메뉴 건너뛰기




Volumn 118, Issue 15, 2014, Pages 4088-4097

The effect of intrachain electrostatic repulsion on conformational disorder and dynamics of the sic1 protein

Author keywords

[No Author keywords available]

Indexed keywords

CHAINS; ELECTROSTATICS; FLUORESCENCE SPECTROSCOPY; HYDRODYNAMICS; SPECTROSCOPIC ANALYSIS;

EID: 84898957660     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp500776v     Document Type: Article
Times cited : (45)

References (57)
  • 1
    • 84866463338 scopus 로고    scopus 로고
    • Structural Biology. Versatility from Protein Disorder
    • Babu, M. M.; Kriwacki, R. W.; Pappu, R. V. Structural Biology. Versatility from Protein Disorder Science 2012, 337 (6101) 1460-1
    • (2012) Science , vol.337 , Issue.6101 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3
  • 3
    • 0029662315 scopus 로고    scopus 로고
    • Structural Studies of p21Waf1/Cip1/Sdi1 in the Free and Cdk2-Bound State: Conformational Disorder Mediates Binding Diversity
    • Kriwacki, R. W.; Hengst, L.; Tennant, L.; Reed, S. I.; Wright, P. E. Structural Studies of p21Waf1/Cip1/Sdi1 in the Free and Cdk2-Bound State: Conformational Disorder Mediates Binding Diversity Proc. Natl. Acad. Sci. U. S. A. 1996, 93 (21) 11504-9
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.21 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 4
    • 63649163700 scopus 로고    scopus 로고
    • How Accurate Are Polymer Models in the Analysis of Förster Resonance Energy Transfer Experiments on Proteins?
    • O'Brien, E. P.; Morrison, G.; Brooks, B. R.; Thirumalai, D. How Accurate Are Polymer Models in the Analysis of Förster Resonance Energy Transfer Experiments on Proteins? J. Chem. Phys. 2009, 130 (12) 124903
    • (2009) J. Chem. Phys. , vol.130 , Issue.12 , pp. 124903
    • O'Brien, E.P.1    Morrison, G.2    Brooks, B.R.3    Thirumalai, D.4
  • 5
    • 57149116929 scopus 로고    scopus 로고
    • Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
    • Gsponer, J.; Futschik, M. E.; Teichmann, S. A.; Babu, M. M. Tight Regulation of Unstructured Proteins: from Transcript Synthesis to Protein Degradation Science 2008, 322 (5906) 1365-8
    • (2008) Science , vol.322 , Issue.5906 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 8
    • 0035969559 scopus 로고    scopus 로고
    • Multisite Phosphorylation of a CDK Inhibitor Sets a Threshold for the Onset of DNA Replication
    • Nash, P.; Tang, X.; Orlicky, S.; Chen, Q.; Gertler, F. B.; Mendenhall, M. D.; Sicheri, F.; Pawson, T.; Tyers, M. Multisite Phosphorylation of a CDK Inhibitor Sets a Threshold for the Onset of DNA Replication Nature 2001, 414 (6863) 514-21
    • (2001) Nature , vol.414 , Issue.6863 , pp. 514-521
    • Nash, P.1    Tang, X.2    Orlicky, S.3    Chen, Q.4    Gertler, F.B.5    Mendenhall, M.D.6    Sicheri, F.7    Pawson, T.8    Tyers, M.9
  • 9
    • 84857698871 scopus 로고    scopus 로고
    • Composite Low Affinity Interactions Dictate Recognition of the Cyclin-Dependent Kinase Inhibitor Sic1 by the SCFCdc4 Ubiquitin Ligase
    • Tang, X.; Orlicky, S.; Mittag, T.; Csizmok, V.; Pawson, T.; Forman-Kay, J. D.; Sicheri, F.; Tyers, M. Composite Low Affinity Interactions Dictate Recognition of the Cyclin-Dependent Kinase Inhibitor Sic1 by the SCFCdc4 Ubiquitin Ligase Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (9) 3287-92
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.9 , pp. 3287-3292
    • Tang, X.1    Orlicky, S.2    Mittag, T.3    Csizmok, V.4    Pawson, T.5    Forman-Kay, J.D.6    Sicheri, F.7    Tyers, M.8
  • 10
    • 0037462424 scopus 로고    scopus 로고
    • Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase
    • Orlicky, S.; Tang, X.; Willems, A.; Tyers, M.; Sicheri, F. Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase Cell 2003, 112 (2) 243-56
    • (2003) Cell , vol.112 , Issue.2 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 12
    • 34547462095 scopus 로고    scopus 로고
    • Polyelectrostatic Interactions of Disordered Ligands Suggest a Physical Basis for Ultrasensitivity
    • Borg, M.; Mittag, T.; Pawson, T.; Tyers, M.; Forman-Kay, J. D.; Chan, H. S. Polyelectrostatic Interactions of Disordered Ligands Suggest a Physical Basis for Ultrasensitivity Proc. Natl. Acad. Sci. U. S. A. 2007, 104 (23) 9650-5
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.23 , pp. 9650-9655
    • Borg, M.1    Mittag, T.2    Pawson, T.3    Tyers, M.4    Forman-Kay, J.D.5    Chan, H.S.6
  • 13
    • 77951631601 scopus 로고    scopus 로고
    • Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an SCF Ubiquitin Ligase
    • Mittag, T.; Marsh, J.; Grishaev, A.; Orlicky, S.; Lin, H.; Sicheri, F.; Tyers, M.; Forman-Kay, J. D. Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an SCF Ubiquitin Ligase Structure 2010, 18 (4) 494-506
    • (2010) Structure , vol.18 , Issue.4 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4    Lin, H.5    Sicheri, F.6    Tyers, M.7    Forman-Kay, J.D.8
  • 15
    • 33746675190 scopus 로고    scopus 로고
    • Single-Molecule Experiments in Biological Physics: Methods and Applications
    • Ritort, F. Single-Molecule Experiments in Biological Physics: Methods and Applications J. Phys.: Condens. Matter 2006, 18 (32) R531-83
    • (2006) J. Phys.: Condens. Matter , vol.18 , Issue.32 , pp. 531-583
    • Ritort, F.1
  • 17
    • 39149087014 scopus 로고    scopus 로고
    • Protein Folding Studied by Single-Molecule FRET
    • Schuler, B.; Eaton, W. A. Protein Folding Studied by Single-Molecule FRET Curr. Opin. Struct. Biol. 2008, 18 (1) 16-26
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , Issue.1 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 18
    • 76649114676 scopus 로고    scopus 로고
    • Protein Dynamics and Conformational Disorder in Molecular Recognition
    • Mittag, T.; Kay, L. E.; Forman-Kay, J. D. Protein Dynamics and Conformational Disorder in Molecular Recognition J. Mol. Recognit. 2010, 23 (2) 105-16
    • (2010) J. Mol. Recognit. , vol.23 , Issue.2 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 19
    • 79959946164 scopus 로고    scopus 로고
    • Visualization of the Nanospring Dynamics of the Iκbα Ankyrin Repeat Domain in Real Time
    • Lamboy, J. A.; Kim, H.; Lee, K. S.; Ha, T.; Komives, E. A. Visualization of the Nanospring Dynamics of the Iκbα Ankyrin Repeat Domain in Real Time Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (25) 10178-83
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.25 , pp. 10178-10183
    • Lamboy, J.A.1    Kim, H.2    Lee, K.S.3    Ha, T.4    Komives, E.A.5
  • 20
    • 77957037991 scopus 로고    scopus 로고
    • Single-Molecule Fluorescence Studies of Intrinsically Disordered Proteins
    • Ferreon, A. C.; Moran, C. R.; Gambin, Y.; Deniz, A. A. Single-Molecule Fluorescence Studies of Intrinsically Disordered Proteins Methods Enzymol. 2010, 472, 179-204
    • (2010) Methods Enzymol. , vol.472 , pp. 179-204
    • Ferreon, A.C.1    Moran, C.R.2    Gambin, Y.3    Deniz, A.A.4
  • 21
    • 0037126290 scopus 로고    scopus 로고
    • Probing the Free-Energy Surface for Protein Folding with Single-Molecule Fluorescence Spectroscopy
    • Schuler, B.; Lipman, E. A.; Eaton, W. A. Probing the Free-Energy Surface for Protein Folding with Single-Molecule Fluorescence Spectroscopy Nature 2002, 419 (6908) 743-7
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 22
