • (2013) Biomacromolecules , vol.14 , pp. 4278-4288
    • Bochicchio, B.1    Laurita, A.2    Heinz, A.3    Schmelzer, C.E.H.4    Pepe, A.5
  • 25
    • 1542281813 scopus 로고    scopus 로고
    • Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin
    • 1:CAS:528:DC%2BD3sXptlGktrk%3D
    • Miao M, Bellingham CM, Stahl RJ, Sitarz EE, Lane CJ, Keeley FW. Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin. J Biol Chem. 2003;278:48553-62.
    • (2003) J Biol Chem , vol.278 , pp. 48553-48562
    • Miao, M.1    Bellingham, C.M.2    Stahl, R.J.3    Sitarz, E.E.4    Lane, C.J.5    Keeley, F.W.6
  • 26
    • 33846250450 scopus 로고    scopus 로고
    • Proline and glycine control protein self-organization into elastomeric or amyloid fibrils
    • 1:CAS:528:DC%2BD28Xht1SmtrzJ
    • Rauscher S, Baud S, Miao M, Keeley FW, Pomès R. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Structure. 2006;14:1667-76.
    • (2006) Structure , vol.14 , pp. 1667-1676
    • Rauscher, S.1    Baud, S.2    Miao, M.3    Keeley, F.W.4    Pomès, R.5
  • 27
    • 57849137449 scopus 로고    scopus 로고
    • Formation of nanostructures by self-assembly of an elastin peptide
    • 1:CAS:528:DC%2BD1cXhsFWisL%2FK
    • Pepe A, Armenante MR, Bochicchio B, Tamburro AM. Formation of nanostructures by self-assembly of an elastin peptide. Soft Matter. 2009;5:104.
    • (2009) Soft Matter , vol.5 , pp. 104
    • Pepe, A.1    Armenante, M.R.2    Bochicchio, B.3    Tamburro, A.M.4
  • 28
    • 79960922167 scopus 로고    scopus 로고
    • Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water
    • 1:CAS:528:DC%2BC3MXpt1Gis7o%3D
    • Salvi AM, Moscarelli P, Satriano G, Bochicchio B, Castle JE, Lucano A, et al. Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water. Biopolymers. 2011;95:702-21.
    • (2011) Biopolymers , vol.95 , pp. 702-721
    • Salvi, A.M.1    Moscarelli, P.2    Satriano, G.3    Bochicchio, B.4    Castle, J.E.5    Lucano, A.6
  • 29
    • 84874340656 scopus 로고    scopus 로고
    • Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides
    • 1:CAS:528:DC%2BC3sXislymsL0%3D
    • Salvi AM, Moscarelli P, Bochicchio B, Lanza G, Castle JE. Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides. Biopolymers. 2013;99:292-313.
    • (2013) Biopolymers , vol.99 , pp. 292-313
    • Salvi, A.M.1    Moscarelli, P.2    Bochicchio, B.3    Lanza, G.4    Castle, J.E.5
  • 30
  • 31
    • 84867501544 scopus 로고    scopus 로고
    • An assessment of various powdered baby formulas by conventional methods (DSC) or FT-IR spectroscopy
    • Ostrowska-Lige¸za E, Górska A, Wirkowska M, Koczoń P. An assessment of various powdered baby formulas by conventional methods (DSC) or FT-IR spectroscopy. J Therm Anal Calorim. 2012;110:465-71.
    • (2012) J Therm Anal Calorim , vol.110 , pp. 465-471
    • Ostrowska-Lige¸za, E.1    Górska, A.2    Wirkowska, M.3    Koczoń, P.4
  • 32
    • 78049454816 scopus 로고    scopus 로고
    • Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry
    • 1:CAS:528:DC%2BC3cXhtFartLvE
    • Briere L-AK, Brandt J-M, Medley JB. Measurement of protein denaturation in human synovial fluid and its analogs using differential scanning calorimetry. J Therm Anal Calorim. 2010;102:99-106.
    • (2010) J Therm Anal Calorim , vol.102 , pp. 99-106
    • Briere, L.-A.K.1    Brandt, J.-M.2    Medley, J.B.3
  • 33
    • 84900613295 scopus 로고    scopus 로고
    • Detection and characterization of hemoglobin dissociation and aggregation using microcalorimetry
    • Suh Y, Kim BJ, Tam KC, Aucoin MG. Detection and characterization of hemoglobin dissociation and aggregation using microcalorimetry. J Therm Anal Calorim. 2013;115:2159-69.
    • (2013) J Therm Anal Calorim , vol.115 , pp. 2159-2169
    • Suh, Y.1    Kim, B.J.2    Tam, K.C.3    Aucoin, M.G.4
  • 35
    • 2542577768 scopus 로고    scopus 로고
    • Effect of water on the molecular mobility of elastin
    • Available from
    • Samouillan V, André C, Dandurand J, Lacabanne C. Effect of water on the molecular mobility of elastin. Biomacromolecules [Internet]. 2004;5:958-64. Available from: http://www.ncbi.nlm.nih.gov/pubmed/15132687.
