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Volumn 89, Issue , 2012, Pages 177-186

Comparative spectroscopic studies on drug binding characteristics and protein surface hydrophobicity of native and modified forms of bovine serum albumin: Possible relevance to change in protein structure/function upon non-enzymatic glycation

Author keywords

Binding site; Bovine serum albumin; Fluorescence quenching; Furosemide; Indomethacin; Protein surface hydrophobicity

Indexed keywords

BOVINE SERUM ALBUMINS; FLUORESCENCE QUENCHING; FUROSEMIDES; INDOMETHACIN; PROTEIN SURFACE HYDROPHOBICITY;

EID: 84856927345     PISSN: 13861425     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.saa.2011.12.058     Document Type: Article
Times cited : (77)

References (56)
  • 1
    • 79955983981 scopus 로고    scopus 로고
    • Effect of human serum albumin on the kinetics of N-glutaryl-L- phenylalanine p-nitroanilide hydrolysis catalyzed by a-chymotrypsin
    • E. Abuin, E. Lissi, M. Ahumada, and C. Calderon Effect of human serum albumin on the kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by a-chymotrypsin Protein J. 30 2011 143 147
    • (2011) Protein J. , vol.30 , pp. 143-147
    • Abuin, E.1    Lissi, E.2    Ahumada, M.3    Calderon, C.4
  • 3
    • 0019538149 scopus 로고
    • Molecular aspects of ligand binding to serum albumin
    • U. Kragh-Hansen Molecular aspects of ligand binding to serum albumin Pharmacol. Rev. 33 1981 17 53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 6
    • 1342343021 scopus 로고    scopus 로고
    • Study of the interaction of kaempferol with bovine serum albumin
    • DOI 10.1016/j.molstruc.2003.12.019
    • J.N. Tian, J.Q. Liu, X. Tian, Z.D. Hu, and X.G. Chen Study of the interaction of kaempferol with bovine serum albumin J. Mol. Struct. 691 2004 197 202 (Pubitemid 38251535)
    • (2004) Journal of Molecular Structure , vol.691 , Issue.1-3 , pp. 197-202
    • Tian, J.1    Liu, J.2    Tian, X.3    Hu, Z.4    Chen, X.5
  • 7
    • 0028948733 scopus 로고
    • In vitro study of the protein-binding of fusidic acid - A contribution to the comprehension of its pharmacokinetic behavior
    • A. Rieutord, P. Bourget, G. Troche, and J.F. Zazzo In vitro study of the protein-binding of fusidic acid - a contribution to the comprehension of its pharmacokinetic behavior Int. J. Pharm. 119 1995 57 64
    • (1995) Int. J. Pharm. , vol.119 , pp. 57-64
    • Rieutord, A.1    Bourget, P.2    Troche, G.3    Zazzo, J.F.4
  • 8
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, and D.N. Wade The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 11 1975 824 832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 9
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, and D.N. Wade Further characterization of specific drug binding sites on human serum albumin Mol. Pharmacol. 12 1976 1052 1061
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 10
    • 0030749791 scopus 로고    scopus 로고
    • Identification of subdomain IB in human serum albumin as a major binding site for polycyclic aromatic hydrocarbon epoxides
    • DOI 10.1021/tx9700782
    • P. Brunmark, S. Harriman, P.L. Skipper, J.S. Wishnok, S. Amin, and S.R. Tannenbaum Identification of subdomain IB in human serum albumin as a major binding site for polycyclic aromatic hydrocarbon epoxides Chem. Res. Toxicol. 10 1997 880 886 (Pubitemid 27350047)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.8 , pp. 880-886
    • Brunmark, P.1    Harriman, S.2    Skipper, P.L.3    Wishnok, J.S.4    Amin, S.5    Tannenbaum, S.R.6
  • 11
    • 81155150399 scopus 로고    scopus 로고
    • Interaction between phillygenin and human serum albumin based on spectroscopic and molecular docking
    • 10.1016/j.saa.2011.09.044
    • W. Song, M.Z. Ao, Y. Shi, L.F. Yuan, X.X. Yuan, and L.J. Yu Interaction between phillygenin and human serum albumin based on spectroscopic and molecular docking Spectrochim. Acta A 2011 10.1016/j.saa.2011.09.044
    • (2011) Spectrochim. Acta A
