메뉴 건너뛰기




Volumn 34, Issue , 2014, Pages 98-103

Dilational surface viscoelasticity of protein solutions. Impact of urea

Author keywords

Bovine serum albumin; Dilational surface elasticity; Protein unfolding; Urea; Lactoglobulin

Indexed keywords

BOVINAE;

EID: 84884533480     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2012.12.012     Document Type: Article
Times cited : (27)

References (50)
  • 3
    • 0036403888 scopus 로고    scopus 로고
    • Use of fl{ligature}uorescence methods to monitor unfolding transitions in beta-lactoglobulin
    • Busti P., Scarpeci S., Gatti C., Delorenzi N. Use of fl{ligature}uorescence methods to monitor unfolding transitions in beta-lactoglobulin. Food Research International 2002, 35:871-877.
    • (2002) Food Research International , vol.35 , pp. 871-877
    • Busti, P.1    Scarpeci, S.2    Gatti, C.3    Delorenzi, N.4
  • 5
    • 40949118015 scopus 로고    scopus 로고
    • Structural evolution during protein denaturation as induced by different methods
    • Chodankar S., Aswal V.K., Kohlbrecher J., Vavrin R., Wagh A.G. Structural evolution during protein denaturation as induced by different methods. Physical Review E 2008, 77:031901.
    • (2008) Physical Review E , vol.77 , pp. 031901
    • Chodankar, S.1    Aswal, V.K.2    Kohlbrecher, J.3    Vavrin, R.4    Wagh, A.G.5
  • 7
    • 61949248655 scopus 로고    scopus 로고
    • Astudy of urea-dependent denaturation of beta-lactoglobulin by principal component analysis and two-dimensional correlation spectroscopy
    • Czarnik-Matusewicz B., Kim S.B., Jung Y.M. Astudy of urea-dependent denaturation of beta-lactoglobulin by principal component analysis and two-dimensional correlation spectroscopy. Journal of Physical Chemistry B 2009, 113:559-566.
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 559-566
    • Czarnik-Matusewicz, B.1    Kim, S.B.2    Jung, Y.M.3
  • 8
    • 0037039276 scopus 로고    scopus 로고
    • Does beta-lactoglobulin denaturation occur via an intermediate state?
    • D'Alfonso L., Collini M., Baldini G. Does beta-lactoglobulin denaturation occur via an intermediate state?. Biochemistry 2002, 41:326-333.
    • (2002) Biochemistry , vol.41 , pp. 326-333
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 9
    • 10044273812 scopus 로고    scopus 로고
    • In situ measurement of conformational changes in proteins at liquid interfaces by circular dichroism spectroscopy
    • Damodaran S. In situ measurement of conformational changes in proteins at liquid interfaces by circular dichroism spectroscopy. Analytical and Bioanalytical Chemistry 2003, 376:182-188.
    • (2003) Analytical and Bioanalytical Chemistry , vol.376 , pp. 182-188
    • Damodaran, S.1
  • 10
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran S. Protein stabilization of emulsions and foams. Journal of Food Science 2005, 70:R54-R56.
    • (2005) Journal of Food Science , vol.70
    • Damodaran, S.1
  • 11
    • 4344647662 scopus 로고    scopus 로고
    • Structural changes during the unfolding of bovine serum albumin in the presence of urea: a small-angle neutron scattering study
    • Das A., Chitra R., Choudhury R.R., Ramanadham M. Structural changes during the unfolding of bovine serum albumin in the presence of urea: a small-angle neutron scattering study. Pramana - Journal of Physics 2004, 63:363-368.
    • (2004) Pramana - Journal of Physics , vol.63 , pp. 363-368
    • Das, A.1    Chitra, R.2    Choudhury, R.R.3    Ramanadham, M.4
