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Volumn 115, Issue 29, 2011, Pages 9022-9032

New insight in protein-ligand interactions. 2. Stability and properties of two mutant forms of the d-galactose/D-glucose-binding protein from E. coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DISSOCIATION; ESCHERICHIA COLI; GLUCOSE SENSORS; LIGANDS; PROTEINS; STABILITY;

EID: 79960643729     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp204555h     Document Type: Article
Times cited : (11)

References (50)
  • 1
    • 62449126447 scopus 로고    scopus 로고
    • Glucose sensors: A review of current and emerging technology
    • Oliver, N. S.; Toumazou, C.; Cass, A. E.; Johnston, D. G. Glucose sensors: a review of current and emerging technology Diabet Med. 2009, 26 (3) 197-210
    • (2009) Diabet Med. , vol.26 , Issue.3 , pp. 197-210
    • Oliver, N.S.1    Toumazou, C.2    Cass, A.E.3    Johnston, D.G.4
  • 2
    • 73749083481 scopus 로고    scopus 로고
    • Global estimates of the prevalence of diabetes for 2010 and 2030
    • Shaw, J. E.; Sicree, R. A.; Zimmet, P. Z. Global estimates of the prevalence of diabetes for 2010 and 2030 Diabetes Res. Clin. Pract. 2010, 87 (1) 4-14
    • (2010) Diabetes Res. Clin. Pract. , vol.87 , Issue.1 , pp. 4-14
    • Shaw, J.E.1    Sicree, R.A.2    Zimmet, P.Z.3
  • 3
    • 0038270085 scopus 로고    scopus 로고
    • Toward the improvement of diabetes treatment: Recent developments in technical support
    • Wojcicki, J. M.; Ladyzynski, P. Toward the improvement of diabetes treatment: recent developments in technical support J. Artif. Organs 2003, 6 (2) 73-87 (Pubitemid 36829948)
    • (2003) Journal of Artificial Organs , vol.6 , Issue.2 , pp. 73-87
    • Wojcicki, J.M.1    Ladyzynski, P.2
  • 4
    • 44349148840 scopus 로고    scopus 로고
    • Current development in non-invasive glucose monitoring
    • DOI 10.1016/j.medengphy.2007.06.003, PII S1350453307001178
    • Ferrante do Amaral, C. E.; Wolf, B. Current development in non-invasive glucose monitoring Med. Eng. Phys. 2008, 30 (5) 541-9 (Pubitemid 351749846)
    • (2008) Medical Engineering and Physics , vol.30 , Issue.5 , pp. 541-549
    • Ferrante Do Amaral, C.E.1    Wolf, B.2
  • 5
    • 0033086405 scopus 로고    scopus 로고
    • Issues and implications in the selection of blood glucose monitoring technologies
    • Ervin, K. R.; Kiser, E. J. Issues and implications in the selection of blood glucose monitoring technologies Diabetes Technol. Ther. 1999, 1 (1) 3-11
    • (1999) Diabetes Technol. Ther. , vol.1 , Issue.1 , pp. 3-11
    • Ervin, K.R.1    Kiser, E.J.2
  • 6
    • 34247134514 scopus 로고    scopus 로고
    • Non-invasive glucose monitoring: Assessment of technologies and devices according to quantitative criteria
    • DOI 10.1016/j.diabres.2006.10.027, PII S0168822706004931
    • Tura, A.; Maran, A.; Pacini, G. Non-invasive glucose monitoring: assessment of technologies and devices according to quantitative criteria Diabetes Res. Clin. Pract. 2007, 77 (1) 16-40 (Pubitemid 46590478)
    • (2007) Diabetes Research and Clinical Practice , vol.77 , Issue.1 , pp. 16-40
    • Tura, A.1    Maran, A.2    Pacini, G.3
  • 7
    • 4344679385 scopus 로고    scopus 로고
    • Fluorescence glucose detection: Advances toward the ideal in vivo biosensor
    • Moschou, E. A.; Sharma, B. V.; Deo, S. K.; Daunert, S. Fluorescence glucose detection: advances toward the ideal in vivo biosensor J. Fluoresc. 2004, 14 (5) 535-47
    • (2004) J. Fluoresc. , vol.14 , Issue.5 , pp. 535-547
    • Moschou, E.A.1    Sharma, B.V.2    Deo, S.K.3    Daunert, S.4
