메뉴 건너뛰기




Volumn 12, Issue 1, 2003, Pages 44-55

Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments

Author keywords

Electrostatic interactions; Fragment complementation; Protein stability; SH2 domain

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; PEPTIDE DERIVATIVE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P85;

EID: 0037215318     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0227903     Document Type: Article
Times cited : (7)

References (81)
  • 1
    • 0025234587 scopus 로고
    • pH-induced denaturation of proteins: A single salt bridge contributes 3 to 5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson, D.E., Becktel, W.J., and Dahlquist, F.W. 1990. pH-induced denaturation of proteins: A single salt bridge contributes 3 to 5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry. 29: 2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 2
    • 0001902066 scopus 로고
    • Heteronuclear J-coupling precession during spin-lock and adiabatic pulses: Use of adiabatic inversion pulses in high-resolution NMR
    • Bendall, M.R. 1995. Heteronuclear J-coupling precession during spin-lock and adiabatic pulses: Use of adiabatic inversion pulses in high-resolution NMR. J. Magn. Reson. Ser. A 116: 46-58.
    • (1995) J. Magn. Reson. Ser. A , vol.116 , pp. 46-58
    • Bendall, M.R.1
  • 3
    • 0035814792 scopus 로고    scopus 로고
    • Fragment complementation studies of protein stabilization by hydrophobic core residues
    • Bergård, T., Julenius, K., Ogard, A., Drakenberg, T., and Linse, S. 2001. Fragment complementation studies of protein stabilization by hydrophobic core residues. Biochemistry 40: 1257-1264.
    • (2001) Biochemistry , vol.40 , pp. 1257-1264
    • Bergård, T.1    Julenius, K.2    Ogard, A.3    Drakenberg, T.4    Linse, S.5
  • 4
    • 0028920304 scopus 로고
    • Alanine scanning mutagenesis of the α-helix 115-123 of phage T4 lysozyme: Effects on structure, stability, and the binding of solvent
    • Blaber, M., Baase, W.A., Gassner, N., and Matthews, B.W. 1995. Alanine scanning mutagenesis of the α-helix 115-123 of phage T4 lysozyme: Effects on structure, stability, and the binding of solvent. J. Mol. Biol. 246: 317-330.
    • (1995) J. Mol. Biol. , vol.246 , pp. 317-330
    • Blaber, M.1    Baase, W.A.2    Gassner, N.3    Matthews, B.W.4
  • 6
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • Bowie, J.U., Reidhaar-Olson, J.F., Lim, W.A., and Sauer, R.T. 1990. Deciphering the message in protein sequences: Tolerance to amino acid substitutions. Science 247: 1306-1310.
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 7
    • 0031430923 scopus 로고    scopus 로고
    • Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments
    • Chaffotte, A.F., Li, J.-H., Georgescu, R.E., Goldberg, M.E., and Tasayco, M.L. 1997. Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments. Biochemistry 36: 16040-16048.
    • (1997) Biochemistry , vol.36 , pp. 16040-16048
    • Chaffotte, A.F.1    Li, J.-H.2    Georgescu, R.E.3    Goldberg, M.E.4    Tasayco, M.L.5
  • 8
    • 0035909809 scopus 로고    scopus 로고
    • Packing is a key selection factor in the evolution of protein hydrophobic cores
    • Chen, J. and Stites, W.E. 2001. Packing is a key selection factor in the evolution of protein hydrophobic cores. Biochemistry 40: 15280-15289.
    • (2001) Biochemistry , vol.40 , pp. 15280-15289
    • Chen, J.1    Stites, W.E.2
  • 9
    • 0033006220 scopus 로고    scopus 로고
    • Tolerance of a protein to multiple polar-to-hydrophobic surface substitution
    • Cordes, M.H.J. and Sauer, R.T. 1999. Tolerance of a protein to multiple polar-to-hydrophobic surface substitution. Protein Sci. 8: 318-325.
    • (1999) Protein Sci. , vol.8 , pp. 318-325
    • Cordes, M.H.J.1    Sauer, R.T.2
  • 12
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat, B.I. and Mayo, S.L. 1997. Probing the role of packing specificity in protein design. Proc. Nat. Acad. Sci. 94: 10172-10177.