    • Song, W.1    Ao, M.Z.2    Shi, Y.3    Yuan, L.F.4    Yuan, X.X.5    Yu, L.J.6
  • 12
    • 80052943071 scopus 로고    scopus 로고
    • Investigation of the binding of Salvianolic acid B to human serum albumin and the effect of metal ions on the binding
    • T. Chen, H. Cao, S. Zhu, Y. Lu, Y. Shang, M. Wang, Y. Tang, and L. Zhu Investigation of the binding of Salvianolic acid B to human serum albumin and the effect of metal ions on the binding Spectrochim. Acta A 81 2011 645 652
    • (2011) Spectrochim. Acta A , vol.81 , pp. 645-652
    • Chen, T.1    Cao, H.2    Zhu, S.3    Lu, Y.4    Shang, Y.5    Wang, M.6    Tang, Y.7    Zhu, L.8
  • 13
    • 0025301143 scopus 로고
    • Structure of human serum albumin
    • D.C. Carter, and X.M. He Structure of human serum albumin Science 249 1990 302 303 (Pubitemid 20232094)
    • (1990) Science , vol.249 , Issue.4966 , pp. 302-303
    • Carter, D.C.1    He, X.-M.2
  • 14
    • 84861234943 scopus 로고    scopus 로고
    • Study of the interaction between 8-azaguanine and bovine serum albumin using optical spectroscopy and molecular modeling methods
    • 10.1007/s00894-011-1069-5
    • Q.L. Gong, X.G. Hu, G.Y. Fang, and X.H. Li Study of the interaction between 8-azaguanine and bovine serum albumin using optical spectroscopy and molecular modeling methods J. Mol. Model. 2011 10.1007/s00894-011-1069-5
    • (2011) J. Mol. Model.
    • Gong, Q.L.1    Hu, X.G.2    Fang, G.Y.3    Li, X.H.4
  • 15
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • DOI 10.1016/j.jasms.2004.05.004, PII S1044030504003393
    • B.X. Huang, H.Y. Kim, and C. Dass Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry J. Am. Soc. Mass Spectrom. 15 2004 1237 1247 (Pubitemid 38970068)
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , Issue.8 , pp. 1237-1247
    • Huang, B.X.1    Kim, H.-Y.2    Dass, C.3
  • 16
    • 85027954912 scopus 로고    scopus 로고
    • Investigation of ternary complex formations of polyacrylic acid with bovine serum albumin in the presence of metal ions by fluorescence and dynamic light scattering measurements
    • M. Karahan, Z. Mustafaeva, and C. Ozeroglu Investigation of ternary complex formations of polyacrylic acid with bovine serum albumin in the presence of metal ions by fluorescence and dynamic light scattering measurements Protein J. 29 2010 336 342
    • (2010) Protein J. , vol.29 , pp. 336-342
    • Karahan, M.1    Mustafaeva, Z.2    Ozeroglu, C.3
  • 17
    • 0019223693 scopus 로고
    • The effect of albumin conformation on the binding of warfarin to human serum albumin. The dependence of the binding of warfarin to human serum albumin on the hydrogen, calcium, and chloride ion concentrations as studied by circular dichroism, fluorescence, and equilibrium dialysis
    • J. Wilting, W.F. van der Giesen, L.H. Janssen, M.M. Weideman, M. Otagiri, and J.H. Perrin The effect of albumin conformation on the binding of warfarin to human serum albumin. The dependence of the binding of warfarin to human serum albumin on the hydrogen, calcium, and chloride ion concentrations as studied by circular dichroism, fluorescence, and equilibrium dialysis J. Biol. Chem. 255 1980 3032 3037 (Pubitemid 10089256)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.7 , pp. 3032-3037
    • Wilting, J.1    Van Der Giesen, W.F.2    Janssen, L.H.M.3
  • 19
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • DOI 10.1016/j.bbagen.2004.10.013, PII S0304416504002843
    • C. Dufour, and O. Dangles Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy Biochim. Biophys. Acta 1721 2005 164 173 (Pubitemid 40093524)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1721 , Issue.1-3 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 20
    • 0031472928 scopus 로고    scopus 로고
    • Species differences of serum albumins: I. Drug binding sites
    • DOI 10.1023/A:1012138604016
    • T. Kosa, T. Maruyama, and M. Otagiri Species differences of serum albumins: I. Drug binding sites Pharm. Res. 14 1997 1607 1612 (Pubitemid 28009214)
