메뉴 건너뛰기




Volumn 8, Issue 2, 2017, Pages 470-477

Probing the Acid-Induced Packing Structure Changes of the Molten Globule Domains of a Protein near Equilibrium Unfolding

Author keywords

[No Author keywords available]

Indexed keywords

BODY FLUIDS; FREE ENERGY; MOLECULAR DYNAMICS; PROTEINS; X RAY SCATTERING;

EID: 85016025156     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/acs.jpclett.6b02722     Document Type: Article
Times cited : (39)

References (50)
  • 1
    • 77957970492 scopus 로고    scopus 로고
    • Dry Molten Globule Intermediates and the Mechanism of Protein Unfolding
    • Baldwin, R. L.; Frieden, C.; Rose, G. D. Dry Molten Globule Intermediates and the Mechanism of Protein Unfolding Proteins: Struct., Funct., Genet. 2010, 78, 2725-2737 10.1002/prot.22803
    • (2010) Proteins: Struct., Funct., Genet. , vol.78 , pp. 2725-2737
    • Baldwin, R.L.1    Frieden, C.2    Rose, G.D.3
  • 2
    • 84897547979 scopus 로고    scopus 로고
    • Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride
    • Jha, S. K.; Marqusee, S. Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride Proc. Natl. Acad. Sci. U. S. A. 2014, 111, 4856-4861 10.1073/pnas.1315453111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 4856-4861
    • Jha, S.K.1    Marqusee, S.2
  • 3
    • 84954159683 scopus 로고    scopus 로고
    • Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein
    • Acharya, N.; Mishra, P.; Jha, S. K. Evidence for Dry Molten Globule-Like Domains in the pH-Induced Equilibrium Folding Intermediate of a Multidomain Protein J. Phys. Chem. Lett. 2016, 7, 173-179 10.1021/acs.jpclett.5b02545
    • (2016) J. Phys. Chem. Lett. , vol.7 , pp. 173-179
    • Acharya, N.1    Mishra, P.2    Jha, S.K.3
  • 4
    • 84873523500 scopus 로고    scopus 로고
    • Packing in molten globules and native states
    • Bhattacharyya, S.; Varadarajan, R. Packing in molten globules and native states Curr. Opin. Struct. Biol. 2013, 23, 11-21 10.1016/j.sbi.2012.10.010
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 11-21
    • Bhattacharyya, S.1    Varadarajan, R.2
  • 5
    • 84906998218 scopus 로고    scopus 로고
    • Dynamic Hydration Shell Restores Kauzmann’s 1959 Explanation of How the Hydrophobic Factor Drives Protein Folding
    • Baldwin, R. L. Dynamic Hydration Shell Restores Kauzmann’s 1959 Explanation of How the Hydrophobic Factor Drives Protein Folding Proc. Natl. Acad. Sci. U. S. A. 2014, 111, 13052-13056 10.1073/pnas.1414556111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 13052-13056
    • Baldwin, R.L.1
  • 6
    • 84873526289 scopus 로고    scopus 로고
    • Molten globules, entropy-driven conformational change and protein folding
    • Baldwin, R. L.; Rose, G. D. Molten globules, entropy-driven conformational change and protein folding Curr. Opin. Struct. Biol. 2013, 23, 4-10 10.1016/j.sbi.2012.11.004
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 4-10
    • Baldwin, R.L.1    Rose, G.D.2
  • 7
    • 84909620043 scopus 로고    scopus 로고
    • Folding pathway of a multidomain protein depends on its topology of domain connectivity
    • Inanami, T.; Terada, T. P.; Sasai, M. Folding pathway of a multidomain protein depends on its topology of domain connectivity Proc. Natl. Acad. Sci. U. S. A. 2014, 111, 15969-15974 10.1073/pnas.1406244111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 15969-15974