    • (1997) Proc. Nat. Acad. Sci. , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 13
    • 0026009211 scopus 로고
    • Cumulative site-directed charge-charge replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability
    • Dao-pin, S., Söderlind, E., Baase, W.A., Wozniak, J.A., Sauer, U., and Matthews, B.W. 1991. Cumulative site-directed charge-charge replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. J. Mol. Biol. 221: 873-887.
    • (1991) J. Mol. Biol. , vol.221 , pp. 873-887
    • Dao-pin, S.1    Söderlind, E.2    Baase, W.A.3    Wozniak, J.A.4    Sauer, U.5    Matthews, B.W.6
  • 14
    • 0034622519 scopus 로고    scopus 로고
    • Real-time kinetic studies on the interaction of transforming growth factor α with the epidermal growth factor receptor extracellular domain reveal a conformational change model
    • De Crescenzo, G., Grothe, S., Lortie, R., Debanne, M.T., and O'Connor-McCourt, M. 2000. Real-time kinetic studies on the interaction of transforming growth factor α with the epidermal growth factor receptor extracellular domain reveal a conformational change model. Biochemistry 39: 9466-9476.
    • (2000) Biochemistry , vol.39 , pp. 9466-9476
    • De Crescenzo, G.1    Grothe, S.2    Lortie, R.3    Debanne, M.T.4    O'Connor-McCourt, M.5
  • 15
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 16
    • 0029995708 scopus 로고    scopus 로고
    • Association of complementary fragments and the elucidation of protein folding pathways
    • de Prat-Gay, G. 1996. Association of complementary fragments and the elucidation of protein folding pathways. Protein Eng. 9: 843-847.
    • (1996) Protein Eng. , vol.9 , pp. 843-847
    • De Prat-Gay, G.1
  • 17
    • 0028200086 scopus 로고
    • Generation of a family of protein fragments for structure-folding studies, 2: Kinetics of association of the two chymotrypsin inhibitor-2 fragments
    • de Prat Gay, G., Ruiz-Sanz, J., and Fersht, A.R. 1994. Generation of a family of protein fragments for structure-folding studies, 2: Kinetics of association of the two chymotrypsin inhibitor-2 fragments. Biochemistry 33: 7964-7970.
    • (1994) Biochemistry , vol.33 , pp. 7964-7970
    • De Prat Gay, G.1    Ruiz-Sanz, J.2    Fersht, A.R.3
  • 19
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A.E., Baase, W.A., Zhang, X.-J., Heinz, D.W., Blaber, M., Baldwin, E.P., and Matthews, B.W. 1992. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255: 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.-J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 21
    • 0028269682 scopus 로고
    • Real-time DNA-binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the P42 and P51 isoforms
    • Fisher, R.J., Fivash, M., Casas-Finet, J., Erickson, J.W., Kondoh, A., Bladen, S.V., Fisher, C., Watson, D.K., and Papas, T. 1994. Real-time DNA-binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the P42 and P51 isoforms. Protein Sci. 3: 257-266.
    • (1994) Protein Sci. , vol.3 , pp. 257-266
    • Fisher, R.J.1    Fivash, M.2    Casas-Finet, J.3    Erickson, J.W.4    Kondoh, A.5    Bladen, S.V.6    Fisher, C.7    Watson, D.K.8    Papas, T.9
  • 22
    • 0035079285 scopus 로고    scopus 로고
    • Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1-73: 74-108) and their noncovalent complex: Evidence for the burial of apolar surface in protein unfolded states
    • Georgescu, R.E., Garcia-Mira, M.M., Tasayco, M.L., and Sanchez-Ruiz, J.M. 2001. Heat capacity analysis of oxidized Escherichia coli thioredoxin fragments (1-73: 74-108) and their noncovalent complex: Evidence for the burial of apolar surface in protein unfolded states. Eur. J. Biochem. 268: 1477-1485.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1477-1485
    • Georgescu, R.E.1    Garcia-Mira, M.M.2    Tasayco, M.L.3    Sanchez-Ruiz, J.M.4
  • 23
    • 0000064822 scopus 로고    scopus 로고
    • Tolerance of a protein helix to multiple alanine and valine substitutions
    • Gregoret, L.M. and Sauer, R.T. 1998. Tolerance of a protein helix to multiple alanine and valine substitutions., Folding Des. 3: 119-126.
