메뉴 건너뛰기




Volumn 135, Issue 1-3, 2008, Pages 51-58

Study of the binding between lysozyme and C10-TAB: Determination and interpretation of the partial properties of protein and surfactant at infinite dilution

Author keywords

Binding; Compressibility; Hydration; Partial volume; Polymeric particle; Protein

Indexed keywords

BROMINE DERIVATIVE; DECYLTRIMETHYLAMMONIUM; LYSOZYME; POLY(METHYL METHACRYLATE); SURFACTANT;

EID: 43049168788     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.03.002     Document Type: Article
Times cited : (8)

References (37)
  • 2
    • 85120252624 scopus 로고
    • C. Tanford The hydrophobic effect: Formation of micelles and biological membranes 1980 Willey New York 146 Chapter 14
    • (1980) , pp. 146
    • Tanford, C.1
  • 4
    • 0028925816 scopus 로고
    • Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility
    • Y. Tamura K. Gekko Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility Biochemistry 34 1995 1878 1884
    • (1995) Biochemistry , vol.34 , pp. 1878-1884
    • Tamura, Y.1    Gekko, K.2
  • 5
    • 0030371848 scopus 로고    scopus 로고
    • The volume and compressibility changes associated with protein denaturation
    • T. Hayashi M. Sakurai K. Nitta The volume and compressibility changes associated with protein denaturation Chem. Lett. 25 1996 723 724
    • (1996) Chem. Lett. , vol.25 , pp. 723-724
    • Hayashi, T.1    Sakurai, M.2    Nitta, K.3
  • 6
    • 0035815110 scopus 로고    scopus 로고
    • Volume, expansibility and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease
    • H. Seemann R. Winter C.A. Royer Volume, expansibility and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease J. Mol. Biol. 307 2001 1091 1102
    • (2001) J. Mol. Biol. , vol.307 , pp. 1091-1102
    • Seemann, H.1    Winter, R.2    Royer, C.A.3
  • 7
    • 0346850625 scopus 로고    scopus 로고
    • Volumetric characterization of homopolymeric amino acids
    • G.D. Noudeh N. Taulier T.V. Chalikian Volumetric characterization of homopolymeric amino acids Biopolymers 70 2003 563 574
    • (2003) Biopolymers , vol.70 , pp. 563-574
    • Noudeh, G.D.1    Taulier, N.2    Chalikian, T.V.3
  • 8
    • 0041846677 scopus 로고    scopus 로고
    • Volume and compressibility changes accompanying thermally-induced native-to-unfolded and molten globule-to-unfolded transitions of cytochrome c: a high pressure study
    • D.N. Dubins R. Filfil R.B. Macgregor Jr. T.V. Chalikian Volume and compressibility changes accompanying thermally-induced native-to-unfolded and molten globule-to-unfolded transitions of cytochrome c : a high pressure study Biochemistry 42 2003 8671 8678
    • (2003) Biochemistry , vol.42 , pp. 8671-8678
    • Dubins, D.N.1    Filfil, R.2    Macgregor, R.B.3    Chalikian, T.V.4
  • 9
    • 0029011017 scopus 로고
    • Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
    • T.V. Chalikian V.S. Gindikin K.J. Breslauer Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH J. Mol. Biol. 250 1995 291 306
    • (1995) J. Mol. Biol. , vol.250 , pp. 291-306
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 10
    • 0031019791 scopus 로고    scopus 로고
    • Molten globule of human a-lactalbumin: hydration, density, and compressibility of the interior
    • D.P. Kharakoz V.E. Bychkova Molten globule of human a-lactalbumin: hydration, density, and compressibility of the interior Biochemistry 36 1997 1882 1890
    • (1997) Biochemistry , vol.36 , pp. 1882-1890
    • Kharakoz, D.P.1    Bychkova, V.E.2
  • 11
    • 0034625325 scopus 로고    scopus 로고
    • Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease
    • R. Filfil T.V. Chalikian Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease J. Mol. Biol. 299 2000 827 842
    • (2000) J. Mol. Biol. , vol.299 , pp. 827-842
    • Filfil, R.1    Chalikian, T.V.2
  • 12
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of beta-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies
    • N. Taulier T.V. Chalikian Characterization of pH-induced transitions of beta-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies J. Mol. Biol. 314 2001 873 889
    • (2001) J. Mol. Biol. , vol.314 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 14
    • 0141842631 scopus 로고    scopus 로고
    • Volumetric study of lysozyme in dimethyl sulfoxide+water solution at 298.15 K
    • T. Kamiyama T. Matsusita T. Kimura Volumetric study of lysozyme in dimethyl sulfoxide + water solution at 298.15 K J. Chem. Eng. Data 48 2003 1301 1305
    • (2003) J. Chem. Eng. Data , vol.48 , pp. 1301-1305
