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Volumn 9, Issue 11, 2008, Pages 3024-3032

Molecular dynamics simulation of the cooperative adsorption of barley lipid transfer protein and cis-isocohumulone at the vacuum-water interface

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; ADSORPTION; BEVERAGES; BINDING ENERGY; DYNAMICS; MOLECULAR DYNAMICS; MOLECULES; PHASE INTERFACES; PHASE STABILITY; QUANTUM CHEMISTRY; SYSTEM STABILITY; VACUUM; VACUUM TECHNOLOGY;

EID: 57049132826     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm8004325     Document Type: Article
Times cited : (29)

References (26)
  • 1
    • 0035146503 scopus 로고    scopus 로고
    • Milk protein interfacial layers and the relationship to emulsion stability and rheology
    • Dickinson, E. Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloid Surf., B 2001, 20, 197-210.
    • (2001) Colloid Surf., B , vol.20 , pp. 197-210
    • Dickinson, E.1
  • 2
    • 0001398234 scopus 로고
    • Stability of emulsions containing both protein and polysaccharide
    • Dickinson, E, Ed, Royal Society of Chemistry: London
    • Dickinson, E.; Euston, S. R. Stability of emulsions containing both protein and polysaccharide. In Food Polymers, Gels and Colloids; Dickinson, E., Ed.; Royal Society of Chemistry: London, 1991; pp 132-146.
    • (1991) Food Polymers, Gels and Colloids , pp. 132-146
    • Dickinson, E.1    Euston, S.R.2
  • 3
    • 0037237311 scopus 로고    scopus 로고
    • Hydrocolloids at interfaces and the influence on the properties of dispersed systems
    • Dickinson, E. Hydrocolloids at interfaces and the influence on the properties of dispersed systems. Food Hydrocolloids 2003, 17, 25-39.
    • (2003) Food Hydrocolloids , vol.17 , pp. 25-39
    • Dickinson, E.1
  • 5
    • 0036097175 scopus 로고    scopus 로고
    • Do not be fobbed off, the substance of beer foam, a review
    • Evans, D. E.; Sheehan, M. C. Do not be fobbed off, the substance of beer foam, a review. J. Am. Soc. Brew. Chem. 2002, 60, 47-57.
    • (2002) J. Am. Soc. Brew. Chem , vol.60 , pp. 47-57
    • Evans, D.E.1    Sheehan, M.C.2
  • 7
    • 0035910388 scopus 로고    scopus 로고
    • Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases
    • Lindorff-Larsen, K.; Winther, J. R. Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. FEBS Lett. 2001, 488, 145-148.
    • (2001) FEBS Lett , vol.488 , pp. 145-148
    • Lindorff-Larsen, K.1    Winther, J.R.2
  • 8
    • 0001686333 scopus 로고    scopus 로고
    • Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form
    • van Wijingaarden, M, Compiler; Oxford University Press: New York
    • Bech, L. M.; Vaag, P.; Heinemann, B.; Breddam, K. Throughout the brewing process barley lipid transfer protein 1 (LTP1) is transformed into a more foam-promoting form, In Proceedings of the 25th European Brewery Convention Congress, Brussels, Belgium, 1995; van Wijingaarden, M., Compiler; Oxford University Press: New York, 1996; pp 561-568.
    • (1996) Proceedings of the 25th European Brewery Convention Congress, Brussels, Belgium, 1995 , pp. 561-568
    • Bech, L.M.1    Vaag, P.2    Heinemann, B.3    Breddam, K.4
  • 9
    • 0033853295 scopus 로고    scopus 로고
    • Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels
    • Douliez, J. P.; Michon, T.; Elmorjani, K.; Marion, D. Structure, biological and technological functions of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels. J. Cereal Sci. 2000, 32, 1-20.
    • (2000) J. Cereal Sci , vol.32 , pp. 1-20
    • Douliez, J.P.1    Michon, T.2    Elmorjani, K.3    Marion, D.4
  • 10
    • 0000604929 scopus 로고
    • New techniques for the evaluation of interactions in foams
    • Maastricht, The Netherlands, Oxford University Press: New York
    • Hughes, P. S.; Wilde, P. J. New techniques for the evaluation of interactions in foams, In Proceedings of the 26th European Brewery Convention Congress, Maastricht, The Netherlands, 1995; Oxford University Press: New York, 1999; pp 525-534.
    • (1995) Proceedings of the 26th European Brewery Convention Congress , pp. 525-534
    • Hughes, P.S.1    Wilde, P.J.2
  • 12
    • 44449135472 scopus 로고    scopus 로고
    • Comparison of the adsorbed conformation of barley lipid transfer protein at the decane-water and vacuum-water interface: A molecular dynamics simulation
    • Euston, S. R.; Hughes, P.; Naser, Md. A.; Westacott, R. E. Comparison of the adsorbed conformation of barley lipid transfer protein at the decane-water and vacuum-water interface: A molecular dynamics simulation. Biomacromolecules 2008, 9, 1443-1453.