    • Inanami, T.1    Terada, T.P.2    Sasai, M.3
  • 8
    • 4644236471 scopus 로고    scopus 로고
    • Hydrophobic Collapse in Multidomain Protein Folding
    • Zhou, R.; Huang, X.; Margulis, C. J.; Berne, B. J. Hydrophobic Collapse in Multidomain Protein Folding Science 2004, 305, 1605-1609 10.1126/science.1101176
    • (2004) Science , vol.305 , pp. 1605-1609
    • Zhou, R.1    Huang, X.2    Margulis, C.J.3    Berne, B.J.4
  • 9
    • 33751257777 scopus 로고    scopus 로고
    • Unfolding and Refolding of Bovine Serum Albumin at Acid pH: Ultrasound and Structural Studies
    • El Kadi, N.; Taulier, N.; Le Huerou, J. Y.; Gindre, M.; Urbach, W.; Nwigwe, I.; Kahn, P. C.; Waks, M. Unfolding and Refolding of Bovine Serum Albumin at Acid pH: Ultrasound and Structural Studies Biophys. J. 2006, 91, 3397-3404 10.1529/biophysj.106.088963
    • (2006) Biophys. J. , vol.91 , pp. 3397-3404
    • El Kadi, N.1    Taulier, N.2    Le Huerou, J.Y.3    Gindre, M.4    Urbach, W.5    Nwigwe, I.6    Kahn, P.C.7    Waks, M.8
  • 10
    • 84856189383 scopus 로고    scopus 로고
    • Spectroscopic studies of protein folding: Linear and nonlinear methods
    • Serrano, A. L.; Waegele, M. M.; Gai, F. Spectroscopic studies of protein folding: Linear and nonlinear methods Protein Sci. 2012, 21, 157-170 10.1002/pro.2006
    • (2012) Protein Sci. , vol.21 , pp. 157-170
    • Serrano, A.L.1    Waegele, M.M.2    Gai, F.3
  • 11
    • 84992580429 scopus 로고    scopus 로고
    • Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments
    • Jeffries, C. M.; Graewert, M. A.; Blanchet, C. E.; Langley, D. B.; Whitten, A. E.; Svergun, D. I. Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments Nat. Protoc. 2016, 11, 2122-2153 10.1038/nprot.2016.113
    • (2016) Nat. Protoc. , vol.11 , pp. 2122-2153
    • Jeffries, C.M.1    Graewert, M.A.2    Blanchet, C.E.3    Langley, D.B.4    Whitten, A.E.5    Svergun, D.I.6
  • 12
    • 84971344156 scopus 로고    scopus 로고
    • Small-angle scattering and 3D structure interpretation
    • Trewhella, J. Small-angle scattering and 3D structure interpretation Curr. Opin. Struct. Biol. 2016, 40, 1-7 10.1016/j.sbi.2016.05.003
    • (2016) Curr. Opin. Struct. Biol. , vol.40 , pp. 1-7
    • Trewhella, J.1
  • 13
    • 84987837599 scopus 로고    scopus 로고
    • Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment
    • Zheng, W.; Borgia, A.; Buholzer, K.; Grishaev, A.; Schuler, B.; Best, R. B. Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment J. Am. Chem. Soc. 2016, 138, 11702-11713 10.1021/jacs.6b05443
    • (2016) J. Am. Chem. Soc. , vol.138 , pp. 11702-11713
    • Zheng, W.1    Borgia, A.2    Buholzer, K.3    Grishaev, A.4    Schuler, B.5    Best, R.B.6
  • 15
    • 34247891557 scopus 로고    scopus 로고
    • Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering
    • Bernadó, P.; Mylonas, E.; Petoukhov, M. V.; Blackledge, M.; Svergun, D. I. Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering J. Am. Chem. Soc. 2007, 129, 5656-5664 10.1021/ja069124n
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernadó, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 16
    • 0032497321 scopus 로고    scopus 로고
    • Protein Denaturation: A Small-Angle X-ray Scattering Study of the Ensemble of Unfolded States of Cytochrome c