    • Kamiyama, T.1    Matsusita, T.2    Kimura, T.3
  • 15
    • 0345412743 scopus 로고    scopus 로고
    • Ultrasonic studies of alcohol-induced transconformation in b-lactoglobulin: the intermediate State
    • S. Kanjilal N. Taulier J.Y. Le Huérou M. Gindre W. Urbach M. Waks Ultrasonic studies of alcohol-induced transconformation in b-lactoglobulin: the intermediate State Biophys. J. 85 2003 3928 3934
    • (2003) Biophys. J. , vol.85 , pp. 3928-3934
    • Kanjilal, S.1    Taulier, N.2    Le Huérou, J.Y.3    Gindre, M.4    Urbach, W.5    Waks, M.6
  • 16
    • 0344845411 scopus 로고    scopus 로고
    • Effects of disulfide bonds on compactness of protein molecules revealed by volume, compressibility, and expansibility changes during reduction
    • K. Gekko A. Kimoto T. Kamiyama Effects of disulfide bonds on compactness of protein molecules revealed by volume, compressibility, and expansibility changes during reduction Biochemistry 42 2003 13746 13753
    • (2003) Biochemistry , vol.42 , pp. 13746-13753
    • Gekko, K.1    Kimoto, A.2    Kamiyama, T.3
  • 17
    • 0028142863 scopus 로고
    • Influence of drug Binding on DNA hydration: acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)·poly(d AdT) and poly(dA)·poly(dT) duplexes and the poly(dT)·poly(dA)·poly(dT) triplex at 25 °C
    • T.V. Chalikian G.E. Plum A.P. Sarvazyan K.J. Breslauer Influence of drug Binding on DNA hydration: acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)·poly(d AdT) and poly(dA)·poly(dT) duplexes and the poly(dT)·poly(dA)·poly(dT) triplex at 25 °C Biochemistry 33 1994 8629 8640
    • (1994) Biochemistry , vol.33 , pp. 8629-8640
    • Chalikian, T.V.1    Plum, G.E.2    Sarvazyan, A.P.3    Breslauer, K.J.4
  • 18
    • 0000493265 scopus 로고    scopus 로고
    • Role of water in protein–ligand interactions: volumetric characterization of the binding of 2¢-CMP and 3¢-CMP to ribonuclease A
    • D.N. Dubins R. Filfil R.B. Macgregor Jr. T.V. Chalikian Role of water in protein–ligand interactions: volumetric characterization of the binding of 2¢-CMP and 3¢-CMP to ribonuclease A J. Phys. Chem., B 104 2000 390 401
    • (2000) J. Phys. Chem., B , vol.104 , pp. 390-401
    • Dubins, D.N.1    Filfil, R.2    Macgregor, R.B.3    Chalikian, T.V.4
  • 19
    • 0034651716 scopus 로고    scopus 로고
    • Hydration effects of Ni2+ binding to synthetic polynucleotides with regularly alternating purine–pyrimidine sequences
    • B.I. Kankia Hydration effects of Ni2+ binding to synthetic polynucleotides with regularly alternating purine–pyrimidine sequences Nucleic Acids Res. 28 2000 911 916
    • (2000) Nucleic Acids Res. , vol.28 , pp. 911-916
    • Kankia, B.I.1
  • 20
    • 0038451250 scopus 로고    scopus 로고
    • Hydration changes accompanying nucleic acid intercalation reactions: volumetric characterizations
    • F. Han T.V. Chalikian Hydration changes accompanying nucleic acid intercalation reactions: volumetric characterizations J. Am. Chem. Soc. 125 2003 7219 7229
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7219-7229
    • Han, F.1    Chalikian, T.V.2
  • 21
    • 0242710675 scopus 로고    scopus 로고
    • Volumetric and spectroscopic characterizations of glucose–hexokinase association
    • R. Filfil T.V. Chalikian Volumetric and spectroscopic characterizations of glucose–hexokinase association FEBS Letters 554 2003 351 356
    • (2003) FEBS Letters , vol.554 , pp. 351-356
    • Filfil, R.1    Chalikian, T.V.2
  • 22
    • 22244467382 scopus 로고    scopus 로고
    • Association of the minor groove binding drug Hoechst 33258 with d(CGCGAATTCGCG)2: volumetric, calorimetric, and spectroscopic characterizations
    • F. Han N. Taulier T.V. Chalikian, Association of the minor groove binding drug Hoechst 33258 with d(CGCGAATTCGCG)2: volumetric, calorimetric, and spectroscopic characterizations Biochemisty 44 2005 9785 9794
    • (2005) Biochemisty , vol.44 , pp. 9785-9794
    • Han, F.1    Taulier, N.2    Chalikian,, T.V.3
  • 23
    • 11344279926 scopus 로고
    • Partial specific volumes in highly concentrated protein solutions. 2. mixtures of water, bovine hernoglobin, and sodium chloride
    • J. Bernhardt H. Pauly Partial specific volumes in highly concentrated protein solutions. 2. mixtures of water, bovine hernoglobin, and sodium chloride J. Phys. Chem. 81 1977 1290 1295
    • (1977) J. Phys. Chem. , vol.81 , pp. 1290-1295
    • Bernhardt, J.1    Pauly, H.2
  • 24
    • 0038487378 scopus 로고    scopus 로고
    • How large are the volume changes accompanying protein transitions and binding?