    • 70349524994 scopus 로고    scopus 로고
    • Direct Observation of Barrier-Limited Folding of BBL by Single-Molecule Fluorescence Resonance Energy Transfer
    • Huang, F.; Ying, L.; Fersht, A. R. Direct Observation of Barrier-Limited Folding of BBL by Single-Molecule Fluorescence Resonance Energy Transfer Proc. Natl. Acad. Sci. U. S. A. 2009, 106 (38) 16239-44
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.38 , pp. 16239-16244
    • Huang, F.1    Ying, L.2    Fersht, A.R.3
  • 23
    • 78249280020 scopus 로고    scopus 로고
    • Single Molecule Characterization of Alpha-Synuclein in Aggregation-Prone States
    • Trexler, A. J.; Rhoades, E. Single Molecule Characterization of Alpha-Synuclein in Aggregation-Prone States Biophys. J. 2010, 99 (9) 3048-55
    • (2010) Biophys. J. , vol.99 , Issue.9 , pp. 3048-3055
    • Trexler, A.J.1    Rhoades, E.2
  • 24
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of Alpha-Synuclein Binding and Conformational Switching Probed by Single-Molecule Fluorescence
    • Ferreon, A. C.; Gambin, Y.; Lemke, E. A.; Deniz, A. A. Interplay of Alpha-Synuclein Binding and Conformational Switching Probed by Single-Molecule Fluorescence Proc. Natl. Acad. Sci. U. S. A. 2009, 106 (14) 5645-50
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.14 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 25
    • 80053353760 scopus 로고    scopus 로고
    • Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153
    • Milles, S.; Lemke, E. A. Single Molecule Study of the Intrinsically Disordered FG-Repeat Nucleoporin 153 Biophys. J. 2011, 101 (7) 1710-9
    • (2011) Biophys. J. , vol.101 , Issue.7 , pp. 1710-1719
    • Milles, S.1    Lemke, E.A.2
  • 26
    • 33847324863 scopus 로고    scopus 로고
    • A Natively Unfolded Yeast Prion Monomer Adopts an Ensemble of Collapsed and Rapidly Fluctuating Structures
    • Mukhopadhyay, S.; Krishnan, R.; Lemke, E. A.; Lindquist, S.; Deniz, A. A. A Natively Unfolded Yeast Prion Monomer Adopts an Ensemble of Collapsed and Rapidly Fluctuating Structures Proc. Natl. Acad. Sci. U. S. A. 2007, 104 (8) 2649-54
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.8 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 28
    • 79960646350 scopus 로고    scopus 로고
    • FRET-FCS Detection of Intralobe Dynamics in Calmodulin
    • Price, E. S.; Aleksiejew, M.; Johnson, C. K. FRET-FCS Detection of Intralobe Dynamics in Calmodulin J. Phys. Chem. B 2011, 115 (29) 9320-6
    • (2011) J. Phys. Chem. B , vol.115 , Issue.29 , pp. 9320-9326
    • Price, E.S.1    Aleksiejew, M.2    Johnson, C.K.3
  • 29
    • 77952335311 scopus 로고    scopus 로고
    • Net Charge per Residue Modulates Conformational Ensembles of Intrinsically Disordered Proteins
    • Mao, A. H.; Crick, S. L.; Vitalis, A.; Chicoine, C. L.; Pappu, R. V. Net Charge per Residue Modulates Conformational Ensembles of Intrinsically Disordered Proteins Proc. Natl. Acad. Sci. U. S. A. 2010, 107 (18) 8183-8
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.18 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 30
    • 78649600626 scopus 로고    scopus 로고
    • Trapping Single Molecules in Liposomes: Surface Interactions and Freeze-Thaw Effects
    • Liu, B.; Mazouchi, A.; Gradinaru, C. C. Trapping Single Molecules in Liposomes: Surface Interactions and Freeze-Thaw Effects J Phys Chem B 2010, 114 (46) 15191-8
    • (2010) J Phys Chem B , vol.114 , Issue.46 , pp. 15191-15198
    • Liu, B.1    Mazouchi, A.2    Gradinaru, C.C.3
  • 31
    • 84884942553 scopus 로고    scopus 로고
    • Sub-Diffusion Decays in Fluorescence Correlation Spectroscopy: Dye Photophysics or Protein Dynamics?