  • 12
    • 12144259012 scopus 로고    scopus 로고
    • Dissecting contributions to the denaturant sensitivities of proteins
    • Dempsey C.E., Piggot T.J., Mason P.E. Dissecting contributions to the denaturant sensitivities of proteins. Biochemistry 2005, 44:775-781.
    • (2005) Biochemistry , vol.44 , pp. 775-781
    • Dempsey, C.E.1    Piggot, T.J.2    Mason, P.E.3
  • 13
    • 79651472499 scopus 로고    scopus 로고
    • Double emulsions stabilized by food biopolymers
    • Dickinson E. Double emulsions stabilized by food biopolymers. Food Biophysics 2011, 6:1-11.
    • (2011) Food Biophysics , vol.6 , pp. 1-11
    • Dickinson, E.1
  • 14
    • 0036400715 scopus 로고    scopus 로고
    • Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    • Dyson H.J., Wright P.E. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Advances in Protein Chemistry 2002, 62:311-340.
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 311-340
    • Dyson, H.J.1    Wright, P.E.2
  • 16
    • 79953759344 scopus 로고    scopus 로고
    • Role of salvation effects in protein denaturation: from thermodynamics to single molecules and back
    • England J.L., Haran G. Role of salvation effects in protein denaturation: from thermodynamics to single molecules and back. Annual Review of Physical Chemistry 2011, 62:257-277.
    • (2011) Annual Review of Physical Chemistry , vol.62 , pp. 257-277
    • England, J.L.1    Haran, G.2
  • 17
    • 49249153429 scopus 로고
    • Proteins at liquid interfaces: I. Kinetics of adsorption and surface denaturation
    • Graham D.E., Phillips M.C. Proteins at liquid interfaces: I. Kinetics of adsorption and surface denaturation. Journal of Colloid & Interface Science 1979, 70:403-414.
    • (1979) Journal of Colloid & Interface Science , vol.70 , pp. 403-414
    • Graham, D.E.1    Phillips, M.C.2
  • 18
  • 19
    • 0022651532 scopus 로고
    • Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin
    • Khan M.Y. Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin. Biochemical Journal 1986, 236:307-310.
    • (1986) Biochemical Journal , vol.236 , pp. 307-310
    • Khan, M.Y.1
  • 20
    • 0023388641 scopus 로고
    • Urea-induced structural transformations in bovine serum albumin
    • Khan M.Y., Agarwal S.K., Hangloo S. Urea-induced structural transformations in bovine serum albumin. Journal of Biochemistry 1987, 102:313-317.
    • (1987) Journal of Biochemistry , vol.102 , pp. 313-317
    • Khan, M.Y.1    Agarwal, S.K.2    Hangloo, S.3
  • 22
    • 70349132068 scopus 로고    scopus 로고
    • Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid
    • Leggio C., Galantini L., Konarev P.V., Pavel N.V. Urea-induced denaturation process on defatted human serum albumin and in the presence of palmitic acid. Journal of Physical Chemistry B 2009, 113:12590-12602.
    • (2009) Journal of Physical Chemistry B , vol.113 , pp. 12590-12602
    • Leggio, C.1    Galantini, L.2    Konarev, P.V.3    Pavel, N.V.4
  • 24
    • 33845902554 scopus 로고    scopus 로고
    • Urea- and thermal-induced unfolding of bovine serum albumin
    • Ma B., Tie Z., Zou D., Li J., Wang W. Urea- and thermal-induced unfolding of bovine serum albumin. Modern Physics Letters B 2006, 20:1909-1916.
    • (2006) Modern Physics Letters B , vol.20 , pp. 1909-1916
    • Ma, B.1    Tie, Z.2    Zou, D.3    Li, J.4    Wang, W.5
  • 26
    • 18544382218 scopus 로고    scopus 로고
