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Volumn 32, Issue 31, 2016, Pages 7821-7828

Structure and Dynamics of Heteroprotein Coacervates

Author keywords

[No Author keywords available]

Indexed keywords

MEDICAL APPLICATIONS; PHASE SEPARATION; PHOTOBLEACHING; PROTEINS;

EID: 84981532051     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/acs.langmuir.6b01015     Document Type: Article
Times cited : (21)

References (23)
  • 3
    • 84947556525 scopus 로고    scopus 로고
    • On the complexation of whey proteins
    • Delboni, L. A.; da Silva, F. L. B. On the complexation of whey proteins Food Hydrocolloids 2016, 55, 89-99 10.1016/j.foodhyd.2015.11.010
    • (2016) Food Hydrocolloids , vol.55 , pp. 89-99
    • Delboni, L.A.1    Da Silva, F.L.B.2
  • 5
    • 84891371192 scopus 로고    scopus 로고
    • Charge and size drive spontaneous self-assembly of oppositely charged globular proteins into microspheres
    • Desfougères, Y.; Croguennec, T.; Lechevalier, V.; Bouhallab, S.; Nau, F. Charge and size drive spontaneous self-assembly of oppositely charged globular proteins into microspheres J. Phys. Chem. B 2010, 114, 4138-4144 10.1021/jp9090427
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4138-4144
    • Desfougères, Y.1    Croguennec, T.2    Lechevalier, V.3    Bouhallab, S.4    Nau, F.5
  • 6
    • 33846849437 scopus 로고    scopus 로고
    • Temperature affects the supramolecular structures resulting from alpha-lactalbumin-lysozyme interaction
    • Nigen, M.; Croguennec, T.; Renard, D.; Bouhallab, S. Temperature affects the supramolecular structures resulting from alpha-lactalbumin-lysozyme interaction Biochemistry 2007, 46, 1248-1255 10.1021/bi062129c
    • (2007) Biochemistry , vol.46 , pp. 1248-1255
    • Nigen, M.1    Croguennec, T.2    Renard, D.3    Bouhallab, S.4
  • 7
    • 84876466339 scopus 로고    scopus 로고
    • Coacervates of lysozyme and β-casein
    • Anema, S. G.; de Kruif, C. G. Coacervates of lysozyme and β-casein J. Colloid Interface Sci. 2013, 398, 255-261 10.1016/j.jcis.2013.02.013
    • (2013) J. Colloid Interface Sci. , vol.398 , pp. 255-261
    • Anema, S.G.1    De Kruif, C.G.2
  • 8
    • 84880851921 scopus 로고    scopus 로고
    • Protein Composition of Different Sized Casein Micelles in Milk after the Binding of Lactoferrin or Lysozyme
    • Anema, S. G.; de Kruif, C. G. Protein Composition of Different Sized Casein Micelles in Milk after the Binding of Lactoferrin or Lysozyme J. Agric. Food Chem. 2013, 61, 7142-7149 10.1021/jf401270h
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 7142-7149
    • Anema, S.G.1    De Kruif, C.G.2
  • 9
    • 84902658539 scopus 로고    scopus 로고
    • Complex coacervates of lactotransferrin and β-lactoglobulin
    • Anema, S. G.; de Kruif, C. G. Complex coacervates of lactotransferrin and β-lactoglobulin J. Colloid Interface Sci. 2014, 430, 214-220 10.1016/j.jcis.2014.05.036
    • (2014) J. Colloid Interface Sci. , vol.430 , pp. 214-220
    • Anema, S.G.1    De Kruif, C.G.2
  • 10
    • 84924859406 scopus 로고    scopus 로고
    • Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
    • Tavares, G. M.; Croguennec, T.; Hamon, P.; Carvalho, A. F.; Bouhallab, S. Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin Food Hydrocolloids 2015, 48, 238-247 10.1016/j.foodhyd.2015.02.027
    • (2015) Food Hydrocolloids , vol.48 , pp. 238-247
    • Tavares, G.M.1    Croguennec, T.2    Hamon, P.3    Carvalho, A.F.4    Bouhallab, S.5
  • 12
    • 84879916282 scopus 로고    scopus 로고
    • PyDockWEB: A web server for rigid-body protein-protein docking using electrostatics and desolvation scoring
    • Jimenez-Garcia, B.; Pons, C.; Fernandez-Recio, J. pyDockWEB: a web server for rigid-body protein-protein docking using electrostatics and desolvation scoring Bioinformatics 2013, 29, 1698-1699 10.1093/bioinformatics/btt262
    • (2013) Bioinformatics , vol.29 , pp. 1698-1699
    • Jimenez-Garcia, B.1    Pons, C.2    Fernandez-Recio, J.3
  • 13
    • 0029831680 scopus 로고    scopus 로고
    • An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies
    • Kelley, L. A.; Gardner, S. P.; Sutcliffe, M. J. An automated approach for clustering an ensemble of NMR-derived protein structures into conformationally related subfamilies Protein Eng., Des. Sel. 1996, 9, 1063-1065 10.1093/protein/9.11.1063
    • (1996) Protein Eng., Des. Sel. , vol.9 , pp. 1063-1065
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 15
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD: visual molecular dynamics J. Mol. Graphics 1996, 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 16
    • 60849099921 scopus 로고    scopus 로고
    • Reversible binding and rapid diffusion of proteins in complex with inositol lipids serves to coordinate free movement with spatial information
    • Hammond, G. R. V.; Sim, Y.; Lagnado, L.; Irvine, R. F. Reversible binding and rapid diffusion of proteins in complex with inositol lipids serves to coordinate free movement with spatial information J. Cell Biol. 2009, 184, 297-308 10.1083/jcb.200809073
    • (2009) J. Cell Biol. , vol.184 , pp. 297-308
    • Hammond, G.R.V.1    Sim, Y.2    Lagnado, L.3    Irvine, R.F.4
  • 17
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • Sprague, B.; McNally, J. FRAP analysis of binding: proper and fitting Trends Cell Biol. 2005, 15, 84-91 10.1016/j.tcb.2004.12.001
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.1    McNally, J.2
  • 18
    • 84922598329 scopus 로고    scopus 로고
    • Diffusion and Partitioning of Macromolecules in Casein Microgels: Evidence for Size-Dependent Attractive Interactions in a Dense Protein System
    • Peixoto, P. D. S.; Bouchoux, A.; Huet, S.; Madec, M.-N.; Thomas, D.; Floury, J.; Gésan-Guiziou, G. Diffusion and Partitioning of Macromolecules in Casein Microgels: Evidence for Size-Dependent Attractive Interactions in a Dense Protein System Langmuir 2015, 31, 1755-1765 10.1021/la503657u
    • (2015) Langmuir , vol.31 , pp. 1755-1765
    • Peixoto, P.D.S.1    Bouchoux, A.2    Huet, S.3    Madec, M.-N.4    Thomas, D.5    Floury, J.6    Gésan-Guiziou, G.7
  • 19
    • 84884355981 scopus 로고    scopus 로고
    • Transport phenomena in a model cheese: The influence of the charge and shape of solutes on diffusion
    • Silva, J. V. C.; Peixoto, P. D. S.; Lortal, S.; Floury, J. Transport phenomena in a model cheese: the influence of the charge and shape of solutes on diffusion J. Dairy Sci. 2013, 96, 6186-6198 10.3168/jds.2013-6552
    • (2013) J. Dairy Sci. , vol.96 , pp. 6186-6198
    • Silva, J.V.C.1    Peixoto, P.D.S.2    Lortal, S.3    Floury, J.4
  • 20
    • 43949090375 scopus 로고    scopus 로고
    • Fundamentals of protein NMR spectroscopy
    • Springer: New Delhi, India
    • Rule, G. S.; Hitchens, T. K. Fundamentals of protein NMR spectroscopy. In Focus on Structural Biology; Springer: New Delhi, India, 2006; Vol. 5.
    • (2006) Focus on Structural Biology , vol.5
    • Rule, G.S.1    Hitchens, T.K.2
  • 21
    • 0000073926 scopus 로고
    • Measurement of proton relaxation rates in proteins
    • Boulat, B.; Bodenhausen, G. Measurement of proton relaxation rates in proteins J. Biomol. NMR 1993, 3, 335-348 10.1007/BF00212519
    • (1993) J. Biomol. NMR , vol.3 , pp. 335-348
    • Boulat, B.1    Bodenhausen, G.2
  • 22
    • 78649876151 scopus 로고    scopus 로고
    • Crowding and hydrodynamic interactions likely dominate in vivo macromolecular motion
    • Ando, T.; Skolnick, J. Crowding and hydrodynamic interactions likely dominate in vivo macromolecular motion Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 18457-18462 10.1073/pnas.1011354107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18457-18462
    • Ando, T.1    Skolnick, J.2
  • 23
    • 80053467043 scopus 로고    scopus 로고
    • Mobility of nonsticky nanoparticles in polymer liquids
    • Cai, L.-H.; Panyukov, S.; Rubinstein, M. Mobility of nonsticky nanoparticles in polymer liquids Macromolecules 2011, 44, 7853-7863 10.1021/ma201583q
    • (2011) Macromolecules , vol.44 , pp. 7853-7863
    • Cai, L.-H.1    Panyukov, S.2    Rubinstein, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.