    • Mazouchi, A.; Bahram, A.; Gradinaru, C. C. Sub-Diffusion Decays in Fluorescence Correlation Spectroscopy: Dye Photophysics or Protein Dynamics? J. Phys. Chem. B 2013, 117 (38) 11100-11
    • (2013) J. Phys. Chem. B , vol.117 , Issue.38 , pp. 11100-11111
    • Mazouchi, A.1    Bahram, A.2    Gradinaru, C.C.3
  • 32
  • 33
    • 34547348810 scopus 로고    scopus 로고
    • Measuring Conformational Dynamics: A New FCS-FRET Approach
    • Torres, T.; Levitus, M. Measuring Conformational Dynamics: A New FCS-FRET Approach J. Phys. Chem. B 2007, 111 (25) 7392-400
    • (2007) J. Phys. Chem. B , vol.111 , Issue.25 , pp. 7392-7400
    • Torres, T.1    Levitus, M.2
  • 34
    • 75649087013 scopus 로고    scopus 로고
    • FRET Fluctuation Spectroscopy of Diffusing Biopolymers: Contributions of Conformational Dynamics and Translational Diffusion
    • Gurunathan, K.; Levitus, M. FRET Fluctuation Spectroscopy of Diffusing Biopolymers: Contributions of Conformational Dynamics and Translational Diffusion J. Phys. Chem. B 2010, 114 (2) 980-6
    • (2010) J. Phys. Chem. B , vol.114 , Issue.2 , pp. 980-986
    • Gurunathan, K.1    Levitus, M.2
  • 35
    • 84882364963 scopus 로고    scopus 로고
    • Conformations of Intrinsically Disordered Proteins are Influenced by Linear Sequence Distributions of Oppositely Charged Residues
    • Das, R. K.; Pappu, R. V. Conformations of Intrinsically Disordered Proteins are Influenced by Linear Sequence Distributions of Oppositely Charged Residues Proc. Natl. Acad. Sci. U. S. A. 2013, 110 (33) 13392-7
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.33 , pp. 13392-13397
    • Das, R.K.1    Pappu, R.V.2
  • 36
    • 77951645923 scopus 로고    scopus 로고
    • Sequence Determinants of Compaction in Intrinsically Disordered Proteins
    • Marsh, J. A.; Forman-Kay, J. D. Sequence Determinants of Compaction in Intrinsically Disordered Proteins Biophys. J. 2010, 98 (10) 2383-90
    • (2010) Biophys. J. , vol.98 , Issue.10 , pp. 2383-2390
    • Marsh, J.A.1    Forman-Kay, J.D.2
  • 40
    • 73649087584 scopus 로고    scopus 로고
    • On the Mechanism of SDS-Induced Protein Denaturation
    • Bhuyan, A. K. On the Mechanism of SDS-Induced Protein Denaturation Biopolymers 2010, 93 (2) 186-99
    • (2010) Biopolymers , vol.93 , Issue.2 , pp. 186-199
    • Bhuyan, A.K.1
  • 41
    • 84897584315 scopus 로고    scopus 로고
    • Theory of Single-Molecule FRET Efficiency Histograms
    • In; John Wiley & Sons, Inc. Hoboken, NJ
    • Gopich, I.V.; Szabo, A. Theory of Single-Molecule FRET Efficiency Histograms. In Single-Molecule Biophysics: Experiment and Theory; John Wiley & Sons, Inc.: Hoboken, NJ, 2011; Vol. 146.