    • (2004) Biomacromolecules [Internet] , vol.5 , pp. 958-964
    • Samouillan, V.1    André, C.2    Dandurand, J.3    Lacabanne, C.4
  • 36
    • 79959277520 scopus 로고    scopus 로고
    • Hydrated elastin: Dynamics of water and protein followed by dielectric spectroscopies
    • 1:CAS:528:DC%2BC3MXntlSgtr8%3D
    • Samouillan V, Tintar D, Lacabanne C. Hydrated elastin: dynamics of water and protein followed by dielectric spectroscopies. Chem Phys. 2011;385:19-26.
    • (2011) Chem Phys , vol.385 , pp. 19-26
    • Samouillan, V.1    Tintar, D.2    Lacabanne, C.3
  • 37
    • 84856971880 scopus 로고    scopus 로고
    • Analysis of the molecular mobility of collagen and elastin in safe, atheromatous and aneurysmal aortas
    • 1:CAS:528:DC%2BC38XitlGhtr8%3D
    • Samouillan V, Dandurand J, Lacabanne C, Stella A, Gargiulo M, Degani A, et al. Analysis of the molecular mobility of collagen and elastin in safe, atheromatous and aneurysmal aortas. Pathol Biol (Paris). 2012;60:58-65.
    • (2012) Pathol Biol (Paris) , vol.60 , pp. 58-65
    • Samouillan, V.1    Dandurand, J.2    Lacabanne, C.3    Stella, A.4    Gargiulo, M.5    Degani, A.6
  • 38
    • 0026557332 scopus 로고
    • Phase transitions and chain dynamics, in the solid state, of a pentapeptide sequence of elastins
    • 1:CAS:528:DyaK38XitlSgt7w%3D
    • Megret C, Guantieri V, Lamure A, Pieraggi MT, Lacabanne C, Tamburro AM. Phase transitions and chain dynamics, in the solid state, of a pentapeptide sequence of elastins. Int J Biol Macromol. 1992;14:45-9.
    • (1992) Int J Biol Macromol , vol.14 , pp. 45-49
    • Megret, C.1    Guantieri, V.2    Lamure, A.3    Pieraggi, M.T.4    Lacabanne, C.5    Tamburro, A.M.6
  • 39
    • 0000630673 scopus 로고    scopus 로고
    • Structural investigation of the poly(pentapeptide) of elastin, poly(GVGVP), in the solid state
    • 1:CAS:528:DyaK1MXltVGjt7g%3D
    • Rodriguez-cabello JC, Alonso M, Diez MI, Caballero MI, Herguedas MM. Structural investigation of the poly(pentapeptide) of elastin, poly(GVGVP), in the solid state. Macromol Chem Phys. 1999;200:1831-8.
    • (1999) Macromol Chem Phys , vol.200 , pp. 1831-1838
    • Rodriguez-Cabello, J.C.1    Alonso, M.2    Diez, M.I.3    Caballero, M.I.4    Herguedas, M.M.5
  • 40
    • 84898425401 scopus 로고    scopus 로고
    • Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers
    • Dandurand J, Samouillan V, Lacoste-Ferre MH, Lacabanne C, Bochicchio B, Pepe A. Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: signature of the amyloid fibers. Pathol Biol (Paris). 2014;60:100-7.
    • (2014) Pathol Biol (Paris) , vol.60 , pp. 100-107
    • Dandurand, J.1    Samouillan, V.2    Lacoste-Ferre, M.H.3    Lacabanne, C.4    Bochicchio, B.5    Pepe, A.6
  • 41
    • 0034610101 scopus 로고    scopus 로고
    • Differential scanning calorimetry study of the hydrophobic hydration of the elastin-based polypentapeptide poly(VPGVG), from deficiency to excess of water
    • Rodriguez-Cabello JC, Alonso M, Perez T, Mar Herguedas M. Differential scanning calorimetry study of the hydrophobic hydration of the elastin-based polypentapeptide poly(VPGVG), from deficiency to excess of water. Biopolymers. 2000;54:282-8.
    • (2000) Biopolymers , vol.54 , pp. 282-288
    • Rodriguez-Cabello, J.C.1    Alonso, M.2    Perez, T.3    Mar Herguedas, M.4
  • 42
    • 70350191419 scopus 로고    scopus 로고
    • Human tropoelastin sequence: Dynamics of polypeptide coded by exon 6 in solution
    • 1:CAS:528:DC%2BD1MXhtVKiurbL
    • Tintar D, Samouillan V, Dandurand J, Lacabanne C, Pepe a, Bochicchio B, et al. Human tropoelastin sequence: dynamics of polypeptide coded by exon 6 in solution. Biopolymers. 2009;91:943-52.