    • Segel, D. J.; Fink, A. L.; Hodgson, K. O.; Doniach, S. Protein Denaturation: A Small-Angle X-ray Scattering Study of the Ensemble of Unfolded States of Cytochrome c Biochemistry 1998, 37, 12443-12451 10.1021/bi980535t
    • (1998) Biochemistry , vol.37 , pp. 12443-12451
    • Segel, D.J.1    Fink, A.L.2    Hodgson, K.O.3    Doniach, S.4
  • 17
    • 84862524410 scopus 로고    scopus 로고
    • Modeling Detergent Organization around Aquaporin-0 Using Small-Angle X-ray Scattering
    • Berthaud, A.; Manzi, J.; Pérez, J.; Mangenot, S. Modeling Detergent Organization around Aquaporin-0 Using Small-Angle X-ray Scattering J. Am. Chem. Soc. 2012, 134, 10080-10088 10.1021/ja301667n
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10080-10088
    • Berthaud, A.1    Manzi, J.2    Pérez, J.3    Mangenot, S.4
  • 18
    • 84943581435 scopus 로고    scopus 로고
    • Solution Structure of Apoptotic BAX Oligomer: Oligomerization Likely Precedes Membrane Insertion
    • Sung, T. C.; Li, C. Y.; Lai, Y. C.; Hung, C. L.; Shih, O.; Yeh, Y. Q.; Jeng, U. S.; Chiang, Y. W. Solution Structure of Apoptotic BAX Oligomer: Oligomerization Likely Precedes Membrane Insertion Structure 2015, 23, 1878-1888 10.1016/j.str.2015.07.013
    • (2015) Structure , vol.23 , pp. 1878-1888
    • Sung, T.C.1    Li, C.Y.2    Lai, Y.C.3    Hung, C.L.4    Shih, O.5    Yeh, Y.Q.6    Jeng, U.S.7    Chiang, Y.W.8
  • 19
    • 20044391816 scopus 로고    scopus 로고
    • Albumin: Biochemical Properties and Therapeutic Potential
    • Quinlan, G. J.; Martin, G. S.; Evans, T. W. Albumin: Biochemical Properties and Therapeutic Potential Hepatology 2005, 41, 1211-1219 10.1002/hep.20720
    • (2005) Hepatology , vol.41 , pp. 1211-1219
    • Quinlan, G.J.1    Martin, G.S.2    Evans, T.W.3
  • 21
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • Bujacz, A. Structures of bovine, equine and leporine serum albumin Acta Crystallogr., Sect. D: Biol. Crystallogr. 2012, D68, 1278-1289 10.1107/S0907444912027047
    • (2012) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.D68 , pp. 1278-1289
    • Bujacz, A.1
  • 22
    • 0035041251 scopus 로고    scopus 로고
    • The Conformation of Serum Albumin in Solution: A Combined Phosphorescence Depolarization-Hydrodynamic Modeling Study
    • Ferrer, M. L.; Duchowicz, R.; Carrasco, B.; de la Torre, J. G.; Acuna, A. U. The Conformation of Serum Albumin in Solution: A Combined Phosphorescence Depolarization-Hydrodynamic Modeling Study Biophys. J. 2001, 80, 2422-2430 10.1016/S0006-3495(01)76211-X
    • (2001) Biophys. J. , vol.80 , pp. 2422-2430
    • Ferrer, M.L.1    Duchowicz, R.2    Carrasco, B.3    De La Torre, J.G.4    Acuna, A.U.5
  • 23
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C.; Ho, J. X. Structure of serum albumin Adv. Protein Chem. 1994, 45, 153-204 10.1016/S0065-3233(08)60640-3
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-204
    • Carter, D.C.1    Ho, J.X.2
  • 24
    • 0002829561 scopus 로고    scopus 로고
    • Molten globule-like state of human serum albumin at low pH
    • Muzammil, S.; Kumar, Y.; Tayyab, S. Molten globule-like state of human serum albumin at low pH Eur. J. Biochem. 1999, 266, 26-32 10.1046/j.1432-1327.1999.00810.x
    • (1999) Eur. J. Biochem. , vol.266 , pp. 26-32
