메뉴 건너뛰기




Volumn 401, Issue 4, 2010, Pages 544-547

Rationalization of poor solubility of TGF-β3 using MD simulation

Author keywords

Hydrophobic patch; Intermediate; Molecular dynamic simulation; Solubility; Transforming growth factor

Indexed keywords

SOLVENT; TRANSFORMING GROWTH FACTOR BETA1; TRANSFORMING GROWTH FACTOR BETA3; UREA;

EID: 77958494726     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.09.090     Document Type: Article
Times cited : (8)

References (16)
  • 1
    • 0033583203 scopus 로고    scopus 로고
    • Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions
    • Pellaud J., Schote U., Arvinte T., Seelig J. Conformation and self-association of human recombinant transforming growth factor-beta3 in aqueous solutions. J. Biol. Chem. 1999, 274:7699-7704.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7699-7704
    • Pellaud, J.1    Schote, U.2    Arvinte, T.3    Seelig, J.4
  • 2
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding
    • Mittl P.R., Priestle J.P., Cox D.A., McMaster G., Cerletti N., Grutter M.G. The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. Protein Sci. 1996, 5:1261-1271.
    • (1996) Protein Sci. , vol.5 , pp. 1261-1271
    • Mittl, P.R.1    Priestle, J.P.2    Cox, D.A.3    McMaster, G.4    Cerletti, N.5    Grutter, M.G.6
  • 3
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 4
    • 0036787760 scopus 로고    scopus 로고
    • Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins
    • Georgescu R.E., Alexov E.G., Gunner M.R. Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins. Biophys. J. 2002, 83:1731-1748.
    • (2002) Biophys. J. , vol.83 , pp. 1731-1748
    • Georgescu, R.E.1    Alexov, E.G.2    Gunner, M.R.3
  • 5
    • 0029633168 scopus 로고
    • Gromacs - a message-passing parallel molecular-dynamics implementation
    • Berendsen H.J.C., Vanderspoel D., Vandrunen R. Gromacs - a message-passing parallel molecular-dynamics implementation. Comput. Phys. Commun. 1995, 91:43-56.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Vanderspoel, D.2    Vandrunen, R.3
  • 6
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 2001, 7:306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 10
    • 33846823909 scopus 로고
    • Particle mesh Ewald - an N·Log(N) method for Ewald sums in large systems
    • Darden T., York D., Pedersen L. Particle mesh Ewald - an N·Log(N) method for Ewald sums in large systems. J. Chem. Phys. 1993, 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 12
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard S.J., Thornton J.M. 'NACCESS' Computer Program 1993, Department of Biochemistry and Molecular Biology, University College, London.
    • (1993) 'NACCESS' Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 13
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991, 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 14
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 15
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.