메뉴 건너뛰기




Volumn 283, Issue 5, 1998, Pages 993-1012

Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in α-helical coiled-coils

Author keywords

Coiled coil; Interhelical ionic interactions; Ion pair; Orientation dependence; Side chain packing

Indexed keywords

GLUTAMIC ACID; GLUTAMINE; LYSINE; PROTEIN SUBUNIT; SYNTHETIC PEPTIDE;

EID: 0032514952     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2125     Document Type: Article
Times cited : (99)

References (108)
  • 1
    • 0027261284 scopus 로고
    • Structure, function and application of the coiled-coil protein folding motif
    • Adamson J.G., Zhou N.E., Hodges R.S. Structure, function and application of the coiled-coil protein folding motif. Curr. Opin. Biotechnol. 4:1993;428-437
    • (1993) Curr. Opin. Biotechnol. , vol.4 , pp. 428-437
    • Adamson, J.G.1    Zhou, N.E.2    Hodges, R.S.3
  • 3
    • 0027297241 scopus 로고
    • Genetic analysis of the leucine heptad repeats of Lac repressor: Evidence for a 4-helical bundle
    • Alberti S., Oehler S., von Wilcken-Bergmann B., Muller-Hill B. Genetic analysis of the leucine heptad repeats of Lac repressor evidence for a 4-helical bundle. EMBO J. 12:1993;3227-3236
    • (1993) EMBO J. , vol.12 , pp. 3227-3236
    • Alberti, S.1    Oehler, S.2    Von Wilcken-Bergmann, B.3    Muller-Hill, B.4
  • 4
    • 0025234587 scopus 로고
    • PH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson D.E., Becktel W.J., Dahlquist F.W. pH-Induced denaturation of proteins A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry. 29:1990;2403-2408
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 5
    • 0030200215 scopus 로고    scopus 로고
    • Acetylcholinesterase: Role of the enzyme's charge distribution in steering charged ligands toward the active site
    • Antosiewicz J., Wlodek S.T., McCammon J.A. Acetylcholinesterase role of the enzyme's charge distribution in steering charged ligands toward the active site. Biopolymers. 39:1996;85-94
    • (1996) Biopolymers , vol.39 , pp. 85-94
    • Antosiewicz, J.1    Wlodek, S.T.2    McCammon, J.A.3
  • 6
    • 0027537576 scopus 로고
    • Interaction of coiled-coils in transcription factors: Where is the specificity?
    • Baxevanis A.D., Vinson C.R. Interaction of coiled-coils in transcription factors where is the specificity? Curr. Opin. Genet. Dev. 3:1993;278-285
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 278-285
    • Baxevanis, A.D.1    Vinson, C.R.2
  • 7
    • 0030983330 scopus 로고    scopus 로고
    • A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein
    • Beck K., Gambee J.E., Kamawal A., Bächinger H.P. A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein. EMBO J. 16:1997;3767-3777
    • (1997) EMBO J. , vol.16 , pp. 3767-3777
    • Beck, K.1    Gambee, J.E.2    Kamawal, A.3    Bächinger, H.P.4
  • 8
    • 0029154811 scopus 로고
    • Native-like and structurally characterized designed α-helical bundles
    • Betz S.F., Bryson J.W., DeGrado W.F. Native-like and structurally characterized designed α-helical bundles. Curr. Opin. Struct. Biol. 5:1995;457-463
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 457-463
    • Betz, S.F.1    Bryson, J.W.2    Degrado, W.F.3
  • 9
    • 0027236794 scopus 로고
    • Structural basis of amino acid α-helix propensity
    • Blaber M., Zhang X.-J., Matthews B.W. Structural basis of amino acid α-helix propensity. Science. 260:1993;1637-1640
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 10
    • 0030445131 scopus 로고    scopus 로고
    • Thermodynamic analysis of a designed three-stranded coiled coil
    • Boice J.A., Dieckmann G.R., DeGrado W.F., Fairman R. Thermodynamic analysis of a designed three-stranded coiled coil. Biochemistry. 35:1996;14480-14485
    • (1996) Biochemistry , vol.35 , pp. 14480-14485
    • Boice, J.A.1    Dieckmann, G.R.2    Degrado, W.F.3    Fairman, R.4
  • 12
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty A., Kortemme T., Baldwin R.L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3:1994;843-852
    • (1994) Protein Sci. , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 13
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong L.T., Dempster S.E., Hendsch Z.S., Lee L.P., Tidor B. Computation of electrostatic complements to proteins a case of charge stabilized binding. Protein Sci. 7:1998;206-210
    • (1998) Protein Sci. , vol.7 , pp. 206-210
    • Chong, L.T.1    Dempster, S.E.2    Hendsch, Z.S.3    Lee, L.P.4    Tidor, B.5
  • 14
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen C., Parry D.A.D. α-Helical coiled coils and bundles how to design an α-helical protein. Proteins: Struct. Funct. Genet. 7:1990;1-15
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 15
    • 0028293441 scopus 로고
    • α-helical coiled-coils: More facts and better predictions
    • Cohen C., Parry D.A.D. α-helical coiled-coils more facts and better predictions. Science. 263:1994;488-489
    • (1994) Science , vol.263 , pp. 488-489
    • Cohen, C.1    Parry, D.A.D.2
  • 16
    • 0027513776 scopus 로고
    • Molecular modeling of coiled-coil α-tropomyosin: Analysis of staggered and in register helix-helix interactions
    • Cregut D., Liautard J.P., Heitz F., Chiche L. Molecular modeling of coiled-coil α-tropomyosin analysis of staggered and in register helix-helix interactions. Protein Eng. 6:1993;51-58