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 25
    • 0034602966 scopus 로고    scopus 로고
    • Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH
    • Dockal, M.; Chang, M.; Carter, D. C.; Rüker, F. Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH J. Biol. Chem. 2000, 275, 3042-3050 10.1074/jbc.275.5.3042
    • (2000) J. Biol. Chem. , vol.275 , pp. 3042-3050
    • Dockal, M.1    Chang, M.2    Carter, D.C.3    Rüker, F.4
  • 26
    • 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 Biochem. J. 1986, 236, 307-310 10.1042/bj2360307
    • (1986) Biochem. J. , vol.236 , pp. 307-310
    • Khan, M.Y.1
  • 27
    • 38349169840 scopus 로고    scopus 로고
    • Intrinsic viscosity of bovine serum albumin conformers
    • Curvale, R.; Masuelli, M.; Padilla, A. P. Intrinsic viscosity of bovine serum albumin conformers Int. J. Biol. Macromol. 2008, 42, 133-137 10.1016/j.ijbiomac.2007.10.007
    • (2008) Int. J. Biol. Macromol. , vol.42 , pp. 133-137
    • Curvale, R.1    Masuelli, M.2    Padilla, A.P.3
  • 28
    • 74049110959 scopus 로고    scopus 로고
    • The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small-Angle X-Ray Scattering Study
    • Barbosa, L. R. S.; Ortore, M. G.; Spinozzi, F.; Mariani, P.; Bernstorff, S.; Itri, R. The Importance of Protein-Protein Interactions on the pH-Induced Conformational Changes of Bovine Serum Albumin: A Small-Angle X-Ray Scattering Study Biophys. J. 2010, 98, 147-157 10.1016/j.bpj.2009.09.056
    • (2010) Biophys. J. , vol.98 , pp. 147-157
    • Barbosa, L.R.S.1    Ortore, M.G.2    Spinozzi, F.3    Mariani, P.4    Bernstorff, S.5    Itri, R.6
  • 29
    • 0001176605 scopus 로고
    • Structure and Interparticle Interactions of Bovine Serum Albumin in Solution Studied by Small-Angle Neutron Scattering
    • Bendedouch, D.; Chen, S. H. Structure and Interparticle Interactions of Bovine Serum Albumin in Solution Studied by Small-Angle Neutron Scattering J. Phys. Chem. 1983, 87, 1473-1477 10.1021/j100232a003
    • (1983) J. Phys. Chem. , vol.87 , pp. 1473-1477
    • Bendedouch, D.1    Chen, S.H.2
  • 30
    • 84908191629 scopus 로고    scopus 로고
    • Synchrotron-based small-angle X-ray scattering (SAXS) of proteins in solution
    • Skou, S.; Gillilan, R. E.; Ando, N. Synchrotron-based small-angle X-ray scattering (SAXS) of proteins in solution Nat. Protoc. 2014, 9, 1727-1739 10.1038/nprot.2014.116
    • (2014) Nat. Protoc. , vol.9 , pp. 1727-1739
    • Skou, S.1    Gillilan, R.E.2    Ando, N.3
  • 31
    • 33846591083 scopus 로고    scopus 로고
    • Effective charge of bovine serum albumin determined by electrophoresis NMR
    • Böhme, U.; Scheler, U. Effective charge of bovine serum albumin determined by electrophoresis NMR Chem. Phys. Lett. 2007, 435, 342-345 10.1016/j.cplett.2006.12.068
    • (2007) Chem. Phys. Lett. , vol.435 , pp. 342-345
    • Böhme, U.1    Scheler, U.2
  • 32
    • 84857132923 scopus 로고    scopus 로고
    • How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective
    • Receveur-Bréchot, V.; Durand, D. How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective Curr. Protein Pept. Sci. 2012, 13, 55-75 10.2174/138920312799277901
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 55-75
    • Receveur-Bréchot, V.1    Durand, D.2
  • 33
    • 0034966446 scopus 로고    scopus 로고
