메뉴 건너뛰기




Volumn 137, Issue 1, 2008, Pages 13-18

Effect of a single point mutation on the stability, residual structure and dynamics in the denatured state of GED: Relevance to self-assembly

Author keywords

Circular dichroism; Denatured state; Fluorescence spectroscopy; GTPase effector domain; Nuclear magnetic resonance

Indexed keywords

DYNAMIN; GUANOSINE TRIPHOSPHATASE; NITROGEN 15; OLIGOMER; POLYPEPTIDE;

EID: 48649096294     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.06.005     Document Type: Article
Times cited : (2)

References (35)
  • 1
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24 (1970) 1-95
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 2
    • 0015890684 scopus 로고
    • Equilibrium and kinetics of the denaturation of a homogeneous human immunoglobulin light chain
    • Rowe E.S., and Tanford C. Equilibrium and kinetics of the denaturation of a homogeneous human immunoglobulin light chain. Biochemistry 12 (1973) 4822-4827
    • (1973) Biochemistry , vol.12 , pp. 4822-4827
    • Rowe, E.S.1    Tanford, C.2
  • 3
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen C.B., and Scheraga H.A. Experimental and theoretical aspects of protein folding. Adv. Protein Chem. 29 (1975) 205-300
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 4
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • Dobson C.M. Experimental investigation of protein folding and misfolding. Methods 34 (2004) 4-14
    • (2004) Methods , vol.34 , pp. 4-14
    • Dobson, C.M.1
  • 5
    • 11244260589 scopus 로고    scopus 로고
    • Monitoring protein folding at atomic resolution
    • Kumar T.K., and Yu C. Monitoring protein folding at atomic resolution. Acc. Chem. Res. 37 (2004) 929-936
    • (2004) Acc. Chem. Res. , vol.37 , pp. 929-936
    • Kumar, T.K.1    Yu, C.2
  • 7
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 8
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: bringing together theory and experiment
    • Dobson C.M., and Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9 (1999) 92-101
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 9
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson H.J., and Wright P.E. Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394 (2005) 299-321
    • (2005) Methods Enzymol. , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 10
    • 0033980811 scopus 로고    scopus 로고
    • Apoflavodoxin (un)folding followed at the residue level by NMR
    • van Mierlo C.P., van den Oever J.M., and Steensma E. Apoflavodoxin (un)folding followed at the residue level by NMR. Protein Sci. 9 (2000) 145-157
    • (2000) Protein Sci. , vol.9 , pp. 145-157
    • van Mierlo, C.P.1    van den Oever, J.M.2    Steensma, E.3
  • 11
    • 0034717064 scopus 로고    scopus 로고
    • Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
    • van Mierlo C.P., and Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J. Biotechnol. 79 (2000) 281-298
    • (2000) J. Biotechnol. , vol.79 , pp. 281-298
    • van Mierlo, C.P.1    Steensma, E.2
  • 12
    • 0029198907 scopus 로고
    • Fluorescence spectroscopy
    • Royer C.A. Fluorescence spectroscopy. Methods Mol. Biol. 40 (1995) 65-89
    • (1995) Methods Mol. Biol. , vol.40 , pp. 65-89
    • Royer, C.A.1
  • 13
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 14
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J.E., and Schmid S.L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374 (1995) 190-192
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 15
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw J.E. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16 (2000) 483-519
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 16
    • 2342473321 scopus 로고    scopus 로고
    • An assembly-incompetent mutant establishes a requirement for dynamin self-assembly in clathrin-mediated endocytosis in vivo
    • Song B.D., Yarar D., and Schmid S.L. An assembly-incompetent mutant establishes a requirement for dynamin self-assembly in clathrin-mediated endocytosis in vivo. Mol. Biol. Cell 15 (2004) 2243-2252
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2243-2252
    • Song, B.D.1    Yarar, D.2    Schmid, S.L.3
  • 17
    • 33645034619 scopus 로고    scopus 로고
    • Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
    • Chugh J., Chatterjee A., Kumar A., Mishra R.K., Mittal R., and Hosur R.V. Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin. FEBS J. 273 (2006) 388-397
    • (2006) FEBS J. , vol.273 , pp. 388-397
    • Chugh, J.1    Chatterjee, A.2    Kumar, A.3    Mishra, R.K.4    Mittal, R.5    Hosur, R.V.6
  • 19
    • 0037077224 scopus 로고    scopus 로고