    • (1998) Folding Des. , vol.3 , pp. 119-126
    • Gregoret, L.M.1    Sauer, R.T.2
  • 25
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z.S. and Tidor, B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3: 211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 26
    • 0032789936 scopus 로고    scopus 로고
    • Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding
    • -, 1999. Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding. Protein Sci. 8: 1381-1392.
    • (1999) Protein Sci. , vol.8 , pp. 1381-1392
  • 27
    • 0028243961 scopus 로고
    • Phosphopeptide binding to the N-terminal SH2 domain of the p85α subunit of PI 3′-kinase: A heteronuclear NMR study
    • Hensmann, M., Booker, G.W., Panayotou, G., Boyd, J., Linacre, J., Waterfield, M., and Campbell, I.D. 1994. Phosphopeptide binding to the N-terminal SH2 domain of the p85α subunit of PI 3′-kinase: A heteronuclear NMR study. Protein Sci. 3: 1020-1030.
    • (1994) Protein Sci. , vol.3 , pp. 1020-1030
    • Hensmann, M.1    Booker, G.W.2    Panayotou, G.3    Boyd, J.4    Linacre, J.5    Waterfield, M.6    Campbell, I.D.7
  • 28
    • 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., and Sanchez-Ruiz, J.M. 1999. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38: 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
  • 29
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson, S.E., Moracci, M., El Masry, N., Johnson, C.M., and Fersht, A.R. 1993. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32: 11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    El Masry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 30
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P., and Saarinen, T. 1992a. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114: 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 31
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins
    • Kay, L.E., Nicholson, L.K., Delaglio, F., Bax, A., and Torchia, D.A. 1992b. Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins. J. Magn. Reson. 97: 359-375.
    • (1992) J. Magn. Reson. , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4    Torchia, D.A.5
  • 32
    • 0024375463 scopus 로고
    • Energetics of complementary side-chain packing in a protein hydrophobic core
    • Kellis, Jr., J.T., Nyberg, K., and Fersht, A.R. 1989. Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry 28: 4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis J.T., Jr.1    Nyberg, K.2    Fersht, A.R.3
  • 33
    • 0033574158 scopus 로고    scopus 로고
    • Fragment reconstitution of a small protein: Disulfide mutant of a short C-terminal fragment derived from streptococcal protein G
    • Kobayashi, N., Honda, S., and Munekata, E. 1999. Fragment reconstitution of a small protein: Disulfide mutant of a short C-terminal fragment derived from streptococcal protein G. Biochemistry 38: 3228-3234.
    • (1999) Biochemistry , vol.38 , pp. 3228-3234
    • Kobayashi, N.1    Honda, S.2    Munekata, E.3
  • 34
    • 0033551039 scopus 로고    scopus 로고
    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state: Differentiation between local and nonlocal interactions
    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state: Differentiation between local and nonlocal interactions. Biochemistry 38: 4896-4903.
    • (1999) Biochemistry , vol.38 , pp. 4896-4903
    • Kuhlman, B.1    Luisi, D.L.2    Young, P.3    Raleigh, D.P.4
  • 35
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim, W.A. and Sauer, R.T. 1991. The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 219: 359-376.
    • (1991) J. Mol. Biol. , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 36
    • 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., and Makhatadze, G.I. 1999. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry 38: 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
  • 37
    • 0035909078 scopus 로고    scopus 로고
    • Probing the structure and stability of a hybrid protein: The human-E. coli thioredoxin chimera
    • Louis, J.M., Georgescu, R.E., Tasayco, M.L., Tcherkasskaya, O., and Gronenborn, A.M. 2001. Probing the structure and stability of a hybrid protein: The human-E. coli thioredoxin chimera. Biochemistry 40: 11184-11192.
    • (2001) Biochemistry , vol.40 , pp. 11184-11192
    • Louis, J.M.1    Georgescu, R.E.2    Tasayco, M.L.3    Tcherkasskaya, O.4    Gronenborn, A.M.5
  • 38
    • 0028574137 scopus 로고
    • Contributions of a hydrogen-bond salt bridge network to the stability of secondary and tertiary structure in λ/repressor
    • Marqusee, S. and Sauer, R.T. 1994. Contributions of a hydrogen-bond salt bridge network to the stability of secondary and tertiary structure in λ/repressor. Protein Sci. 3: 2217-2225.