    • (1997) Pharmaceutical Research , vol.14 , Issue.11 , pp. 1607-1612
    • Kosa, T.1    Maruyama, T.2    Otagiri, M.3
  • 21
    • 0035210356 scopus 로고    scopus 로고
    • Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: A spectrospic study
    • DOI 10.1046/j.0014-2956.2001.02569.x
    • S. Baroni, M. Mattu, A. Vannini, R. Cipollone, S. Aime, P. Ascenzi, and M. Fasano Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin. A spectroscopic study Eur. J. Biochem. 268 2001 6214 6220 (Pubitemid 33132042)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.23 , pp. 6214-6220
    • Baroni, S.1    Mattu, M.2    Vannini, A.3    Cipollone, R.4    Aime, S.5    Ascenzi, P.6    Fasano, M.7
  • 22
    • 3042610086 scopus 로고    scopus 로고
    • Studies on electrochemical oxidation of azithromycin and its interaction with bovine serum albumin
    • DOI 10.1016/j.bioelechem.2004.03.005, PII S1567539404001768
    • Y. Wu, X. Ji, and S. Hu Studies on electrochemical oxidation of azithromycin and its interaction with bovine serum albumin Bioelectrochemistry 64 2004 91 97 (Pubitemid 38813327)
    • (2004) Bioelectrochemistry , vol.64 , Issue.1 , pp. 91-97
    • Wu, Y.1    Ji, X.2    Hu, S.3
  • 23
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • DOI 10.1007/s00726-003-0016-x
    • C.L. Hawkins, D.I. Pattison, and M.J. Davies Hypochlorite-induced oxidation of amino acids, peptides and proteins Amino Acids 25 2003 259 274 (Pubitemid 38041264)
    • (2003) Amino Acids , vol.25 , Issue.3-4 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 24
    • 0020975006 scopus 로고
    • Covalant attachment of soluble proteins by nonenzymatically glycosylated collagen. Role in the in situ formation of immune complexes
    • M. Brownlee, S. Pongor, and A. Cerami Covalent attachment of soluble proteins by nonenzymatically glycosylated collagen. Role in the in situ formation of immune complexes J. Exp. Med. 158 1983 1739 1744 (Pubitemid 14241385)
    • (1983) Journal of Experimental Medicine , vol.158 , Issue.5 , pp. 1739-1744
    • Brownlee, M.1    Pongor, S.2    Cerami, A.3
  • 25
    • 33847354303 scopus 로고    scopus 로고
    • Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin
    • DOI 10.1134/S0006297907020034
    • M.W. Khan, Z. Rasheed, W.A. Khan, and R. Ali Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin Biochemistry (Mosc) 72 2007 146 152 (Pubitemid 46347479)
    • (2007) Biochemistry (Moscow) , vol.72 , Issue.2 , pp. 146-152
    • Khan, M.W.A.1    Rasheed, Z.2    Khan, W.A.3    Ali, R.4
  • 26
    • 0019467378 scopus 로고
    • Effect of free fatty acid concentration on furosemide binding to human serum albumin
    • P.A. Schwartz, C.T. Rhodes, and D.S. Greene Effect of free fatty acid concentration on furosemide binding to human serum albumin Pharmacology 22 1981 364 370 (Pubitemid 11064202)
    • (1981) Pharmacology , vol.22 , Issue.6 , pp. 364-370
    • Schwartz, P.A.1    Rhodes, C.T.2    Greene, D.S.3
  • 27
    • 0343942487 scopus 로고
    • Indomethacin: A new non-steroid anti-inflammatory agent
    • F.D. Hart, and P.L. Boardman Indomethacin: a new non-steroid anti-inflammatory agent Br. Med. J. 2 1963 965 970
    • (1963) Br. Med. J. , vol.2 , pp. 965-970
    • Hart, F.D.1    Boardman, P.L.2
  • 31
    • 0037805209 scopus 로고    scopus 로고
    • Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry
    • DOI 10.1016/S1044-0305(02)00911-X
    • F. Fenaille, P.A. Guy, and J.C. Tabet Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry J. Am. Soc. Mass Spectrom. 14 2003 215 226 (Pubitemid 36876048)
    • (2003) Journal of the American Society for Mass Spectrometry , vol.14 , Issue.3 , pp. 215-226
    • Fenaille, F.1    Guy, P.A.2    Tabet, J.-C.3
  • 32
    • 0016636179 scopus 로고
    • An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines
    • S.L. Snyder, and P.Z. Sobocinski An improved 2,4,6- trinitrobenzenesulfonic acid method for the determination of amines Anal. Biochem. 64 1975 284 288
