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Volumn 332, Issue 4, 2003, Pages 927-936

Rearrangement of charge-charge interactions in variant ubiquitins as detected by double-mutant cycles and NMR

Author keywords

Charge; Electrostatic; pK; Protein; Ubiquitin

Indexed keywords

UBIQUITIN;

EID: 0041324868     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00995-1     Document Type: Article
Times cited : (17)

References (67)
  • 1
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • Markley J.L., Bax A., Arata Y., Hilbers C.W., Kaptein R., Sykes B.D., et al. Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. J. Biomol. NMR. 12:1998;1-23.
    • (1998) J. Biomol. NMR , vol.12 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6
  • 2
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • Warshel A. Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites. J. Biol. Chem. 273:1998;27035-27038.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27035-27038
    • Warshel, A.1
  • 3
    • 0032516494 scopus 로고    scopus 로고
    • a s in the active site of Escherichia coli thioredoxin
    • a s in the active site of Escherichia coli thioredoxin. Biochemistry. 37:1998;10298-10306.
    • (1998) Biochemistry , vol.37 , pp. 10298-10306
    • Dillet, V.1    Dyson, H.J.2    Bashford, D.3
  • 4
    • 0034616226 scopus 로고    scopus 로고
    • UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions
    • Beard M.B., Olsen A.E., Jones R.E., Erdogan S., Houslay M.D., Bolger G.B. UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions. J. Biol. Chem. 275:2000;10349-10358.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10349-10358
    • Beard, M.B.1    Olsen, A.E.2    Jones, R.E.3    Erdogan, S.4    Houslay, M.D.5    Bolger, G.B.6
  • 5
    • 0035895423 scopus 로고    scopus 로고
    • Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase
    • Archontis G., Simonson T., Karplus M. Binding free energies and free energy components from molecular dynamics and Poisson-Boltzmann calculations. Application to amino acid recognition by aspartyl-tRNA synthetase. J. Mol. Biol. 306:2001;307-327.
    • (2001) J. Mol. Biol. , vol.306 , pp. 307-327
    • Archontis, G.1    Simonson, T.2    Karplus, M.3
  • 6
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden J.B., Phillips G.N.J., Neal T.M., Raushel F.M., Holden H.M. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry. 40:2001;6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.J.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 7
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • Joshi M.D., Sidhu G., Nielsen J.E., Brayer G.D., Withers S.G., McIntosh L.P. Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry. 40:2001;10115-10139.
    • (2001) Biochemistry , vol.40 , pp. 10115-10139
    • Joshi, M.D.1    Sidhu, G.2    Nielsen, J.E.3    Brayer, G.D.4    Withers, S.G.5    McIntosh, L.P.6
  • 9
    • 20644436466 scopus 로고    scopus 로고
    • Solvent models for protein-ligand binding: Comparison of implicit solvent Poisson and surface generalized born models with explicit solvent simulations
    • Zhang L.Y., Gallicchio E., Friesner R.A., Levy R.M. Solvent models for protein-ligand binding: comparison of implicit solvent Poisson and surface generalized born models with explicit solvent simulations. J. Comput. Chem. 22:2001;591-607.
    • (2001) J. Comput. Chem. , vol.22 , pp. 591-607
    • Zhang, L.Y.1    Gallicchio, E.2    Friesner, R.A.3    Levy, R.M.4
  • 10
    • 0034824313 scopus 로고    scopus 로고
    • Electrostatic complementarity at ligand binding sites: Application to chorismate mutase
    • Kangas E., Tidor B. Electrostatic complementarity at ligand binding sites: application to chorismate mutase. J. Phys. Chem. B. 105:2001;880-888.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 880-888
    • Kangas, E.1    Tidor, B.2
  • 11
    • 0036286654 scopus 로고    scopus 로고
    • Free energy simulations come of age: Protein-ligand recognition
    • Simonson T., Archontis G., Karplus M. Free energy simulations come of age: protein-ligand recognition. Accts. Chem. Res. 35:2002;430-437.
    • (2002) Accts. Chem. Res. , vol.35 , pp. 430-437
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 12
    • 0019325832 scopus 로고
    • Experimental evaluation of the effective dielectric constant of proteins
    • Rees D.C. Experimental evaluation of the effective dielectric constant of proteins. J. Mol. Biol. 141:1980;323-326.
    • (1980) J. Mol. Biol. , vol.141 , pp. 323-326
    • Rees, D.C.1
  • 13
    • 0000502040 scopus 로고
    • Factors influencing redox potentials of electron transfer proteins
    • Moore G.R., Pettigrew G.W., Rogers N.K. Factors influencing redox potentials of electron transfer proteins. Proc. Natl Acad. Sci. USA. 83:1986;4998-4999.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4998-4999
    • Moore, G.R.1    Pettigrew, G.W.2    Rogers, N.K.3
  • 14
    • 0032579404 scopus 로고    scopus 로고
    • Modeling charge interactions and redox properties in DsbA