  • 8
    • 77955533214 scopus 로고    scopus 로고
    • On the design of low-cost fluorescent protein biosensors
    • Tolosa, L. On the design of low-cost fluorescent protein biosensors Adv. Biochem. Eng. Biotechnol. 2009, 116, 143-57
    • (2009) Adv. Biochem. Eng. Biotechnol. , vol.116 , pp. 143-157
    • Tolosa, L.1
  • 9
    • 0030606240 scopus 로고    scopus 로고
    • Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins
    • DOI 10.1006/jmbi.1996.0645
    • Shilton, B. H.; Flocco, M. M.; Nilsson, M.; Mowbray, S. L. Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins J. Mol. Biol. 1996, 264 (2) 350-63 (Pubitemid 26402702)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.2 , pp. 350-363
    • Shilton, B.H.1    Flocco, M.M.2    Nilsson, M.3    Mowbray, S.L.4
  • 10
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R.; Saier, M. H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria Microbiol. Rev. 1993, 57 (2) 320-46 (Pubitemid 23170095)
    • (1993) Microbiological Reviews , vol.57 , Issue.2 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 11
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • DOI 10.1016/j.sbi.2004.07.004, PII S0959440X04001113
    • Dwyer, M. A.; Hellinga, H. W. Periplasmic binding proteins: a versatile superfamily for protein engineering Curr. Opin. Struct. Biol. 2004, 14 (4) 495-504 (Pubitemid 39094355)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.4 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 12
    • 34249781722 scopus 로고    scopus 로고
    • Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures
    • DOI 10.1110/ps.062707807
    • Borrok, M. J.; Kiessling, L. L.; Forest, K. T. Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures Protein Sci. 2007, 16 (6) 1032-41 (Pubitemid 46849213)
    • (2007) Protein Science , vol.16 , Issue.6 , pp. 1032-1041
    • Borrok, M.J.1    Kiessling, L.L.2    Forest, K.T.3
  • 13
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N. K.; Vyas, M. N.; Quiocho, F. A. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein Science 1988, 242 (4883) 1290-5 (Pubitemid 19008057)
    • (1988) Science , vol.242 , Issue.4883 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 14
    • 0025794052 scopus 로고
    • Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose: Structural and functional similarity
    • Vyas, N. K.; Vyas, M. N.; Quiocho, F. A. Comparison of the periplasmic receptors for L-arabinose, D-glucose/D-galactose, and D-ribose. Structural and Functional Similarity J. Biol. Chem. 1991, 266 (8) 5226-37 (Pubitemid 21909480)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.8 , pp. 5226-5237
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 15
    • 0028244277 scopus 로고
    • Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D- galactose
    • DOI 10.1021/bi00182a003
    • Vyas, M. N.; Vyas, N. K.; Quiocho, F. A. Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose Biochemistry 1994, 33 (16) 4762-8 (Pubitemid 24158424)
    • (1994) Biochemistry , vol.33 , Issue.16 , pp. 4762-4768
    • Vyas, M.N.1    Vyas, N.K.2    Quiocho, F.A.3
  • 17
    • 26844548373 scopus 로고    scopus 로고
    • Monitoring glycemic control: The importance of self-monitoring of blood glucose
    • DOI 10.1016/j.amjmed.2005.07.052, PII S0002934305006649
    • Renard, E. Monitoring glycemic control: the importance of self-monitoring of blood glucose Am. J. Med. 2005, 118 (Suppl 9A) 12S-19S (Pubitemid 41446938)
    • (2005) American Journal of Medicine , vol.118 , Issue.9 SUPPL.