    • (1975) Anal. Biochem. , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 33
    • 39449100272 scopus 로고    scopus 로고
    • Structural perturbation of αB-crystallin by zinc and temperature related to its chaperone-like activity
    • DOI 10.1016/j.ijbiomac.2007.10.012, PII S0141813007002644
    • A. Coi, A.M. Bianucci, F. Bonomi, P. Rasmussen, G.M. Mura, and M.L. Ganadu Structural perturbation of alphaB-crystallin by zinc and temperature related to its chaperone-like activity Int. J. Biol. Macromol. 42 2008 229 234 (Pubitemid 351273406)
    • (2008) International Journal of Biological Macromolecules , vol.42 , Issue.3 , pp. 229-234
    • Coi, A.1    Bianucci, A.M.2    Bonomi, F.3    Rasmussen, P.4    Mura, G.M.5    Ganadu, M.L.6
  • 34
    • 33646151957 scopus 로고    scopus 로고
    • Study of protein-ligand binding by fluorescence
    • DOI 10.1002/bmb.2002.494030050089
    • M. Moller, and A. Denicola Study of protein-ligand binding by fluorescence Biochem. Mol. Biol. Educ. 30 2002 309 312 (Pubitemid 44132716)
    • (2002) Biochemistry and Molecular Biology Education , vol.30 , Issue.5 , pp. 309-312
    • Moller, M.1    Denicola, A.2
  • 35
    • 0035834599 scopus 로고    scopus 로고
    • Human serum albumin binding of novel antiretroviral nucleoside derivatives of AZT
    • DOI 10.1006/bbrc.2001.5878
    • M.A. Quevedo, G.N. Moroni, and M.C. Brinon Human serum albumin binding of novel antiretroviral nucleoside derivatives of AZT Biochem. Biophys. Res. Commun. 288 2001 954 960 (Pubitemid 33140976)
    • (2001) Biochemical and Biophysical Research Communications , vol.288 , Issue.4 , pp. 954-960
    • Quevedo, M.A.1    Moroni, G.N.2    Brinon, M.C.3
  • 36
    • 0022291011 scopus 로고
    • Measurement of ligand binding to proteins by fluorescence spectroscopy
    • L.D. Ward Measurement of ligand binding to proteins by fluorescence spectroscopy Methods Enzymol. 117 1985 400 414
    • (1985) Methods Enzymol. , vol.117 , pp. 400-414
    • Ward, L.D.1
  • 37
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • T. Schwede, J. Kopp, N. Guex, and M. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucl. Acids Res. 31 2003 3381 3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 38
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 39
    • 3142746827 scopus 로고    scopus 로고
    • NMR structure determination and calcium binding effects of lipopeptide antibiotic daptomycin
    • L.J. Ball, C.M. Goult, J.A. Donarski, J. Micklefield, and V. Ramesh NMR structure determination and calcium binding effects of lipopeptide antibiotic daptomycin Org. Biomol. Chem. 2 2004 1872 1878
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1872-1878
    • Ball, L.J.1    Goult, C.M.2    Donarski, J.A.3    Micklefield, J.4    Ramesh, V.5
  • 41
    • 0032495131 scopus 로고    scopus 로고
    • Investigation of the interaction between acridine orange and bovine serum albumin
    • X.Z. Feng, Z. Lin, L.J. Yang, C. Wang, and C.L. Bai Investigation of the interaction between acridine orange and bovine serum albumin Talanta 47 1998 1223 1229
    • (1998) Talanta , vol.47 , pp. 1223-1229
    • Feng, X.Z.1    Lin, Z.2    Yang, L.J.3    Wang, C.4    Bai, C.L.5
  • 42
    • 33751390870 scopus 로고
    • HyperChem, Release 2: Molecular modeling for the personal computer
    • B.J. Teppen HyperChem, Release 2: molecular modeling for the personal computer J. Chem. Inf. Comput. Sci. 2 1992 757 759
    • (1992) J. Chem. Inf. Comput. Sci. , vol.2 , pp. 757-759
    • Teppen, B.J.1
  • 44
    • 33750517742 scopus 로고    scopus 로고
    • Efficient molecular surface generation using level-set methods
    • DOI 10.1016/j.jmgm.2006.02.012, PII S109332630600060X
    • T. Can, C.I. Chen, and Y.F. Wang Efficient molecular surface generation using level-set methods J. Mol. Graph. Model. 25 2006 442 454 (Pubitemid 44667586)
    • (2006) Journal of Molecular Graphics and Modelling , vol.25 , Issue.4 , pp. 442-454