    • Heat-induced Unfolding of Neocarzinostatin, a Small All-b Protein Investigated by Small-angle X-ray Scattering
    • Perez, J.; Vachette, P.; Russo, D.; Desmadril, M.; Durand, D. Heat-induced Unfolding of Neocarzinostatin, a Small All-b Protein Investigated by Small-angle X-ray Scattering J. Mol. Biol. 2001, 308, 721-743 10.1006/jmbi.2001.4611
    • (2001) J. Mol. Biol. , vol.308 , pp. 721-743
    • Perez, J.1    Vachette, P.2    Russo, D.3    Desmadril, M.4    Durand, D.5
  • 35
    • 45449117662 scopus 로고    scopus 로고
    • SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach
    • Sinibaldi, R.; Ortore, M. G.; Spinozzi, F.; de Souza Funari, S.; Teixeira, J.; Mariani, P. SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach Eur. Biophys. J. 2008, 37, 673-681 10.1007/s00249-008-0306-z
    • (2008) Eur. Biophys. J. , vol.37 , pp. 673-681
    • Sinibaldi, R.1    Ortore, M.G.2    Spinozzi, F.3    De Souza Funari, S.4    Teixeira, J.5    Mariani, P.6
  • 36
    • 0020110010 scopus 로고
    • Circular dichroic and fluoropolarimetric studies on tryptophyl residues in acid-induced isomerization of bovine plasma albumin
    • Sogami, M.; Era, S.; Nagaoka, S.; Inouye, H. Circular dichroic and fluoropolarimetric studies on tryptophyl residues in acid-induced isomerization of bovine plasma albumin Int. J. Pept. Protein Res. 1982, 19, 263-269 10.1111/j.1399-3011.1982.tb03037.x
    • (1982) Int. J. Pept. Protein Res. , vol.19 , pp. 263-269
    • Sogami, M.1    Era, S.2    Nagaoka, S.3    Inouye, H.4
  • 37
    • 0022365532 scopus 로고
    • Circular dichroic and fluorometric studies on the acid-induced isomerization of bovine plasma albumin--1 -anilino-8-naphthalenesulfonate complex
    • Era, S.; Nagaoka, S.; Sogami, M.; Watari, H.; Akasaka, K.; Kida, K.; Sogami, M.; Yoshida, A. Circular dichroic and fluorometric studies on the acid-induced isomerization of bovine plasma albumin--1-anilino-8-naphthalenesulfonate complex Int. J. Pept. Protein Res. 1985, 26, 575-583 10.1111/j.1399-3011.1985.tb03214.x
    • (1985) Int. J. Pept. Protein Res. , vol.26 , pp. 575-583
    • Era, S.1    Nagaoka, S.2    Sogami, M.3    Watari, H.4    Akasaka, K.5    Kida, K.6    Sogami, M.7    Yoshida, A.8
  • 38
    • 33746075741 scopus 로고    scopus 로고
    • Application of the generalized kinetic Ising model to the kinetics of protein folding
    • Liang, K. K.; Hayashi, M.; Shiu, Y. J.; Mo, Y.; Shao, J.; Yan, Y.; Lin, S. H. Application of the generalized kinetic Ising model to the kinetics of protein folding J. Chin. Chem. Soc. 2003, 50, 335-338 10.1002/jccs.200300050
    • (2003) J. Chin. Chem. Soc. , vol.50 , pp. 335-338
    • Liang, K.K.1    Hayashi, M.2    Shiu, Y.J.3    Mo, Y.4    Shao, J.5    Yan, Y.6    Lin, S.H.7
  • 40
    • 34248327297 scopus 로고    scopus 로고
    • A modified Ising model for the thermodynamic properties of local and global protein folding-unfolding observed by circular dichroism and small-angle X-ray scattering
    • Shiu, Y. J.; Jeng, U.; Su, C.; Huang, Y. S.; Hayashi, M.; Liang, K. K.; Yeh, Y. L.; Lin, S. H. A modified Ising model for the thermodynamic properties of local and global protein folding-unfolding observed by circular dichroism and small-angle X-ray scattering J. Appl. Crystallogr. 2007, 40, s195-s199 10.1107/S0021889807003597