    • (2011) Single-Molecule Biophysics: Experiment and Theory , vol.146
    • Gopich, I.V.1    Szabo, A.2
  • 43
    • 77949569719 scopus 로고    scopus 로고
    • Alternating-Laser Excitation of Single Molecules
    • In; Selvin, P. R. Ha, T. CSHL Press: New York, Chapter 5
    • Xiao, J.; Elf, J.; Li, G.-W.; Yu, J.; Xie, X. S. Alternating-Laser Excitation of Single Molecules. In Single Molecule Techniques: A Laboratory Manual; Selvin, P. R.; Ha, T., Eds.; CSHL Press: New York, 2008; Chapter 5.
    • (2008) Single Molecule Techniques: A Laboratory Manual
    • Xiao, J.1    Elf, J.2    Li, G.-W.3    Yu, J.4    Xie, X.S.5
  • 44
    • 79953853888 scopus 로고    scopus 로고
    • Identifying Molecular Dynamics in Single-Molecule FRET Experiments with Burst Variance Analysis
    • Torella, J. P.; Holden, S. J.; Santoso, Y.; Hohlbein, J.; Kapanidis, A. N. Identifying Molecular Dynamics in Single-Molecule FRET Experiments with Burst Variance Analysis Biophys. J. 2011, 100 (6) 1568-77
    • (2011) Biophys. J. , vol.100 , Issue.6 , pp. 1568-1577
    • Torella, J.P.1    Holden, S.J.2    Santoso, Y.3    Hohlbein, J.4    Kapanidis, A.N.5
  • 46
    • 84865333057 scopus 로고    scopus 로고
    • Application of Confocal Single-Molecule FRET to Intrinsically Disordered Proteins
    • Schuler, B.; Muller-Spath, S.; Soranno, A.; Nettels, D. Application of Confocal Single-Molecule FRET to Intrinsically Disordered Proteins Methods Mol. Biol. 2012, 896, 21-45
    • (2012) Methods Mol. Biol. , vol.896 , pp. 21-45
    • Schuler, B.1    Muller-Spath, S.2    Soranno, A.3    Nettels, D.4
  • 47
    • 0342280403 scopus 로고
    • Conformations of a Polyelectrolyte Chain
    • Ha, B. Y.; Thirumalai, D. Conformations of a Polyelectrolyte Chain Phys. Rev. A 1992, 46 (6) R3012-R3015
    • (1992) Phys. Rev. A , vol.46 , Issue.6
    • Ha, B.Y.1    Thirumalai, D.2
  • 48
    • 80052917268 scopus 로고    scopus 로고
    • A Molecular Debye-Huckel Theory and Its Applications to Electrolyte Solutions
    • Xiao, T.; Song, X. A Molecular Debye-Huckel Theory and Its Applications to Electrolyte Solutions J. Chem. Phys. 2011, 135 (10) 104104
    • (2011) J. Chem. Phys. , vol.135 , Issue.10 , pp. 104104
    • Xiao, T.1    Song, X.2
  • 49
    • 0026729426 scopus 로고
    • Protein Interactions with Urea and Guanidinium Chloride. A Calorimetric Study
    • Makhatadze, G. I.; Privalov, P. L. Protein Interactions with Urea and Guanidinium Chloride. A Calorimetric Study J. Mol. Biol. 1992, 226 (2) 491-505
    • (1992) J. Mol. Biol. , vol.226 , Issue.2 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 50
    • 72249118262 scopus 로고    scopus 로고
    • Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation
    • Tadeo, X.; Lopez-Mendez, B.; Castano, D.; Trigueros, T.; Millet, O. Protein Stabilization and the Hofmeister Effect: The Role of Hydrophobic Solvation Biophys. J. 2009, 97 (9) 2595-603
    • (2009) Biophys. J. , vol.97 , Issue.9 , pp. 2595-2603