    • Warwicker J. Modeling charge interactions and redox properties in DsbA. J. Biol. Chem. 273:1998;2501-2504.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2501-2504
    • Warwicker, J.1
  • 15
    • 7144257841 scopus 로고    scopus 로고
    • The role of electrostatic interactions for cytochrome c oxidase function
    • Kannt A., Lancaster C.R., Michel H. The role of electrostatic interactions for cytochrome c oxidase function. J. Bioenerg. Biomembr. 30:1998;81-87.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 81-87
    • Kannt, A.1    Lancaster, C.R.2    Michel, H.3
  • 16
    • 0032054517 scopus 로고    scopus 로고
    • Electrostatic effects in macromolecules: Fundamental concepts and practical modeling
    • Warshel A., Papazyan A. Electrostatic effects in macromolecules: fundamental concepts and practical modeling. Curr. Opin. Struct. Biol. 8:1998;211-217.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 211-217
    • Warshel, A.1    Papazyan, A.2
  • 17
    • 0035312897 scopus 로고    scopus 로고
    • Electrostatics calculations: Recent methodological advances and applications to membranes
    • Tobias D.J. Electrostatics calculations: recent methodological advances and applications to membranes. Curr. Opin. Struct. Biol. 11:2001;253-261.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 253-261
    • Tobias, D.J.1
  • 18
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B., Yang A.S. Free energy balance in protein folding. Advan. Protein Chem. 46:1995;27-58.
    • (1995) Advan. Protein Chem. , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 19
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • Nakamura H. Roles of electrostatic interaction in proteins. Quart. Rev. Biophys. 29:1996;1-90.
    • (1996) Quart. Rev. Biophys. , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 21
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and thermotolerance of proteins from hyperthermophiles: A 'traffic' rule for hot roads
    • Karshikoff A., Ladenstein R. Ion pairs and thermotolerance of proteins from hyperthermophiles: a 'traffic' rule for hot roads. Trends Biochem. Sci. 26:2001;550-556.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 22
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • LoConte L., Chothia C., Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285:1999;2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • LoConte, L.1    Chothia, C.2    Janin, J.3
  • 23
    • 0036805481 scopus 로고    scopus 로고
    • Intramolecular interactions at protein surfaces and their impact on protein function
    • Robertson A.D. Intramolecular interactions at protein surfaces and their impact on protein function. Trends Biochem. Sci. 27:2002;521-526.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 521-526
    • Robertson, A.D.1
  • 24
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science. 268:1995;1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 25
    • 0035312551 scopus 로고    scopus 로고
    • Macromolecular electrostatics: Continuum models and their growing pains
    • Simonson T. Macromolecular electrostatics: continuum models and their growing pains. Curr. Opin. Struct. Biol. 11:2001;243-252.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 243-252
    • Simonson, T.1
  • 26
    • 0035451052 scopus 로고    scopus 로고
    • What are the dielectric constants of proteins and how to validate electrostatic models?
    • Schutz C.N., Warshel A. What are the dielectric constants of proteins and how to validate electrostatic models? Proteins: Struct. Funct. Genet. 44:2001;400-417.
    • (2001) Proteins: Struct. Funct. Genet. , vol.44 , pp. 400-417
    • Schutz, C.N.1    Warshel, A.2
  • 28
    • 0025923869 scopus 로고
    • a shifts accompanying the inactivating Asp121-Asn substitution in a semisynthetic bovine pancreatic ribonuclease
    • a shifts accompanying the inactivating Asp121-Asn substitution in a semisynthetic bovine pancreatic ribonuclease. Proc. Natl Acad. Sci. USA. 88:1991;8116-8120.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8116-8120
    • Cederholm, M.T.1    Stuckey, J.A.2    Doscher, M.S.3    Lee, L.4
  • 29
    • 0030612614 scopus 로고    scopus 로고
    • a changes in a protein tyrosine phosphatase: Experimental and theoretical determination of electrostatic properties in a small protein
    • a changes in a protein tyrosine phosphatase: experimental and theoretical determination of electrostatic properties in a small protein. Biochemistry. 36:1997;11984-11994.
    • (1997) Biochemistry , vol.36 , pp. 11984-11994
    • Tishmack, P.A.1    Bashford, D.2    Harms, E.3    Van Etten, R.L.4
  • 30
    • 0032535188 scopus 로고    scopus 로고
    • Coulombic effects of remote subsites on the active site of ribonuclease A
    • Fisher B.M., Schultz L.W., Raines R.T. Coulombic effects of remote subsites on the active site of ribonuclease A. Biochemistry. 37:1998;17386-17401.
    • (1998) Biochemistry , vol.37 , pp. 17386-17401
    • Fisher, B.M.1    Schultz, L.W.2    Raines, R.T.3
  • 31
    • 0032589144 scopus 로고    scopus 로고
    • a values in the wild-type, D121N, and D121A enzymes
    • a values in the wild-type, D121N, and D121A enzymes. Biophys. J. 76:1999;1571-1579.