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. s195-s199
    • Shiu, Y.J.1    Jeng, U.2    Su, C.3    Huang, Y.S.4    Hayashi, M.5    Liang, K.K.6    Yeh, Y.L.7    Lin, S.H.8
  • 41
    • 45849135628 scopus 로고    scopus 로고
    • Global and Local Structural Changes of Cytochrome c and Lysozyme Characterized by a Multigroup Unfolding Process
    • Shiu, Y. J.; Jeng, U.; Huang, Y. S.; Lai, Y. H.; Lu, H. F.; Liang, C. T.; Hsu, I.-J.; Su, C. H.; Su, C.; Chao, I.; Su, A. C.; Lin, S. H. Global and Local Structural Changes of Cytochrome c and Lysozyme Characterized by a Multigroup Unfolding Process Biophys. J. 2008, 94, 4828-4836 10.1529/biophysj.107.124214
    • (2008) Biophys. J. , vol.94 , pp. 4828-4836
    • Shiu, Y.J.1    Jeng, U.2    Huang, Y.S.3    Lai, Y.H.4    Lu, H.F.5    Liang, C.T.6    Hsu, I.-J.7    Su, C.H.8    Su, C.9    Chao, I.10    Su, A.C.11    Lin, S.H.12
  • 42
    • 0035010533 scopus 로고    scopus 로고
    • Determination of Domain Structure of Proteins from X-Ray Solution Scattering
    • Svergun, D. I.; Petoukhov, M. V.; Koch, M. H. Determination of Domain Structure of Proteins from X-Ray Solution Scattering Biophys. J. 2001, 80, 2946-2953 10.1016/S0006-3495(01)76260-1
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 44
    • 77950867479 scopus 로고    scopus 로고
    • Monitoring local unfolding of Bovine Serum Albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy
    • Togashi, D. M.; Ryder, A. G.; O’Shaughnessy, D. Monitoring local unfolding of Bovine Serum Albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy J. Fluoresc. 2010, 20, 441-452 10.1007/s10895-009-0566-8
    • (2010) J. Fluoresc. , vol.20 , pp. 441-452
    • Togashi, D.M.1    Ryder, A.G.2    O’Shaughnessy, D.3
  • 45
    • 0027417602 scopus 로고
    • a, values and unfolding of the N-terminus during the N to F transition
    • a, values and unfolding of the N-terminus during the N to F transition Eur. J. Biochem. 1993, 212, 811-817 10.1111/j.1432-1033.1993.tb17722.x
    • (1993) Eur. J. Biochem. , vol.212 , pp. 811-817
    • Sadler, P.J.1    Tucker, A.2
  • 46
    • 84936847118 scopus 로고    scopus 로고
    • Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering
    • Tria, G.; Mertens, H. D. T.; Kachala, M.; Svergun, D. I. Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering IUCrJ 2015, 2, 207-217 10.1107/S205225251500202X
    • (2015) IUCrJ , vol.2 , pp. 207-217
    • Tria, G.1    Mertens, H.D.T.2    Kachala, M.3    Svergun, D.I.4
  • 47
    • 77950603964 scopus 로고    scopus 로고
    • Structure Parameters of Synaptic Vesicles Quantified by Small-Angle X-Ray Scattering
    • Castorph, S.; Riedel, D.; Arleth, L.; Sztucki, M.; Jahn, R.; Holt, M.; Salditt, T. Structure Parameters of Synaptic Vesicles Quantified by Small-Angle X-Ray Scattering Biophys. J. 2010, 98, 1200-1208 10.1016/j.bpj.2009.12.4278
    • (2010) Biophys. J. , vol.98 , pp. 1200-1208
    • Castorph, S.1    Riedel, D.2    Arleth, L.3    Sztucki, M.4    Jahn, R.5    Holt, M.6    Salditt, T.7
  • 49
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev, A.; Bashford, D.; Case, D. A. Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins: Struct., Funct., Genet. 2004, 55, 383-394 10.1002/prot.20033
    • (2004) Proteins: Struct., Funct., Genet. , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.