    • Renard, E.1
  • 18
    • 77954217602 scopus 로고    scopus 로고
    • The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation
    • Turoverov, K. K.; Kuznetsova, I. M.; Uversky, V. N. The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation Prog. Biophys. Mol. Biol. 2010, 102 (2-3) 73-84
    • (2010) Prog. Biophys. Mol. Biol. , vol.102 , Issue.2-3 , pp. 73-84
    • Turoverov, K.K.1    Kuznetsova, I.M.2    Uversky, V.N.3
  • 19
    • 0020608207 scopus 로고
    • Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning
    • Harayama, S.; Bollinger, J.; Iino, T.; Hazelbauer, G. L. Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning J. Bacteriol. 1983, 153 (1) 408-15 (Pubitemid 13119567)
    • (1983) Journal of Bacteriology , vol.153 , Issue.1 , pp. 408-415
    • Harayama, S.1    Bollinger, J.2    Iino, T.3    Hazelbauer, G.L.4
  • 20
    • 0014413977 scopus 로고
    • Transport systems for galactose and galactosides in Escherichia coli. II. Substrate and inducer specificities
    • Rotman, B.; Ganesan, A. K.; Guzman, R. Transport systems for galactose and galactosides in Escherichia coli. II. Substrate and inducer specificities J. Mol. Biol. 1968, 36 (2) 247-60
    • (1968) J. Mol. Biol. , vol.36 , Issue.2 , pp. 247-260
    • Rotman, B.1    Ganesan, A.K.2    Guzman, R.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227 (5259) 680-5
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 85044704833 scopus 로고    scopus 로고
    • A complex of apparatus and programs for the measurement of spectral, polarization and kinetic characteristics of fluorescence in solution
    • Turoverov, K. K.; Biktashev, A. G.; Dorofeiuk, A. V.; Kuznetsova, I. M. [A complex of apparatus and programs for the measurement of spectral, polarization and kinetic characteristics of fluorescence in solution] Tsitologiia 1998, 40 (8-9) 806-17
    • (1998) Tsitologiia , vol.40 , Issue.8-9 , pp. 806-817
    • Turoverov, K.K.1    Biktashev, A.G.2    Dorofeiuk, A.V.3    Kuznetsova, I.M.4
  • 24
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. The use of fluorescence methods to monitor unfolding transitions in proteins Biophys. J. 1994, 66 (2 Pt 1) 482-501 (Pubitemid 24058467)
    • (1994) Biophysical Journal , vol.66 , Issue.2 , pp. 482-501
    • Eftink, M.R.1
  • 27
    • 2442452683 scopus 로고    scopus 로고
    • Use of the phase diagram method to analyze the protein unfolding-refolding reactions: Fishing out the "invisible" intermediates
    • DOI 10.1021/pr034094y
    • Kuznetsova, I. M.; Turoverov, K. K.; Uversky, V. N. Use of the phase diagram method to analyze the protein unfolding-refolding reactions: fishing out the "invisible" intermediates J. Proteome Res. 2004, 3 (3) 485-94 (Pubitemid 39207353)
    • (2004) Journal of Proteome Research , vol.3 , Issue.3 , pp. 485-494
    • Kuznetsova, I.M.1    Turoverov, K.K.2    Uversky, V.N.3
  • 28
    • 2442572168 scopus 로고    scopus 로고
    • Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence
    • DOI 10.1021/bi0359325
    • Stepanenko, O. V.; Kuznetsova, I. M.; Turoverov, K. K.; Huang, C.; Wang, C. C. Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence Biochemistry 2004, 43 (18) 5296-303 (Pubitemid 38620921)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5296-5303
    • Stepanenko, O.V.1    Kuznetsova, I.M.2    Turoverov, K.K.3    Huang, C.4    Wang, C.-C.5
  • 30
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M. R. Fluorescence techniques for studying protein structure Methods Biochem. Anal. 1991, 35, 127-205
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 32
    • 10044280728 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy mutations in α-tropomyosin, Asp175Asn and Glut180Gly, on the thermal unfolding of actin-bound tropomyosin
    • DOI 10.1529/biophysj.104.048793
    • Kremneva, E.; Boussouf, S.; Nikolaeva, O.; Maytum, R.; Geeves, M. A.; Levitsky, D. I.; Levitsky, D. I.; Rostkova, E. V.; Orlov, V. N.; Nikolaeva, O. P.; Moiseeva, L. N.; Teplova, M. V.; Gusev, N. B. Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin Biophys. J. 2004, 87 (6) 3922-33 (Pubitemid 39602898)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 3922-3933
    • Kremneva, E.1    Boussouf, S.2    Nikolaeva, O.3    Maytum, R.4    Geeves, M.A.5    Levitsky, D.I.6
  • 35
    • 42049123241 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation
    • Markov, D. I.; Pivovarova, A. V.; Chernik, I. S.; Gusev, N. B.; Levitsky, D. I. Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation FEBS Lett. 2008, 582 (10) 1407-12
    • (2008) FEBS Lett. , vol.582 , Issue.10 , pp. 1407-1412
    • Markov, D.I.1    Pivovarova, A.V.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 36
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov, P. L.; Potekhin, S. A. Scanning microcalorimetry in studying temperature-induced changes in proteins Methods Enzymol. 1986, 131, 4-51 (Pubitemid 16002194)
    • (1986) Methods in Enzymology , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 37
    • 0017836908 scopus 로고
    • Statisical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems
    • DOI 10.1002/bip.1978.360170212
    • Freire, E.; Biltonen, R. L. Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems Biopolymers 1978, 17, 463-479 (Pubitemid 8317016)
    • (1978) Biopolymers , vol.17 , Issue.2 , pp. 463-479
    • Freire, E.1    Biltonen, R.L.2
  • 38
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W.; Glockner, J. Estimation of globular protein secondary structure from circular dichroism Biochemistry 1981, 20 (1) 33-7
    • (1981) Biochemistry , vol.20 , Issue.1 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 42
    • 0035814136 scopus 로고    scopus 로고
    • Partially folded conformations in the folding pathway of bovine carbonic anhydrase II: A fluorescence spectroscopic analysis
    • Bushmarina, N. A.; Kuznetsova, I. M.; Biktashev, A. G.; Turoverov, K. K.; Uversky, V. N. Partially folded conformations in the folding pathway of bovine carbonic anhydrase II: a fluorescence spectroscopic analysis ChemBioChem 2001, 2 (11) 813-21 (Pubitemid 33722673)
    • (2001) ChemBioChem , vol.2 , Issue.11 , pp. 813-821
    • Turoverov, K.K.1
  • 43
    • 36348956239 scopus 로고    scopus 로고
    • A strategic fluorescence labeling of D-galactose/D-glucose-binding protein from Escherichia coli helps to shed light on the protein structural stability and dynamics
    • DOI 10.1021/pr070439r
    • Scognamiglio, V.; Scire, A.; Aurilia, V.; Staiano, M.; Crescenzo, R.; Palmucci, C.; Bertoli, E.; Rossi, M.; Tanfani, F.; D'Auria, S. A strategic fluorescence labelling of D-galactose/D-glucose-binding protein from E. coli helps to shed light on the protein structural stability and dynamics J. Proteome Res. 2007, 6 (11) 4119-4126 (Pubitemid 350158490)
    • (2007) Journal of Proteome Research , vol.6 , Issue.11 , pp. 4119-4126
    • Scognamiglio, V.1    Scire, A.2    Aurilia, V.3    Staiano, M.4    Crescenzo, R.5    Palmucci, C.6    Bertoli, E.7    Rossi, M.8    Tanfani, F.9    D'Auria, S.10
  • 44
    • 33644945086 scopus 로고    scopus 로고
    • Thermal unfolding of smooth muscle and nonmuscle tropomyosin alpha-homodimers with alternatively spliced exons
    • Kremneva, E.; Nikolaeva, O.; Maytum, R.; Arutyunyan, A. M.; Kleimenov, S. Y.; Geeves, M. A.; Levitsky, D. I. Thermal unfolding of smooth muscle and nonmuscle tropomyosin alpha-homodimers with alternatively spliced exons FEBS J. 2006, 273 (3) 588-600
    • (2006) FEBS J. , vol.273 , Issue.3 , pp. 588-600
    • Kremneva, E.1    Nikolaeva, O.2    Maytum, R.3    Arutyunyan, A.M.4    Kleimenov, S.Y.5    Geeves, M.A.6    Levitsky, D.I.7
  • 45
  • 46
    • 0029080918 scopus 로고
    • Interaction of smooth muscle calponin with phospholipids
    • Bogatcheva, N. V.; Gusev, N. B. Interaction of smooth muscle calponin with phospholipids FEBS Lett. 1995, 371 (2) 123-6
    • (1995) FEBS Lett. , vol.371 , Issue.2 , pp. 123-126
    • Bogatcheva, N.V.1    Gusev, N.B.2
  • 47
    • 35648996014 scopus 로고    scopus 로고
    • Engineering and rapid selection of a low-affinity glucose/galactose- binding protein for a glucose biosensor
    • DOI 10.1110/ps.073119507
    • Amiss, T. J.; Sherman, D. B.; Nycz, C. M.; Andaluz, S. A.; Pitner, J. B. Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor Protein Sci. 2007, 16 (11) 2350-9 (Pubitemid 350036742)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2350-2359
    • Amiss, T.J.1    Sherman, D.B.2    Nycz, C.M.3    Andaluz, S.A.4    Pitner, J.B.5
  • 50
    • 0030815133 scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A.; Bacon, D. J. Raster3D: Photorealistic molecular graphics Methods Enzymol. 1977, 277, 505-524
    • (1977) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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