    • (1999) Biophys. J. , vol.76 , pp. 1571-1579
    • Quirk, D.J.1    Raines, R.T.2
  • 32
    • 0034636803 scopus 로고    scopus 로고
    • a values in the ovomucoid third domain to charge replacement at a neighboring residue
    • a values in the ovomucoid third domain to charge replacement at a neighboring residue. Biochemistry. 39:2000;8067-8072.
    • (2000) Biochemistry , vol.39 , pp. 8067-8072
    • Forsyth, W.R.1    Robertson, A.D.2
  • 33
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A., Jordan M.R., Horner S.R., Batori V., Koide S. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry. 40:2001;10326-10333.
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1    Jordan, M.R.2    Horner, S.R.3    Batori, V.4    Koide, S.5
  • 34
    • 0036228118 scopus 로고    scopus 로고
    • Distance dependence and salt sensitivity of pairwise coulombic interactions in a protein
    • Lee K.K., Fitch C.A., Garcia-Moreno B. Distance dependence and salt sensitivity of pairwise coulombic interactions in a protein. Protein Sci. 11:2002;1004-1016.
    • (2002) Protein Sci. , vol.11 , pp. 1004-1016
    • Lee, K.K.1    Fitch, C.A.2    Garcia-Moreno, B.3
  • 35
    • 0037129945 scopus 로고    scopus 로고
    • Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups
    • Sundd M., Iverson N., Ibarra-Molero B., Sanchez-Ruiz J.M., Robertson A.D. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry. 41:2002;7586-7596.
    • (2002) Biochemistry , vol.41 , pp. 7586-7596
    • Sundd, M.1    Iverson, N.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4    Robertson, A.D.5
  • 37
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability: Guidelines for protein engineering
    • Makhatadze G., Loladze V., Ermolenko D., Chen X., Thomas S. Contribution of surface salt bridges to protein stability: guidelines for protein engineering. J. Mol. Biol. 327:2003;1135-1148.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1135-1148
    • Makhatadze, G.1    Loladze, V.2    Ermolenko, D.3    Chen, X.4    Thomas, S.5
  • 38
    • 0023644679 scopus 로고
    • Structure at ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar S., Bugg C.E., Cook W.J. Structure at ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194:1987;531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 39
    • 0022034438 scopus 로고
    • The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)
    • Bode W., Epp O., Huber R., Laskowski M.J.J., Ardelt W. The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). Eur. J. Biochem. 147:1985;387-395.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 387-395
    • Bode, W.1    Epp, O.2    Huber, R.3    Laskowski, M.J.J.4    Ardelt, W.5
  • 40
    • 0347298770 scopus 로고    scopus 로고
    • Changes in stability upon charge reversal and neutralization substitution in Staphylococcal nuclease are dominated by favorable electrostatic effects
    • Schwehmm J.M., Fitch C.A., Dang B.N., Garcia-Moreno B., Stites W.E. Changes in stability upon charge reversal and neutralization substitution in Staphylococcal nuclease are dominated by favorable electrostatic effects. Biochemistry. 42:2003;1118-1128.
    • (2003) Biochemistry , vol.42 , pp. 1118-1128
    • Schwehmm, J.M.1    Fitch, C.A.2    Dang, B.N.3    Garcia-Moreno, B.4    Stites, W.E.5
  • 41
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews B.W. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62:1995;139-160.
    • (1995) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 42
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
    • Serrano L., Horovitz A., Avron B., Bycroft M., Fersht A. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry. 29:1990;9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 43
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • Horovitz A., Fersht A.R. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214:1990;613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 44
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Dao-pin S., Sauer U., Nicholson H., Matthews B.W. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry. 30:1991;7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Dao-pin, S.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 45
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes
    • Whitby F.G., Xia G., Pickart C.M., Hill C.P. Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J. Biol. Chem. 273:1998;34983-34991.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 46
    • 0032567404 scopus 로고    scopus 로고
    • The rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in Arabidopsis
    • Rao-Naik C., de la Cruz W., Laplaza J.M., Tan S., Callis J., Fisher A.J. The rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in Arabidopsis. J. Biol. Chem. 273:1998;34976-34982.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34976-34982
    • Rao-Naik, C.1    De la Cruz, W.2    Laplaza, J.M.3    Tan, S.4    Callis, J.5    Fisher, A.J.6
  • 47
    • 0034923356 scopus 로고    scopus 로고
    • Use of chemical shifts in macromolecular structure determination
