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Volumn 6, Issue , 2009, Pages 133-145

Exploiting the sequence of naturally occurring elastin: Construction, production and characterization of a recombinant thermoplastic proteinbased polymer

Author keywords

Elastin like polymers; Nanoparticles; Thermoplastic; Thermoresponsive polymer; VPAVG

Indexed keywords

AMINO ACID COMPOSITIONS; BACTERIA CELL; CARBON SOURCE; CENTRAL COMPOSITE DESIGNS; CULTURE MEDIA; ELASTIN-LIKE POLYMERS; HYSTERESIS BEHAVIOUR; INVERSE TEMPERATURE TRANSITIONS; LOW COSTS; MICRO-PARTICLES; MOLECULAR WEIGHT POLYMERS; NATURALLY OCCURRING; PRECISE CONTROL; PROTEIN-BASED POLYMERS; SALT CONCENTRATION; SELF-ASSEMBLING; THERMORESPONSIVE POLYMER;

EID: 74949091067     PISSN: 16625250     EISSN: 16619897     Source Type: Journal    
DOI: 10.4028/www.scientific.net/JNanoR.6.133     Document Type: Article
Times cited : (20)

References (25)
  • 4
    • 0037135070 scopus 로고    scopus 로고
    • Stretching the limits
    • DOI 10.1126/science.297.5580.329
    • J. Alper, Science. 297 (2002) 329-331. doi:10.1126/science.297.5580.329 (Pubitemid 34790739)
    • (2002) Science , vol.297 , Issue.5580 , pp. 329-331
    • Alper, J.1
  • 8
    • 26644451842 scopus 로고    scopus 로고
    • Developing functionality in elastin-like polymers by increasing their molecular complexity: The power of the genetic engineering approach
    • DOI 10.1016/j.progpolymsci.2005.07.004, PII S0079670005000948
    • J.C. Rodríguez-Cabello, J. Reguera, A. Girotti, M. Alonso, A.M. Testera, Progress in Polymer Science. 30 (2005) 1119-1145. doi:10.1016/j. progpolymsci.2005.07.004 (Pubitemid 41443491)
    • (2005) Progress in Polymer Science (Oxford) , vol.30 , Issue.11 , pp. 1119-1145
    • Rodriguez-Cabello, J.C.1    Reguera, J.2    Girotti, A.3    Alonso, M.4    Testera, A.M.5
  • 10
    • 0025675856 scopus 로고
    • doi:10.1016/0378-1119(90)90336-P
    • H. Inoue, H. Nojima, H. Okayama, Gene. 96 (1990) 23-28. doi:10.1016/0378-1119(90)90336-P
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 12
    • 2942557320 scopus 로고    scopus 로고
    • Cheese whey-induced high-cell-density production of recombinant proteins in Escherichia coli
    • DOI 10.1186/1475-2859-2-2
    • M.I. Viitanen, A. Vasala, P. Neubauer, T. Alatossava, Microbial Cell Factories. 2 (2003) 1-10. doi:10.1186/1475-2859-2-2 (Pubitemid 38751439)
    • (2003) Microbial Cell Factories , vol.2 , pp. 2
    • Viitanen, M.I.1    Vasala, A.2    Neubauer, P.3    Alatossava, T.4
  • 14
    • 28944455509 scopus 로고    scopus 로고
    • Response surface optimization of the medium components for the production of biosurfactants by probiotic bacteria
    • DOI 10.1016/j.procbio.2005.01.030, PII S135951130500276X
    • L. Rodrigues, J. Teixeira, R. Oliveira, H.C. van der Mei, Process Biochemistry. 41 (2006) 1-10. doi:10.1016/j.procbio.2005.01.030 (Pubitemid 41785576)
    • (2006) Process Biochemistry , vol.41 , Issue.1 , pp. 1-10
    • Rodrigues, L.1    Teixeira, J.2    Oliveira, R.3    Van Der Mei, H.C.4
  • 18
    • 16344392698 scopus 로고    scopus 로고
    • Role of water in structural changes of poly(AVGVP) and poly(GVGVP) studied by FTIR and Raman spectroscopy and ab initio calculations
    • DOI 10.1021/bm049461t
    • P. Schmidt, J. Dybal, J.C. Rodríguez-Cabello, V. Reboto, Biomacromolecules. 6 (2005) 697-706. doi:10.1021/bm049461t (Pubitemid 40467812)
    • (2005) Biomacromolecules , vol.6 , Issue.2 , pp. 697-706
    • Schmidt, P.1    Dybal, J.2    Rodriguez-Cabello, J.C.3    Reboto, V.4
  • 20
    • 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
    • DOI 10.1021/bm060936l
    • J. Reguera, D.W. Urry, T.M. Parker, D.T. McPherson, J.C. Rodríguez-Cabello, Biomacromolecules. 8 (2007) 354-358. doi:10.1021/bm060936l (Pubitemid 46323247)
    • (2007) Biomacromolecules , vol.8 , Issue.2 , pp. 354-358
    • Reguera, J.1    Urry, D.W.2    Parker, T.M.3    McPherson, D.T.4    Rodriguez-Cabello, J.C.5
  • 21
    • 0032080534 scopus 로고    scopus 로고
    • Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect
    • DOI 10.1002/(SICI)1097-0134(19980501)31:2<107::AID-PROT1>3.0.CO;2-J
    • Q. Zou, S.M. Habermann-Rottinghaus, K.P. Murphy, PROTEINS. 31 (1998) 107-115. doi:10.1002/(SICI)1097-0134(19980501)31:2<107::AID-PROT1>3.0. CO;2-J (Pubitemid 28198703)
    • (1998) Proteins: Structure, Function and Genetics , vol.31 , Issue.2 , pp. 107-115
    • Zou, Q.1    Habermann-Rottinghaus, S.M.2    Murphy, K.P.3
  • 25
    • 9344234999 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion
    • DOI 10.1110/ps.04931604
    • K. Trabbic-Carlson, L. Liu, B. Kim, A. Chilkoti, Protein Science. 13 (2004) 3274-3284. doi:10.1110/ps.04931604 (Pubitemid 39557797)
    • (2004) Protein Science , vol.13 , Issue.12 , pp. 3274-3284
    • Trabbic-Carlson, K.1    Liu, L.2    Kim, B.3    Chilkoti, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.