    • (1994) Protein Sci. , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 39
    • 0035827175 scopus 로고    scopus 로고
    • In vitro selection of highly stabilized protein variants with optimized surface
    • Martin, A., Sieber, V., and Schmid, F.X. 2001. In vitro selection of highly stabilized protein variants with optimized surface. J. Mol. Biol. 309: 717-726.
    • (2001) J. Mol. Biol. , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 40
    • 0033952566 scopus 로고    scopus 로고
    • Stability of the molten globule state of a domain-exchanged chimeric protein between human and bovine α-lactalbumin
    • Masaki, K., Masuda, R., Takase, K., Kawano, K., and Nitta, K. 2000. Stability of the molten globule state of a domain-exchanged chimeric protein between human and bovine α-lactalbumin. Protein Eng. 13: 1-4.
    • (2000) Protein Eng. , vol.13 , pp. 1-4
    • Masaki, K.1    Masuda, R.2    Takase, K.3    Kawano, K.4    Nitta, K.5
  • 41
    • 0030045089 scopus 로고    scopus 로고
    • Structural and genetic analysis of the folding and function of T4 lysozyme
    • Matthews, B.W. 1996. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J. 10: 35-41.
    • (1996) FASEB J. , vol.10 , pp. 35-41
    • Matthews, B.W.1
  • 42
    • 0029967068 scopus 로고    scopus 로고
    • Contributions of the ionizable amino acids to the stability of staphylococcal nuclease
    • Meeker, A.K., Garcia-Moreno, E.B., and Shortle, D. 1996. Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. Biochemistry 35: 6443-6449.
    • (1996) Biochemistry , vol.35 , pp. 6443-6449
    • Meeker, A.K.1    Garcia-Moreno, E.B.2    Shortle, D.3
  • 43
    • 0028485627 scopus 로고
    • Protein stability effects of a complete set of alanine substitutions in Arc repressor
    • Milla, M.E., Brown, B.M., and Sauer, R.T. 1994. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nat. Struct. Biol. 1: 518-523.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 518-523
    • Milla, M.E.1    Brown, B.M.2    Sauer, R.T.3
  • 44
    • 0034685617 scopus 로고    scopus 로고
    • Local and longrange interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin
    • Mizuguchi, M., Masaki, K., Demura, M., and Nitta, K. 2000. Local and longrange interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin. J. Mol. Biol. 298: 985-995.
    • (2000) J. Mol. Biol. , vol.298 , pp. 985-995
    • Mizuguchi, M.1    Masaki, K.2    Demura, M.3    Nitta, K.4
  • 45
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interracial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. 1991. Protein folding and association: Insights from the interracial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0034769501 scopus 로고    scopus 로고
    • Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR
    • Ojennus, D.D., Fleissner, M.R., and Wuttke, D.S. 2001. Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR. Protein Sci. 10: 2162-2175.
    • (2001) Protein Sci. , vol.10 , pp. 2162-2175
    • Ojennus, D.D.1    Fleissner, M.R.2    Wuttke, D.S.3
  • 47
    • 0028157937 scopus 로고
    • Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: A critique of the surface plasmon resonance literature
    • O'Shannessy, D.J. 1994. Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: A critique of the surface plasmon resonance literature. Curr. Opin. Biotech. 5: 65-71.
    • (1994) Curr. Opin. Biotech. , vol.5 , pp. 65-71
    • O'Shannessy, D.J.1
  • 48
    • 0029939283 scopus 로고    scopus 로고
    • Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology
    • O'Shannessy, D.J. and Winzor, D.J. 1996. Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology. Anal. Biochem. 236: 275-283.
    • (1996) Anal. Biochem. , vol.236 , pp. 275-283
    • O'Shannessy, D.J.1    Winzor, D.J.2
  • 49
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace, C.N., Alston, R.W., and Shaw, K.L. 2000. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9: 1395-1398.
    • (2000) Protein Sci. , vol.9 , pp. 1395-1398
    • Pace, C.N.1    Alston, R.W.2    Shaw, K.L.3
  • 51
    • 0035914477 scopus 로고    scopus 로고
    • Electrostatic stabilization of a thermophilic cold shock protein
    • Perl, D. and Schmid, F.X. 2001. Electrostatic stabilization of a thermophilic cold shock protein. J. Mol. Biol. 313: 343-357.