    • The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum
    • Accola M.A., Huang B., Al M.A., and McNiven M.A. The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum. J. Biol. Chem. 277 (2002) 21829-21835
    • (2002) J. Biol. Chem. , vol.277 , pp. 21829-21835
    • Accola, M.A.1    Huang, B.2    Al, M.A.3    McNiven, M.A.4
  • 20
    • 0033895264 scopus 로고    scopus 로고
    • A monomeric GTPase-negative MxA mutant with antiviral activity
    • Janzen C., Kochs G., and Haller O. A monomeric GTPase-negative MxA mutant with antiviral activity. J. Virol. 74 (2000) 8202-8206
    • (2000) J. Virol. , vol.74 , pp. 8202-8206
    • Janzen, C.1    Kochs, G.2    Haller, O.3
  • 21
    • 0037159208 scopus 로고    scopus 로고
    • Molecular hinges in protein folding: the urea-denatured state of apomyoglobin
    • Schwarzinger S., Wright P.E., and Dyson H.J. Molecular hinges in protein folding: the urea-denatured state of apomyoglobin. Biochemistry 41 (2002) 12681-12686
    • (2002) Biochemistry , vol.41 , pp. 12681-12686
    • Schwarzinger, S.1    Wright, P.E.2    Dyson, H.J.3
  • 22
    • 48249102645 scopus 로고    scopus 로고
    • J. Chugh, S. Sharma, R.V. Hosur, NMR insights into a megadalton-sized protein self-assembly, Protein Sci. in press, doi:10.1110/ps.035840.108.
    • J. Chugh, S. Sharma, R.V. Hosur, NMR insights into a megadalton-sized protein self-assembly, Protein Sci. in press, doi:10.1110/ps.035840.108.
  • 23
    • 35448958168 scopus 로고    scopus 로고
    • Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of dynamin
    • Chugh J., Sharma S., and Hosur R.V. Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of dynamin. Biochemistry 46 (2007) 11819-11832
    • (2007) Biochemistry , vol.46 , pp. 11819-11832
    • Chugh, J.1    Sharma, S.2    Hosur, R.V.3
  • 24
    • 3042755600 scopus 로고    scopus 로고
    • Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants
    • Murugan R., and Mazumdar S. Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: effect of temperature and low concentrations of denaturants. J. Biol. Inorg. Chem. 9 (2004) 477-488
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 477-488
    • Murugan, R.1    Mazumdar, S.2
  • 25
    • 1042265192 scopus 로고    scopus 로고
    • Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study
    • Patel S., Chaffotte A.F., Goubard F., and Pauthe E. Urea-induced sequential unfolding of fibronectin: a fluorescence spectroscopy and circular dichroism study. Biochemistry 43 (2004) 1724-1735
    • (2004) Biochemistry , vol.43 , pp. 1724-1735
    • Patel, S.1    Chaffotte, A.F.2    Goubard, F.3    Pauthe, E.4
  • 27
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
    • Privalov P.L., and Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86 (1974) 665-684
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 28
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 29
    • 27744533599 scopus 로고    scopus 로고
    • Comparison of guanidine hydrochloride (GdnHCl) and urea denaturation on inactivation and unfolding of human placental cystatin (HPC)
    • Rashid F., Sharma S., and Bano B. Comparison of guanidine hydrochloride (GdnHCl) and urea denaturation on inactivation and unfolding of human placental cystatin (HPC). Protein J. 24 (2005) 283-292
    • (2005) Protein J. , vol.24 , pp. 283-292
    • Rashid, F.1    Sharma, S.2    Bano, B.3
  • 30
    • 0037174849 scopus 로고    scopus 로고
    • Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters
    • Kamal J.K., Nazeerunnisa M., and Behere D.V. Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters. J. Biol. Chem. 277 (2002) 40717-40721
    • (2002) J. Biol. Chem. , vol.277 , pp. 40717-40721
    • Kamal, J.K.1    Nazeerunnisa, M.2    Behere, D.V.3
  • 31
    • 0037162406 scopus 로고    scopus 로고
    • Thermal and conformational stability of seed coat soybean peroxidase
    • Kamal J.K., and Behere D.V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 41 (2002) 9034-9042
    • (2002) Biochemistry , vol.41 , pp. 9034-9042
    • Kamal, J.K.1    Behere, D.V.2
  • 32
    • 0027402748 scopus 로고
    • A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies
    • Pappa H.S., and Cass A.E. A step towards understanding the folding mechanism of horseradish peroxidase. Tryptophan fluorescence and circular dichroism equilibrium studies. Eur. J. Biochem. 212 (1993) 227-235
    • (1993) Eur. J. Biochem. , vol.212 , pp. 227-235
    • Pappa, H.S.1    Cass, A.E.2
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson H.J., and Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 104 (2004) 3607-3622
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.