    • Wishart D.S., Case D.A. Use of chemical shifts in macromolecular structure determination. Methods Enzymol. 338:2001;3-34.
    • (2001) Methods Enzymol. , vol.338 , pp. 3-34
    • Wishart, D.S.1    Case, D.A.2
  • 49
    • 0002870406 scopus 로고
    • Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy
    • Markley J.L. Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy. Accts. Chem. Res. 8:1975;70-80.
    • (1975) Accts. Chem. Res. , vol.8 , pp. 70-80
    • Markley, J.L.1
  • 50
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 51
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason T., Ellison M. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14:1994;7876-7883.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.2
  • 52
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson E.S., Ma P.C., Ota I.M., Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270:1995;17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 53
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H., Mayer T., Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 96:1999;635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.4    Mayer, T.5    Jentsch, S.6
  • 54
    • 0033578781 scopus 로고    scopus 로고
    • E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains
    • Mastrandrea L.D., You J., Niles E.G., Pickart C.M. E2/E3-mediated assembly of lysine 29-linked polyubiquitin chains. J. Biol. Chem. 274:1999;27299-27306.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27299-27306
    • Mastrandrea, L.D.1    You, J.2    Niles, E.G.3    Pickart, C.M.4
  • 55
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten K., de Vrij F.M.S., Verhoef L.G.G.C., Fischer D.F., van Leeuwen F.W., Hol E.M., et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157:2002;417-427.
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1    De Vrij, F.M.S.2    Verhoef, L.G.G.C.3    Fischer, D.F.4    Van Leeuwen, F.W.5    Hol, E.M.6
  • 57
    • 0037474539 scopus 로고    scopus 로고
    • Charge-charge interactions are key determinants of the pK values of ionizable groups in Ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2)
    • Laurents D.V., Huyghues-Despointes B.M.P., Bruix M., Thurlkill R.L., Schell D., Newsom S., et al. Charge-charge interactions are key determinants of the pK values of ionizable groups in Ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2) . J. Mol. Biol. 325:2003;1077-1092.
    • (2003) J. Mol. Biol. , vol.325 , pp. 1077-1092
    • Laurents, D.V.1    Huyghues-Despointes, B.M.P.2    Bruix, M.3    Thurlkill, R.L.4    Schell, D.5    Newsom, S.6
  • 58
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero B., Loladze V.V., Makhatadze G.I., Sanchez-Ruiz J.M. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry. 38:1999;8138-8149.
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 59
    • 0025398721 scopus 로고
    • WHAT IF - A moleclar modeling and drug design program
    • Vriend G. WHAT IF - a moleclar modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 60
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze V.V., Ibarra-Molero B., Sanchez-Ruiz J.M., Makhatadze G.I. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry. 38:1999;16419-16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 61
    • 0036136161 scopus 로고    scopus 로고
    • Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable
    • Loladze V.V., Makhatadze G.I. Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Sci. 11:2002;174-177.
    • (2002) Protein Sci. , vol.11 , pp. 174-177
    • Loladze, V.V.1    Makhatadze, G.I.2
  • 62
    • 0032537485 scopus 로고    scopus 로고
    • Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain
    • Forsyth W.R., Gilson M.K., Antosiewicz J., Jaren O.R., Robertson A.D. Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain. Biochemistry. 37:1998;8643-8652.
    • (1998) Biochemistry , vol.37 , pp. 8643-8652
    • Forsyth, W.R.1    Gilson, M.K.2    Antosiewicz, J.3    Jaren, O.R.4    Robertson, A.D.5
  • 64
    • 0000132887 scopus 로고
    • PH Dependence of internal references
    • DeMarco A. pH Dependence of internal references. J. Magn. Reson. 26:1977;527-528.
    • (1977) J. Magn. Reson. , vol.26 , pp. 527-528
    • DeMarco, A.1
  • 65
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers. 18:1979;299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wüthrich, K.2
  • 66
    • 0023522384 scopus 로고
    • 1H NMR study of human ubiquitin: A main chain directed assignment and structure analysis
    • 1H NMR study of human ubiquitin: a main chain directed assignment and structure analysis. Biochemistry. 26:1987;7272-7281.
    • (1987) Biochemistry , vol.26 , pp. 7272-7281
    • Di Stefano, D.L.1    Wand, A.J.2
  • 67
    • 0023522385 scopus 로고
    • 1H NMR assignments and secondary structure identification of human ubiquitin
    • 1H NMR assignments and secondary structure identification of human ubiquitin. Biochemistry. 26:1987;7282-7290.
    • (1987) Biochemistry , vol.26 , pp. 7282-7290
    • Weber, P.L.1    Brown, S.C.2    Mueller, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.