    • (2008) Biomacromolecules , vol.9 , pp. 1443-1453
    • Euston, S.R.1    Hughes, P.2    Naser, M.A.3    Westacott, R.E.4
  • 13
    • 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
  • 14
    • 84988129057 scopus 로고
    • Optimization parameters for semi-empirical methods I. Method
    • Stewart, J. J. P. Optimization parameters for semi-empirical methods I. Method. J. Comput. Chem. 1989, 10, 209-220.
    • (1989) J. Comput. Chem , vol.10 , pp. 209-220
    • Stewart, J.J.P.1
  • 15
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force-field based on the free enthalpy of hydration and salvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; van Gunsteren, W. F. A biomolecular force-field based on the free enthalpy of hydration and salvation: The GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 2004, 25, 1656-1676.
    • (2004) J. Comput. Chem , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    van Gunsteren, W.F.4
  • 16
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and Reparametraization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides
    • Kaminski, G. A.; Friesner, R. A.; Tirado-Rives, J.; Jorgensen, W. L. Evaluation and Reparametraization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides. J. Phys. Chem. B 2001, 105, 6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 18
    • 0034761413 scopus 로고    scopus 로고
    • The measurement of hydrophobic polypeptides in beer using the fluorophore 1-anilino-8-napthalene sulfonate
    • Bamforth, C. W.; Kapp, G. R.; Smythe, J. E. The measurement of hydrophobic polypeptides in beer using the fluorophore 1-anilino-8-napthalene sulfonate. Food Chem. 2001, 75, 377-383.
    • (2001) Food Chem , vol.75 , pp. 377-383
    • Bamforth, C.W.1    Kapp, G.R.2    Smythe, J.E.3
  • 19
    • 0242659822 scopus 로고    scopus 로고
    • Beer spoilage bacteria and hop resistance
    • Sakamoto, K.; Konings, W. N. Beer spoilage bacteria and hop resistance. Int. J. Food Microbiol. 2003, 89, 105-124.
    • (2003) Int. J. Food Microbiol , vol.89 , pp. 105-124
    • Sakamoto, K.1    Konings, W.N.2
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. Electrophoresis 1997, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 21
    • 14044276162 scopus 로고    scopus 로고
    • Molecular dynamics simulation of peptide-surface interactions
    • Raut, V. P.; Agashe, M. A.; Stuart, S. J.; Latour, R. A. Molecular dynamics simulation of peptide-surface interactions. Langmuir 2005, 21, 1629-1639.
    • (2005) Langmuir , vol.21 , pp. 1629-1639
    • Raut, V.P.1    Agashe, M.A.2    Stuart, S.J.3    Latour, R.A.4
  • 23
    • 18744394070 scopus 로고    scopus 로고
    • An energy-based method for the prediction of protein-ligand binding sites
    • Laurie, A. T.; Jackson, R. M. Q-SiteFinder: An energy-based method for the prediction of protein-ligand binding sites. Bioinformatics 2005, 21, 1908-1916.
    • (2005) Bioinformatics , vol.21 , pp. 1908-1916
    • Laurie, A.T.1    Jackson, R.2    Q-SiteFinder, M.3
  • 24
    • 0000458011 scopus 로고
    • Isolation and characterization of foaming proteins of beer
    • Asana, K.; Hashimoto, N. Isolation and characterization of foaming proteins of beer. J. Am. Soc. Brew. Chem. 1980, 38B, 129-137.
    • (1980) J. Am. Soc. Brew. Chem , vol.38 B , pp. 129-137
    • Asana, K.1    Hashimoto, N.2
  • 25
    • 0001818725 scopus 로고
    • Stabilisation of beer foams by hop-derived bitter acids. Chemical interactions in beer foam
    • Simpson, W. J.; Hughes, P. S. Stabilisation of beer foams by hop-derived bitter acids. Chemical interactions in beer foam. Cerevisiae Biotechnol. 1994, 19, 39-44.
    • (1994) Cerevisiae Biotechnol , vol.19 , pp. 39-44
    • Simpson, W.J.1    Hughes, P.S.2
  • 26
    • 0021517989 scopus 로고
    • The interaction of sodium caseinate with monoglyceride and diglyceride at the oil/water interface in corn oil-in-water emulsions and its effect on emulsion stability
    • Doxastakis, G.; Sherman, P. The interaction of sodium caseinate with monoglyceride and diglyceride at the oil/water interface in corn oil-in-water emulsions and its effect on emulsion stability. Colloid Polym. Sci. 1984, 262, 902-905.
    • (1984) Colloid Polym. Sci , vol.262 , pp. 902-905
    • Doxastakis, G.1    Sherman, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.