    • Tadeo, X.1    Lopez-Mendez, B.2    Castano, D.3    Trigueros, T.4    Millet, O.5
  • 51
    • 79551522926 scopus 로고    scopus 로고
    • On the Performance of Bioanalytical Fluorescence Correlation Spectroscopy Measurements in a Multiparameter Photon-Counting Microscope
    • Mazouchi, A.; Liu, B.; Bahram, A.; Gradinaru, C. C. On the Performance of Bioanalytical Fluorescence Correlation Spectroscopy Measurements in a Multiparameter Photon-Counting Microscope Anal. Chim. Acta 2011, 688 (1) 61-9
    • (2011) Anal. Chim. Acta , vol.688 , Issue.1 , pp. 61-69
    • Mazouchi, A.1    Liu, B.2    Bahram, A.3    Gradinaru, C.C.4
  • 52
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between Macromolecules and Ions: The Hofmeister Series
    • Zhang, Y. J.; Cremer, P. S. Interactions between Macromolecules and Ions: The Hofmeister Series Curr. Opin. Chem. Biol. 2006, 10 (6) 658-663
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , Issue.6 , pp. 658-663
    • Zhang, Y.J.1    Cremer, P.S.2
  • 53
    • 0036303785 scopus 로고    scopus 로고
    • The Effects of Ionic Strength on Protein Stability: The Cold Shock Protein Family
    • Dominy, B. N.; Perl, D.; Schmid, F. X.; Brooks, C. L., 3rd. The Effects of Ionic Strength on Protein Stability: The Cold Shock Protein Family J. Mol. Biol. 2002, 319 (2) 541-54
    • (2002) J. Mol. Biol. , vol.319 , Issue.2 , pp. 541-554
    • Dominy, B.N.1    Perl, D.2    Schmid, F.X.3    Brooks III, C.L.4
  • 54
    • 1942519360 scopus 로고    scopus 로고
    • The Efficiency of Different Salts to Screen Charge Interactions in Proteins: A Hofmeister Effect?
    • Perez-Jimenez, R.; Godoy-Ruiz, R.; Ibarra-Molero, B.; Sanchez-Ruiz, J. M. The Efficiency of Different Salts to Screen Charge Interactions in Proteins: A Hofmeister Effect? Biophys. J. 2004, 86 (4) 2414-29
    • (2004) Biophys. J. , vol.86 , Issue.4 , pp. 2414-2429
    • Perez-Jimenez, R.1    Godoy-Ruiz, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 55
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically Disordered Proteins: A 10-Year Recap
    • Tompa, P. Intrinsically Disordered Proteins: A 10-Year Recap Trends Biochem. Sci. 2012, 37, 509-16
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 509-516
    • Tompa, P.1
  • 57
    • 84867048390 scopus 로고    scopus 로고
    • Polymer Scaling Laws of Unfolded and Intrinsically Disordered Proteins Quantified with Single-Molecule Spectroscopy
    • Hofmann, H.; Soranno, A.; Borgia, A.; Gast, K.; Nettels, D.; Schuler, B. Polymer Scaling Laws of Unfolded and Intrinsically Disordered Proteins Quantified with Single-Molecule Spectroscopy Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (40) 16155-60
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.40 , pp. 16155-16160
    • Hofmann, H.1    Soranno, A.2    Borgia, A.3    Gast, K.4    Nettels, D.5    Schuler, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.