    • T.V. Chalikian R. Filfil How large are the volume changes accompanying protein transitions and binding? Biophys. Chemist. 104 2003 489 499
    • (2003) Biophys. Chemist. , vol.104 , pp. 489-499
    • Chalikian, T.V.1    Filfil, R.2
  • 25
    • 11344269737 scopus 로고    scopus 로고
    • Thermodynamics of fractions and its application to the hydration study of the swelling process in functionalized polymer particles
    • M. Corea M.J. García B. Padilla J.M. del Río Thermodynamics of fractions and its application to the hydration study of the swelling process in functionalized polymer particles J. Phys. Chem., B 108 2004 20310 20321
    • (2004) J. Phys. Chem., B , vol.108 , pp. 20310-20321
    • Corea, M.1    García, M.J.2    Padilla, B.3    del Río, J.M.4
  • 26
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °C
    • K. Gekko H. Noguchi Compressibility of globular proteins in water at 25 °C J. Phys. Chem. 83 1979 2706 2714
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 27
    • 0022999267 scopus 로고
    • Compressibility–structure relationship of globular proteins
    • K. Gekko Y. Hasegawa Compressibility–structure relationship of globular proteins Biochemistry 25 1986 6563 6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 28
    • 0001514917 scopus 로고
    • Partial molar volumes, expansibilities, and compressibilities of a,w-aminocarboxylic acids in aqueous solutions between 18 and 55 °C
    • T.V. Chalikian A.P. Sarvazyan K.J. Breslauer Partial molar volumes, expansibilities, and compressibilities of a,w-aminocarboxylic acids in aqueous solutions between 18 and 55 °C J. Phys. Chem 97 1993 13017–13017
    • (1993) J. Phys. Chem , vol.97
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 29
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data
    • T.V. Chalikian M. Totrov R. Abagyan K.J. Breslauer The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data J. Mol. Biol. 260 1996 588 603
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 30
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °C
    • K. Gekko H. Noguchi Compressibility of globular proteins in water at 25 °C J. Phys. Chem. 83 1979 2706 2714
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 31
    • 0002480199 scopus 로고
    • Flexibility of food proteins as revealed by compressibility
    • K. Gekko K. Yamagami Flexibility of food proteins as revealed by compressibility J. Agric. Food Chem. 39 1991 57 62
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 57-62
    • Gekko, K.1    Yamagami, K.2
  • 32
    • 1842539352 scopus 로고    scopus 로고
    • A linear correlation between the energetics of allosteric communication and protein flexibility in the Escherichia coli cyclic AMP receptor protein revealed by mutation-induced changes in compressibility and amide hydrogen–deuterium exchange
    • K. Gekko N. Obu J. Li J.C. Lee A linear correlation between the energetics of allosteric communication and protein flexibility in the Escherichia coli cyclic AMP receptor protein revealed by mutation-induced changes in compressibility and amide hydrogen–deuterium exchange Biochemistry 43 2004 3844 3852
    • (2004) Biochemistry , vol.43 , pp. 3844-3852
    • Gekko, K.1    Obu, N.2    Li, J.3    Lee, J.C.4
  • 34
    • 0033588264 scopus 로고    scopus 로고
    • The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding
    • K. Sasahara M. Sakurai N. Katsutoshi The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding J. Mol. Biol. 291 1999 693 701
    • (1999) J. Mol. Biol. , vol.291 , pp. 693-701
    • Sasahara, K.1    Sakurai, M.2    Katsutoshi, N.3
  • 35
    • 0002050426 scopus 로고
    • Conformational transitions of proteins in water and in aqueous solutions mixtures
    • J.F. Brandts Conformational transitions of proteins in water and in aqueous solutions mixtures S.N. Timasheff G.D. Fasman Structure and Stability of Biological Macromolecules 1969 Marcel Dekker, Inc New York 213 290
    • (1969) , pp. 213-290
    • Brandts, J.F.1
  • 36
  • 37
    • 0014268486 scopus 로고
    • The inhibitory interaction of cationic detergents with the active center of lysozyme. 11. The pH dependence of the interaction
    • K. Hayashi M. Kugimiya T. Imoto M. Funatsu C.C. Bigelow The inhibitory interaction of cationic detergents with the active center of lysozyme. 11. The pH dependence of the interaction Biochemisty 7 1968 1467 1472
    • (1968) Biochemisty , vol.7 , pp. 1467-1472
    • Hayashi, K.1    Kugimiya, M.2    Imoto, T.3    Funatsu, M.4    Bigelow, C.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.