    • (2009) Biopolymers , vol.91 , pp. 943-952
    • Tintar, D.1    Samouillan, V.2    Dandurand, J.3    Lacabanne, C.4    Pepe, A.5    Bochicchio, B.6
  • 43
    • 34948847082 scopus 로고    scopus 로고
    • DSC approach for the investigation of mobile water fractions in aqueous solutions of NaCl and Tris buffer
    • [cited 2014 Jan 17]
    • Kamasa P, Bokor M, Pyda M, Tompa K. DSC approach for the investigation of mobile water fractions in aqueous solutions of NaCl and Tris buffer. Thermochim Acta [Internet]. 2007 [cited 2014 Jan 17];464:29-34.
    • (2007) Thermochim Acta [Internet] , vol.464 , pp. 29-34
    • Kamasa, P.1    Bokor, M.2    Pyda, M.3    Tompa, K.4
  • 44
    • 65649133556 scopus 로고    scopus 로고
    • Thermal response with exothermic effects of beta2-microglobulin amyloid fibrils and fibrillation
    • 1:CAS:528:DC%2BD1MXms1aitbo%3D
    • Sasahara K, Yagi H, Naiki H, Goto Y. Thermal response with exothermic effects of beta2-microglobulin amyloid fibrils and fibrillation. J Mol Biol. 2009;389:584-94.
    • (2009) J Mol Biol , vol.389 , pp. 584-594
    • Sasahara, K.1    Yagi, H.2    Naiki, H.3    Goto, Y.4
  • 46
    • 79961029655 scopus 로고    scopus 로고
    • Low temperature exothermic effects on cooling of homoionic clays
    • Kozlowski T. Low temperature exothermic effects on cooling of homoionic clays. Cold Reg Sci Technol. 2011;68:139-49.
    • (2011) Cold Reg Sci Technol , vol.68 , pp. 139-149
    • Kozlowski, T.1
  • 48
    • 0003058648 scopus 로고    scopus 로고
    • Interaction between water and hydrophilic polymers
    • 1:CAS:528:DyaK1cXksVKqtw%3D%3D
    • Hatakeyama H, Hatakeyama T. Interaction between water and hydrophilic polymers. Thermochim Acta. 1998;308:3-22.
    • (1998) Thermochim Acta , vol.308 , pp. 3-22
    • Hatakeyama, H.1    Hatakeyama, T.2
  • 49
    • 0019610634 scopus 로고
    • Studies on bound water of cellulose by differential scanning calorimetry
    • 1:CAS:528:DyaL3MXltlChsbs%3D
    • Nakamura K, Hatakeyama T, Hatakeyama H. Studies on bound water of cellulose by differential scanning calorimetry. Text Res J. 1981;51:607-13.
    • (1981) Text Res J , vol.51 , pp. 607-613
    • Nakamura, K.1    Hatakeyama, T.2    Hatakeyama, H.3
  • 50
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • 1:CAS:528:DC%2BD38Xos1aju70%3D
    • Bochicchio B, Tamburro AM. Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality. 2002;14:782-92.
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 51
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • 1:CAS:528:DC%2BD2cXmsVCrtb4%3D
    • DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J Mol Biol. 2004;341:1317-26.
    • (2004) J Mol Biol , vol.341 , pp. 1317-1326
    • Dubay, K.F.1    Pawar, A.P.2    Chiti, F.3    Zurdo, J.4    Dobson, C.M.5    Vendruscolo, M.6
  • 52
    • 4344602172 scopus 로고    scopus 로고
    • Protein hydration dynamics in solution: A critical survey
    • 1:CAS:528:DC%2BD2cXnvFWhsbc%3D discussion 1223-4, 1323-8
    • Halle B. Protein hydration dynamics in solution: a critical survey. Philos Trans R Soc Lond B Biol Sci. 2004;359:1207-23 discussion 1223-4, 1323-8.
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 1207-1223
    • Halle, B.1
  • 54
    • 33751546902 scopus 로고    scopus 로고
    • Study of CCl3F hydrate formation and dissociation in W/O emulsion by differential scanning calorimetry and X-ray diffraction
    • 1:CAS:528:DC%2BD28Xht1Kiu77M
    • Fouconnier B, Komunjer L, Ollivon M, Lesieur P, Keller G, Clausse D. Study of CCl3F hydrate formation and dissociation in W/O emulsion by differential scanning calorimetry and X-ray diffraction. Fluid Phase Equilib. 2006;250:76-82.
    • (2006) Fluid Phase Equilib , vol.250 , pp. 76-82
    • Fouconnier, B.1    Komunjer, L.2    Ollivon, M.3    Lesieur, P.4    Keller, G.5    Clausse, D.6
  • 55
    • 77954730534 scopus 로고    scopus 로고
    • Kinetics and morphology of self-assembly of an elastin-like polypeptide based on the alternating domain arrangement of human tropoelastin
    • 1:CAS:528:DC%2BC3cXns1Cnsro%3D
    • Cirulis JT, Keeley FW. Kinetics and morphology of self-assembly of an elastin-like polypeptide based on the alternating domain arrangement of human tropoelastin. Biochemistry. 2010;49:5726-33.
    • (2010) Biochemistry , vol.49 , pp. 5726-5733
    • Cirulis, J.T.1    Keeley, F.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.