    • (2001) J. Mol. Biol. , vol.313 , pp. 343-357
    • Perl, D.1    Schmid, F.X.2
  • 52
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenár, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 53
    • 0033609475 scopus 로고    scopus 로고
    • Putative interhelix ion pairs involved in the stability of myoglobin
    • Ramos, C.H.I., Kay, M.S., and Baldwin, R.L. 1999. Putative interhelix ion pairs involved in the stability of myoglobin. Biochemistry 38: 9783-9790.
    • (1999) Biochemistry , vol.38 , pp. 9783-9790
    • Ramos, C.H.I.1    Kay, M.S.2    Baldwin, R.L.3
  • 55
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F.M. 1977. Areas, volumes, packing and protein structure. Ann. Rev. Biophys. Bioeng. 6: 151-176.
    • (1977) Ann. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 56
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little to the stability of barnase
    • Sali, D., Bycroft, M., and Fersht, A.R. 1991. Surface electrostatic interactions contribute little to the stability of barnase. J. Mol. Biol. 220: 779-788.
    • (1991) J. Mol. Biol. , vol.220 , pp. 779-788
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 58
    • 0024400292 scopus 로고
    • Influence of interior packing and hydrophobicity on the stability of a protein
    • Sandberg, W.S. and Terwilliger, T.C. 1989. Influence of interior packing and hydrophobicity on the stability of a protein. Science 245: 54-57.
    • (1989) Science , vol.245 , pp. 54-57
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 59
    • 0030065958 scopus 로고    scopus 로고
    • Sequence determinants of folding and stability for the P22 arc repressor dimer
    • Sauer, R.T., Milla, M.E., Waldburger, C.D., Brown, B.M., and Schildbach, J.F. 1996. Sequence determinants of folding and stability for the P22 arc repressor dimer. FASEB J. 10: 42-48.
    • (1996) FASEB J. , vol.10 , pp. 42-48
    • Sauer, R.T.1    Milla, M.E.2    Waldburger, C.D.3    Brown, B.M.4    Schildbach, J.F.5
  • 61
    • 0032510765 scopus 로고    scopus 로고
    • Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease
    • Schwehm, J.M., Kristyanne, E.S., Biggers, C.C., and Stites, W.E. 1998. Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease. Biochemistry 37: 6939-6948.
    • (1998) Biochemistry , vol.37 , pp. 6939-6948
    • Schwehm, J.M.1    Kristyanne, E.S.2    Biggers, C.C.3    Stites, W.E.4
  • 62
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D., Stites, W.E., and Meeker, A.K. 1990. Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry 29: 8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 63
    • 48549111126 scopus 로고
    • Highly selective pi/2 and pi-pulse generation
    • Silver, M.S., Joseph, R.I., and Hoult, D.I. 1984. Highly selective pi/2 and pi-pulse generation. J. Magn. Reson. 59: 347-351.
    • (1984) J. Magn. Reson. , vol.59 , pp. 347-351
    • Silver, M.S.1    Joseph, R.I.2    Hoult, D.I.3
  • 64
    • 0031659672 scopus 로고    scopus 로고
    • Effects of salt bridges on protein structure and design
    • Sindelar, C.V., Hendsch, Z.S., and Tidor, B. 1998. Effects of salt bridges on protein structure and design. Protein Sci. 7: 1898-1914.
    • (1998) Protein Sci. , vol.7 , pp. 1898-1914
    • Sindelar, C.V.1    Hendsch, Z.S.2    Tidor, B.3
  • 65
    • 0028126676 scopus 로고
    • Optimization of the electrostatic interactions in proteins of different functional and folding type
    • Spassov, V.Z., Karshikoff, A.D., and Ladenstein, R. 1994. Optimization of the electrostatic interactions in proteins of different functional and folding type. Prot. Sci. 3: 1556-1569.
    • (1994) Prot. Sci. , vol.3 , pp. 1556-1569
    • Spassov, V.Z.1    Karshikoff, A.D.2    Ladenstein, R.3
  • 67
    • 0034673153 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability
    • Strop, P. and Mayo, S.L. 2000. Contribution of surface salt bridges to protein stability. Biochemistry 39: 1251-1255.