    • Can, T.1    Chen, C.-I.2    Wang, Y.-F.3
  • 45
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • M.F. Sanner Python: a programming language for software integration and development J. Mol. Graph. Model. 17 1999 57 61 (Pubitemid 30029318)
    • (1999) Journal of Molecular Graphics and Modelling , vol.17 , Issue.1 , pp. 57-61
    • Sanner, M.F.1
  • 46
    • 34447498860 scopus 로고    scopus 로고
    • Modulating the activity of avian pancreatic lipases by an alkyl chain reacting with an accessible sulfhydryl group
    • DOI 10.1016/j.bbrc.2007.06.115, PII S0006291X07013770
    • A. Fendri, F. Frikha, N. Miled, A. Ben Bacha, and Y. Gargouri Modulating the activity of avian pancreatic lipases by an alkyl chain reacting with an accessible sulfhydryl group Biochem. Biophys. Res. Commun. 360 2007 765 771 (Pubitemid 47082436)
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , Issue.4 , pp. 765-771
    • Fendri, A.1    Frikha, F.2    Miled, N.3    Ben Bacha, A.4    Gargouri, Y.5
  • 47
    • 53849098410 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between nicotinamide and bovine serum albumin
    • H. Xu, Q. Liu, and Y. Wen Spectroscopic studies on the interaction between nicotinamide and bovine serum albumin Spectrochim. Acta A 71 2008 984 988
    • (2008) Spectrochim. Acta A , vol.71 , pp. 984-988
    • Xu, H.1    Liu, Q.2    Wen, Y.3
  • 49
    • 77950520681 scopus 로고    scopus 로고
    • Influence of myristic acid on furosemide binding to bovine serum albumin comparison with furosemide-human serum albumin complex
    • B. Bojko, A. Sulkowska, M. Maciazek-Jurczyk, J. Rownicka, and W.W. Sulkowski Influence of myristic acid on furosemide binding to bovine serum albumin comparison with furosemide-human serum albumin complex Spectrochim. Acta A 76 2010 6 11
    • (2010) Spectrochim. Acta A , vol.76 , pp. 6-11
    • Bojko, B.1    Sulkowska, A.2    MacIazek-Jurczyk, M.3    Rownicka, J.4    Sulkowski, W.W.5
  • 51
    • 41849123136 scopus 로고    scopus 로고
    • A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography
    • L. Zhu, F. Yang, L. Chen, E.J. Meehan, and M. Huang A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography J. Struct. Biol. 162 2008 40 49
    • (2008) J. Struct. Biol. , vol.162 , pp. 40-49
    • Zhu, L.1    Yang, F.2    Chen, L.3    Meehan, E.J.4    Huang, M.5
  • 52
    • 49449116404 scopus 로고    scopus 로고
    • Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes
    • k. Osama, O.K. Abou-Zied, and O.I.K. Al-Shihi Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes J. Am. Chem. Soc. 130 2008 10793 10801
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10793-10801
    • Osama, K.1    Abou-Zied, O.K.2    Al-Shihi, O.I.K.3
  • 53
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 1981 3096 3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 54
    • 70350468866 scopus 로고    scopus 로고
    • In vitro study of DNA interaction with a water-soluble dinitrogen Schiff base
    • N. Shahabadi, S. Kashanian, and F. Darabi In vitro study of DNA interaction with a water-soluble dinitrogen Schiff base DNA Cell Biol. 28 2009 589 596
    • (2009) DNA Cell Biol. , vol.28 , pp. 589-596
    • Shahabadi, N.1    Kashanian, S.2    Darabi, F.3
  • 55
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • M. Cardamone, and N.K. Puri Spectrofluorimetric assessment of the surface hydrophobicity of proteins Biochem. J. 282 1992 589 593
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 56
    • 0036700020 scopus 로고    scopus 로고
    • Quantifying the accessible surface area of protein residues in their local environment
    • U. Samanta, R.P. Bahadur, and P. Chakrabarti Quantifying the accessible surface area of protein residues in their local environment Protein Eng. 15 2002 659 667 (Pubitemid 35175918)
    • (2002) Protein Engineering , vol.15 , Issue.8 , pp. 659-667
    • Samanta, U.1    Bahadur, R.P.2    Chakrabarti, P.3


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