메뉴 건너뛰기




Volumn 31, Issue 10, 2015, Pages 2946-2955

Thermally Induced Conformational Transitions in Nascent Branched Amphiphilic Peptide Capsules

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCOMPATIBILITY; ENCAPSULATION; PROTEINS;

EID: 84925002849     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la504381y     Document Type: Article
Times cited : (16)

References (27)
  • 3
    • 0029778868 scopus 로고    scopus 로고
    • CLEAR: A novel family of highly cross-linked polymeric supports for solid phase synthesis
    • Kempe, M.; Barany, G. CLEAR: A novel family of highly cross-linked polymeric supports for solid phase synthesis J. Am. Chem. Soc. 1996, 118, 7083-7093
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7083-7093
    • Kempe, M.1    Barany, G.2
  • 4
    • 0028285338 scopus 로고
    • Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels
    • Iwamoto, T.; Grove, A.; Montal, M. O.; Montal, M.; Tomich, J. M. Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels Int. J. Pept. Protein Res. 1994, 43, 597-607
    • (1994) Int. J. Pept. Protein Res. , vol.43 , pp. 597-607
    • Iwamoto, T.1    Grove, A.2    Montal, M.O.3    Montal, M.4    Tomich, J.M.5
  • 5
    • 49849116621 scopus 로고
    • Stoichiometry of the reaction between methyl mercury (II) iodide and soluble sulphides
    • Gruen, L. C. Stoichiometry of the reaction between methyl mercury (II) iodide and soluble sulphides Anal. Chim. Acta 1970, 50, 299-303
    • (1970) Anal. Chim. Acta , vol.50 , pp. 299-303
    • Gruen, L.C.1
  • 6
    • 84888579995 scopus 로고
    • Determination of -SS and -SH groups in proteins. I. A reassessment of the use of methylmercuric iodide
    • Forbes, W. F.; Hamlin, C. R. Determination of -SS and -SH groups in proteins. I. A reassessment of the use of methylmercuric iodide Can. J. Chem. 1968, 46, 3033-3040
    • (1968) Can. J. Chem. , vol.46 , pp. 3033-3040
    • Forbes, W.F.1    Hamlin, C.R.2
  • 7
    • 0016537404 scopus 로고
    • A new method for the disulfide analysis of peptides
    • Anderson, W. L.; Wetlaufer, D. B. A new method for the disulfide analysis of peptides Anal. Biochem. 1975, 67, 493-502
    • (1975) Anal. Biochem. , vol.67 , pp. 493-502
    • Anderson, W.L.1    Wetlaufer, D.B.2
  • 8
    • 0000412948 scopus 로고
    • Measurements of absolute values in biochemical fluorescence spectroscopy
    • Chen, R. F. Measurements of absolute values in biochemical fluorescence spectroscopy J. Res. Natl. Bur. Stand. 1972, 76A (6) 593-606
    • (1972) J. Res. Natl. Bur. Stand. , vol.76 A , Issue.6 , pp. 593-606
    • Chen, R.F.1
  • 9
    • 36849121988 scopus 로고
    • Remarks on the absorption spectra of phenylalanine and tyrosine in connection with the absorption in toluene and paracresol
    • Sponer, H. Remarks on the absorption spectra of phenylalanine and tyrosine in connection with the absorption in toluene and paracresol J. Chem. Phys. 1942, 10, 672
    • (1942) J. Chem. Phys. , vol.10 , pp. 672
    • Sponer, H.1
  • 10
    • 34447629532 scopus 로고    scopus 로고
    • Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis
    • Kuipers, B. J.; Gruppen, H. Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis J. Agric. Food Chem. 2007, 55, 5445-5451
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5445-5451
    • Kuipers, B.J.1    Gruppen, H.2
  • 11
    • 0023419545 scopus 로고
    • A glow discharge unit to render electron microscope grids and other surfaces hydrophilic
    • Aebi, U.; Pollard, T. D. A glow discharge unit to render electron microscope grids and other surfaces hydrophilic J. Electron Microsc. Technol. 1987, 7, 29-33
    • (1987) J. Electron Microsc. Technol. , vol.7 , pp. 29-33
    • Aebi, U.1    Pollard, T.D.2
  • 12
    • 0037443028 scopus 로고    scopus 로고
    • Application of high-angle annular dark field scanning transmission electron microscopy, scanning transmission electron microscopy-energy dispersive X-ray spectrometry, and energy-filtered transmission electron microscopy to the characterization of nanoparticles in the environment