    • Correlation between mechanical behavior of protein films at the air/water interface and intrinsic stability of protein molecules
    • Martin A.H., Cohen Stuart M.A., Bos M.A., van Vliet T. Correlation between mechanical behavior of protein films at the air/water interface and intrinsic stability of protein molecules. Langmuir 2005, 21:4083-4089.
    • (2005) Langmuir , vol.21 , pp. 4083-4089
    • Martin, A.H.1    Cohen Stuart, M.A.2    Bos, M.A.3    van Vliet, T.4
  • 27
    • 0037723870 scopus 로고    scopus 로고
    • Conformational aspects of proteins at the air/water interface studied by infrared reflection-absorption spectroscopy
    • Martin A.H., Meinders M.B.J., Bos M.A., Cohen Stuart M.A., van Vliet T. Conformational aspects of proteins at the air/water interface studied by infrared reflection-absorption spectroscopy. Langmuir 2003, 19:2922-2928.
    • (2003) Langmuir , vol.19 , pp. 2922-2928
    • Martin, A.H.1    Meinders, M.B.J.2    Bos, M.A.3    Cohen Stuart, M.A.4    van Vliet, T.5
  • 28
    • 84860390288 scopus 로고    scopus 로고
    • Formation of protein/surfactant adsorption layer at the air/water interface as studied by dilational surface rheology
    • Mikhailovskaya A.A., Noskov B.A., Lin S.-Y., Loglio G., Miller R. Formation of protein/surfactant adsorption layer at the air/water interface as studied by dilational surface rheology. Journal of Physical Chemistry B 2011, 115:9971-9979.
    • (2011) Journal of Physical Chemistry B , vol.115 , pp. 9971-9979
    • Mikhailovskaya, A.A.1    Noskov, B.A.2    Lin, S.-Y.3    Loglio, G.4    Miller, R.5
  • 30
    • 77954029652 scopus 로고    scopus 로고
    • Dilational surface rheology of polymer and polymer/surfactant solutions
    • Noskov B.A. Dilational surface rheology of polymer and polymer/surfactant solutions. Current Opinion in Colloid & Interface Science 2010, 15:229-236.
    • (2010) Current Opinion in Colloid & Interface Science , vol.15 , pp. 229-236
    • Noskov, B.A.1
  • 34
    • 33746883952 scopus 로고    scopus 로고
    • Dynamic surface elasticity of polyelectrolyte/surfactant adsorption films at the air/water interface: dodecyltrimethylammonium bromide and copolymer of sodium 2-acrylamido-2-methyl-1-propansulfonate with N-isopropylacrylamide
    • Noskov B.A., Loglio G., Lin S.-Y., Miller R. Dynamic surface elasticity of polyelectrolyte/surfactant adsorption films at the air/water interface: dodecyltrimethylammonium bromide and copolymer of sodium 2-acrylamido-2-methyl-1-propansulfonate with N-isopropylacrylamide. Journal of Colloid & Interface Science 2006, 301:386-394.
    • (2006) Journal of Colloid & Interface Science , vol.301 , pp. 386-394
    • Noskov, B.A.1    Loglio, G.2    Lin, S.-Y.3    Miller, R.4
  • 35
    • 80053567944 scopus 로고    scopus 로고
    • Dilational surface visco-elasticity of polyelectrolyte/surfactant solutions: formation of heterogeneous adsorption layers
    • Noskov B.A., Loglio G., Miller R. Dilational surface visco-elasticity of polyelectrolyte/surfactant solutions: formation of heterogeneous adsorption layers. Advances in Colloid & Interface Science 2011, 168:179-197.
    • (2011) Advances in Colloid & Interface Science , vol.168 , pp. 179-197
    • Noskov, B.A.1    Loglio, G.2    Miller, R.3
  • 36
    • 78650349817 scopus 로고    scopus 로고
    • Bovine serum albumin unfolding at the air/water interface as studied by dilational surface rheology
    • Noskov B.A., Mikhailovskaya A.A., Lin S.-Y., Loglio G., Miller R. Bovine serum albumin unfolding at the air/water interface as studied by dilational surface rheology. Langmuir 2010, 26:17225-17231.