    • (2000) Biochemistry , vol.39 , pp. 1251-1255
    • Strop, P.1    Mayo, S.L.2
  • 68
    • 2342519701 scopus 로고    scopus 로고
    • Genetic studies of the lac repressor. XV: 4000 Single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure
    • Suckow, J., Markiewicz, P., Kleina, L.G., Miller, J., Kisters-Woike, B., and Müller-Hill, B. 1996. Genetic studies of the lac repressor, XV: 4000 Single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure. J. Mol. Biol. 261: 509-523.
    • (1996) J. Mol. Biol. , vol.261 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.G.3    Miller, J.4    Kisters-Woike, B.5    Müller-Hill, B.6
  • 69
    • 0034633994 scopus 로고    scopus 로고
    • Contribution of salt bridges near the surface of a protein to the conformational stability
    • Takano, K., Tsuchimori, K., Yamagata, Y., and Yutani, K. 2000. Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry 39: 12375-12381.
    • (2000) Biochemistry , vol.39 , pp. 12375-12381
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 70
    • 0040951542 scopus 로고    scopus 로고
    • Interaction between two discontiguous chain segments from the β-sheet of Escherichia coli thioredoxin suggests an initiation site for folding
    • Tasayco, M.L., Fuchs, J., Yang, X.-M., Dyalram, D., and Georgescu, R.E. 2000. Interaction between two discontiguous chain segments from the β-sheet of Escherichia coli thioredoxin suggests an initiation site for folding. Biochemistry 39: 10613-10618.
    • (2000) Biochemistry , vol.39 , pp. 10613-10618
    • Tasayco, M.L.1    Fuchs, J.2    Yang, X.-M.3    Dyalram, D.4    Georgescu, R.E.5
  • 71
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 74
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D., and Kuriyan, J. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms. Cell 72: 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kuriyan, J.5
  • 75
    • 0034700307 scopus 로고    scopus 로고
    • pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state
    • Whitten, S.T. and Garcia-Moreno, EB. 2000. pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state. Biochemistry 39: 14292-14304.
    • (2000) Biochemistry , vol.39 , pp. 14292-14304
    • Whitten, S.T.1    Garcia-Moreno, E.B.2
  • 76
    • 0027423604 scopus 로고
    • Cooperative self-assembly of SH2 domain fragments restores phosphopetide binding
    • Williams, K.P. and Shoelson, S.E. 1993. Cooperative self-assembly of SH2 domain fragments restores phosphopetide binding. Biochemistry 32: 11279-11284.
    • (1993) Biochemistry , vol.32 , pp. 11279-11284
    • Williams, K.P.1    Shoelson, S.E.2
  • 77
    • 0034628913 scopus 로고    scopus 로고
    • Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
    • Wong, K.B., Clarke, J., Bond, C.J., Neira, J.L., Freund, S.M.V., Fersht, A.R., and Daggett, V. 2000. Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J. Mol. Biol. 296: 1257-1282.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1257-1282
    • Wong, K.B.1    Clarke, J.2    Bond, C.J.3    Neira, J.L.4    Freund, S.M.V.5    Fersht, A.R.6    Daggett, V.7
  • 78
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • Xiao, L. and Honig, B. 1999. Electrostatic contributions to the stability of hyperthermophilic proteins. J. Mol. Biol. 289: 1435-1444.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 79
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu, J., Baase, W.A., Baldwin, E., and Matthews, B.W. 1998. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7: 158-177.
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 80
    • 0028906357 scopus 로고
    • Solution structure of the human pp60(c-Src) SH2 domain complexed with a phosphorylated tyrosine pentapeptide
    • Xu, R.X., Word, J.M., Davis, D.G., Rink, M.J., Willard, Jr., D.H., and Gampe, Jr., R.T. 1995. Solution structure of the human pp60(c-Src) SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Biochemistry 34: 2107-2121.
    • (1995) Biochemistry , vol.34 , pp. 2107-2121
    • Xu, R.X.1    Word, J.M.2    Davis, D.G.3    Rink, M.J.4    Willard D.H., Jr.5    Gampe R.T., Jr.6
  • 81
    • 0029018778 scopus 로고
    • Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis
    • Yu, M.-H., Weissman, J.S., and Kim, P.S. 1995. Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J. Mol. Biol. 249: 388-397.
    • (1995) J. Mol. Biol. , vol.249 , pp. 388-397
    • Yu, M.-H.1    Weissman, J.S.2    Kim, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.