    • Utsunomiya, S.; Ewing, R. C. Application of high-angle annular dark field scanning transmission electron microscopy, scanning transmission electron microscopy-energy dispersive X-ray spectrometry, and energy-filtered transmission electron microscopy to the characterization of nanoparticles in the environment Environ. Sci. Technol. 2003, 37, 786-791
    • (2003) Environ. Sci. Technol. , vol.37 , pp. 786-791
    • Utsunomiya, S.1    Ewing, R.C.2
  • 13
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky, A.; Golay, M. J. E. Smoothing and differentiation of data by simplified least squares procedures Anal. Chem. 1964, 36, 1627-1639
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 14
    • 33746608515 scopus 로고    scopus 로고
    • Model systems for β-hairpins and β-sheets
    • Hughes, R. M.; Waters, M. L. Model systems for β-hairpins and β-sheets Curr. Opin. Struct. Biol. 2006, 16, 514-524
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 514-524
    • Hughes, R.M.1    Waters, M.L.2
  • 15
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide i infrared spectra
    • Dong, A.; Hoang, P.; Caughey, W. S. Protein secondary structures in water from second-derivative amide I infrared spectra Biochemistry 1990, 29, 3303-3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Hoang, P.2    Caughey, W.S.3
  • 16
    • 65549139776 scopus 로고    scopus 로고
    • Flexible structures and ligand interactions of tandem repeats consisting of proline, glycine, asparagine, serine, and/or threonine rich oligopeptides in proteins
    • Matsushima, N.; Yoshida, H.; Kumaki, Y.; Kamiya, M.; Tanaka, T.; Izumi, Y.; Kretsinger, R. H. Flexible structures and ligand interactions of tandem repeats consisting of proline, glycine, asparagine, serine, and/or threonine rich oligopeptides in proteins Curr. Protein Pept. Sci. 2008, 9, 591-610
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 591-610
    • Matsushima, N.1    Yoshida, H.2    Kumaki, Y.3    Kamiya, M.4    Tanaka, T.5    Izumi, Y.6    Kretsinger, R.H.7
  • 17
  • 19
    • 0017709445 scopus 로고
    • Beta-turns in proteins
    • Chou, P. Y.; Fasman, G. D. Beta-turns in proteins J. Mol. Biol. 1977, 115, 135-175
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 20
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of beta-turn in proteins
    • Wilmot, C. M.; Thornton, J. M. Analysis and prediction of the different types of beta-turn in proteins J. Mol. Biol. 1988, 203, 221-232
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 21
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • Whitesides, G. M.; Mathias, J. P.; Seto, C. T. Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures Science 1991, 254, 1312-1319
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 23
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan, N.; Vishveshwara, S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins Protein Eng. 2000, 13, 753-761
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 24
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles
    • Serrano, L.; Bycroft, M.; Fersht, A. R. Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles J. Mol. Biol. 1991, 218, 465-475
    • (1991) J. Mol. Biol. , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 26
    • 10044225776 scopus 로고    scopus 로고
    • Effects of particle size and surface coating on cellular uptake of polymeric nanoparticles for oral delivery of anticancer drugs
    • Win, K. Y.; Feng, S. S. Effects of particle size and surface coating on cellular uptake of polymeric nanoparticles for oral delivery of anticancer drugs Biomaterials 2005, 26, 2713-2722
    • (2005) Biomaterials , vol.26 , pp. 2713-2722
    • Win, K.Y.1    Feng, S.S.2
  • 27
    • 84883887168 scopus 로고    scopus 로고
    • Effects of particle size and surface modification on cellular uptake and biodistribution of polymeric nanoparticles for drug delivery
    • Kulkarni, S. A.; Feng, S. S. Effects of particle size and surface modification on cellular uptake and biodistribution of polymeric nanoparticles for drug delivery Pharm. Res. 2013, 30, 2512-2522
    • (2013) Pharm. Res. , vol.30 , pp. 2512-2522
    • Kulkarni, S.A.1    Feng, S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.