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Volumn 84, Issue 5, 2003, Pages 611-616

The Influence of Molecular Variation on Protein Interactions

Author keywords

Lysozyme; Molecular variation; Protein interactions; Second virial; Solvation forces

Indexed keywords

HYDROPHOBICITY; PROTEINS;

EID: 0242301201     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10815     Document Type: Article
Times cited : (5)

References (21)
  • 1
    • 0000303810 scopus 로고
    • Interaction between particles suspended in solutions of macromolecules
    • Asakura S, Oosawa F. 1958. Interaction between particles suspended in solutions of macromolecules. J Polym Sci. 33:183-192.
    • (1958) J Polym Sci , vol.33 , pp. 183-192
    • Asakura, S.1    Oosawa, F.2
  • 2
    • 0037196817 scopus 로고    scopus 로고
    • Molecular thermodynamics and bioprocessing: From intracellullar events to bioseparations
    • Blanch HW, Prausnitz JM, Curtis RA, Bratko D. 2002. Molecular thermodynamics and bioprocessing: From intracellullar events to bioseparations. Fluid Phase Equilibria. 194-197:31-41.
    • (2002) Fluid Phase Equilibria , vol.194-197 , pp. 31-41
    • Blanch, H.W.1    Prausnitz, J.M.2    Curtis, R.A.3    Bratko, D.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochem 72:248-254.
    • (1976) Analytical Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0037076107 scopus 로고    scopus 로고
    • Orientation-averaged pair potentials between dipolar proteins of colloids
    • Bratko D, Stroilo A, Wu Z, Blanch HW, Prausnitz JM. 2002. Orientation-averaged pair potentials between dipolar proteins of colloids. J Phys Chem 106:2714-2720.
    • (2002) J Phys Chem , vol.106 , pp. 2714-2720
    • Bratko, D.1    Stroilo, A.2    Wu, Z.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 5
    • 0029278478 scopus 로고
    • Salting-out of aqueous proteins: Phase equilibria and intermolecular potentials
    • Coen CJ, Blanch HW, Prausnitz JM. 1995. Salting-out of aqueous proteins: Phase equilibria and intermolecular potentials. AIChE J 41:996-1004.
    • (1995) AIChE J , vol.41 , pp. 996-1004
    • Coen, C.J.1    Blanch, H.W.2    Prausnitz, J.M.3
  • 6
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis RA, Prausnitz JM, Blanch HW. 1998. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol Bioeng 57(1):11-21.
    • (1998) Biotechnol Bioeng , vol.57 , Issue.1 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 7
    • 0037008361 scopus 로고    scopus 로고
    • Hydrophobic forces between protein molecules in aqueous solutions of concentrated electrolyte
    • Curtis RA, Steinbrecher C, Heinemann M, Blanch HW. Prausnitz JM. 2002. Hydrophobic forces between protein molecules in aqueous solutions of concentrated electrolyte. Biophys Chem 98:249-265.
    • (2002) Biophys Chem , vol.98 , pp. 249-265
    • Curtis, R.A.1    Steinbrecher, C.2    Heinemann, M.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 9
    • 0027904389 scopus 로고
    • Formation dynamics of protein precrystallization fractal-clusters
    • Georgalis Y, Zoumi A, Eberstein W, Saenger W. 1993. Formation dynamics of protein precrystallization fractal-clusters. J Cryst Growth 126:245-260.
    • (1993) J Cryst Growth , vol.126 , pp. 245-260
    • Georgalis, Y.1    Zoumi, A.2    Eberstein, W.3    Saenger, W.4
  • 10
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George A, Wilson WW. 1994. Predicting protein crystallization from a dilute solution property. Acta Crystallogr D. 50:361-365.
    • (1994) Acta Crystallogr D , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 12
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient
    • Ho JGS, Middelberg APJ, Ramage P, Kocher HP. 2003. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Prot Sci 12:708-716.
    • (2003) Prot Sci , vol.12 , pp. 708-716
    • Ho, J.G.S.1    Middelberg, A.P.J.2    Ramage, P.3    Kocher, H.P.4
  • 15
    • 23544458810 scopus 로고
    • The statistical thermodynamics of multicomponent systems
    • McMillan WG, Mayer JE. 1945. The statistical thermodynamics of multicomponent systems. J Chem Phys 13:276-305.
    • (1945) J Chem Phys , vol.13 , pp. 276-305
    • McMillan, W.G.1    Mayer, J.E.2
  • 16
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • Neal BL, Asthagiri D, Lenhoff AM. 1998. Molecular origins of osmotic second virial coefficients of proteins. Biophys J 75:2469-2477.
    • (1998) Biophys J , vol.75 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 17
    • 2842530177 scopus 로고
    • Van-der Waals interactions between surfaces of biological interest
    • Nir S. 1976. Van-der Waals interactions between surfaces of biological interest. Prog Surf Sci 8:1-58.
    • (1976) Prog Surf Sci , vol.8 , pp. 1-58
    • Nir, S.1
  • 18
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal growth of proteins
    • Ries-Kautt MA, Ducruix AF. 1989. Relative effectiveness of various ions on the solubility and crystal growth of proteins. J Biol Chem 264:745-750.
    • (1989) J Biol Chem , vol.264 , pp. 745-750
    • Ries-Kautt, M.A.1    Ducruix, A.F.2
  • 19
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solutions characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • Velev OD, Kaler EW, Lenhoff AM, 1998. Protein interactions in solutions characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen. Biophys J 75:2682-2697.
    • (1998) Biophys J , vol.75 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 21
    • 49049146776 scopus 로고
    • Osmotic pressure of concentrated protein solutions: The effect of concentration and pH in saline solutions of bovine serum albumin
    • Viiker VL, Colton CK, Smith KA. 1981. Osmotic pressure of concentrated protein solutions: The effect of concentration and pH in saline solutions of bovine serum albumin. J Colloid Interf Sci 79:548-566.
    • (1981) J Colloid Interf Sci , vol.79 , pp. 548-566
    • Viiker, V.L.1    Colton, C.K.2    Smith, K.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.