    • (2010) Langmuir , vol.26 , pp. 17225-17231
    • Noskov, B.A.1    Mikhailovskaya, A.A.2    Lin, S.-Y.3    Loglio, G.4    Miller, R.5
  • 37
    • 0036637655 scopus 로고    scopus 로고
    • Revised conformational stability parameters for beta-lactoglobulin isothermal denaturation by urea
    • Owusu-Apenten I.K. Revised conformational stability parameters for beta-lactoglobulin isothermal denaturation by urea. Journal of Food Biochemistry 2002, 26:181-190.
    • (2002) Journal of Food Biochemistry , vol.26 , pp. 181-190
    • Owusu-Apenten, I.K.1
  • 41
    • 0041831002 scopus 로고    scopus 로고
    • Structure and denaturation of adsorbed lysozyme at the air-water interface
    • Postel C., Abillon O., Desbat B. Structure and denaturation of adsorbed lysozyme at the air-water interface. Journal of Colloid & Interface Science 2003, 266:74-81.
    • (2003) Journal of Colloid & Interface Science , vol.266 , pp. 74-81
    • Postel, C.1    Abillon, O.2    Desbat, B.3
  • 43
  • 44
    • 0029896525 scopus 로고    scopus 로고
    • Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects
    • Smith J.S., Scholtz J.M. Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects. Biochemistry 1996, 35:7292-7297.
    • (1996) Biochemistry , vol.35 , pp. 7292-7297
    • Smith, J.S.1    Scholtz, J.M.2
  • 45
    • 0034649231 scopus 로고    scopus 로고
    • Use of domain specifl{ligature}c ligands to study urea-induced unfolding of bovine serum albumin
    • Tayyab S., Sharma N., Khan M.M. Use of domain specifl{ligature}c ligands to study urea-induced unfolding of bovine serum albumin. Biochemical and Biophysical Research Communications 2000, 277:83-88.
    • (2000) Biochemical and Biophysical Research Communications , vol.277 , pp. 83-88
    • Tayyab, S.1    Sharma, N.2    Khan, M.M.3
  • 46
    • 0037343333 scopus 로고    scopus 로고
    • The dominant interaction between peptide and urea is electrostatic in nature: a molecular dynamic simulation study
    • Tobi D., Elber R., Thirumalai D. The dominant interaction between peptide and urea is electrostatic in nature: a molecular dynamic simulation study. Biopolymers 2003, 68:359-369.
    • (2003) Biopolymers , vol.68 , pp. 359-369
    • Tobi, D.1    Elber, R.2    Thirumalai, D.3
  • 47
    • 36549015809 scopus 로고    scopus 로고
    • Unfolding kinetics of beta-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study
    • Viseu M.I., Melo E.P., Carvalho T.I., Correia R.F., Costa S.M.B. Unfolding kinetics of beta-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study. Biophysical Journal 2007, 93:3601-3612.
    • (2007) Biophysical Journal , vol.93 , pp. 3601-3612
    • Viseu, M.I.1    Melo, E.P.2    Carvalho, T.I.3    Correia, R.F.4    Costa, S.M.B.5
  • 50
    • 60849085453 scopus 로고    scopus 로고
    • Driving force behind adsorption-induced protein unfolding: a time-resolved X-ray reflectivity study on lysozyme adsorbed at an air/water interface
    • Yano Y.F., Uruga T., Tanida H., Toyokawa H., Terada Y., Takagaki M., et al. Driving force behind adsorption-induced protein unfolding: a time-resolved X-ray reflectivity study on lysozyme adsorbed at an air/water interface. Langmuir 2009, 25:32-35.
    • (2009) Langmuir , vol.25 , pp. 32-35
    • Yano, Y.F.1    Uruga, T.2    Tanida, H.3    Toyokawa, H.4    Terada, Y.5    Takagaki, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.