    • (1993) Protein Eng. , vol.6 , pp. 51-58
    • Cregut, D.1    Liautard, J.P.2    Heitz, F.3    Chiche, L.4
  • 17
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by direct mutagenesis
    • Dao-pin S., Sauer U., Nicholson H., Matthews B.M. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by direct 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.M.4
  • 18
    • 0031022887 scopus 로고    scopus 로고
    • Additivity principles in biochemistry
    • Dill K.A. Additivity principles in biochemistry. J. Biol. Chem. 272:1997;701-704
    • (1997) J. Biol. Chem. , vol.272 , pp. 701-704
    • Dill, K.A.1
  • 19
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig A.J., Sternberg M.J.E. Side-chain conformational entropy in protein folding. Protein Sci. 4:1995;2247-2251
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.E.2
  • 20
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uniterrupted α-helices: Crystal structure of the protein-DNA complex
    • Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C. The GCN4 basic region leucine zipper binds DNA as a dimer of uniterrupted α-helices crystal structure of the protein-DNA complex. Cell. 71:1992;1223-1237
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 21
    • 0029997591 scopus 로고    scopus 로고
    • On the choice of reference mutant states in the application of the double-mutant cycle method
    • Faiman G.A., Horovitz A. On the choice of reference mutant states in the application of the double-mutant cycle method. Protein Eng. 9:1996;315-316
    • (1996) Protein Eng. , vol.9 , pp. 315-316
    • Faiman, G.A.1    Horovitz, A.2
  • 23
    • 0015505502 scopus 로고
    • Conformational equilibria in α- And δ-chymotrypsin. the energetics and importance of the salt bridge
    • Fersht A.R. Conformational equilibria in α- and δ-chymotrypsin. The energetics and importance of the salt bridge. J. Mol. Biol. 64:1972;497-509
    • (1972) J. Mol. Biol. , vol.64 , pp. 497-509
    • Fersht, A.R.1
  • 24
    • 0031008575 scopus 로고    scopus 로고
    • On the calculation of binding free energies using continuum methods: Application to MHC class I protein-peptide interactions
    • Froloff N., Windemuth A., Honig B. On the calculation of binding free energies using continuum methods application to MHC class I protein-peptide interactions. Protein Sci. 6:1997;1293-1301
    • (1997) Protein Sci. , vol.6 , pp. 1293-1301
    • Froloff, N.1    Windemuth, A.2    Honig, B.3
  • 25
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover J.N.M., Harrison S.C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 26
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzalez L. Jr, Woolfson D.N., Alber T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nature Struct. Biol. 3:1996;1011-1018
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzalez Jr., L.1    Woolfson, D.N.2    Alber, T.3
  • 27
    • 0027146666 scopus 로고
    • Controlled formation of model homo- and heterodimer coiled-coil polypeptides
    • Graddis T.J., Myszka D.G., Chaiken I.M. Controlled formation of model homo- and heterodimer coiled-coil polypeptides. Biochemistry. 32:1993;12664-12671
    • (1993) Biochemistry , vol.32 , pp. 12664-12671
    • Graddis, T.J.1    Myszka, D.G.2    Chaiken, I.M.3
  • 28
    • 0026755510 scopus 로고
    • Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: Evidence for mutational effects on the free energy of the denatured state
    • Green S.M., Meeker A.K., Shortle D. Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease evidence for mutational effects on the free energy of the denatured state. Biochemistry. 31:1992;5717-5728
    • (1992) Biochemistry , vol.31 , pp. 5717-5728
    • Green, S.M.1    Meeker, A.K.2    Shortle, D.3
  • 29
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel T.M., Williams S.A., DeGrado W.F. Metal ion-dependent modulation of the dynamics of a designed protein. Science. 261:1993;879-885
    • (1993) Science , vol.261 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    Degrado, W.F.3
  • 30
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 31
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury P.B., Kim P.S., Alber T. Crystal structure of an isoleucine-zipper trimer. Nature. 371:1994;80-83
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 32
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? a continuum electrostatic analysis
    • Hendsch Z.S., Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3:1994;211-226
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 33
    • 0030345054 scopus 로고    scopus 로고
    • De novo design of α-helical proteins: Basic research to medical applications
    • Hodges R.S. De novo design of α-helical proteins basic research to medical applications. Biochem. Cell Biol. 74:1996;133-154
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 133-154
    • Hodges, R.S.1
  • 34
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B., Yang A.-S. Free energy balance in protein folding. Adv. Protein Chem. 46:1995;27-58
    • (1995) Adv. Protein Chem. , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.-S.2
  • 35
    • 0025663105 scopus 로고
    • Strength and cooperativity of contributions of surface salt bridges to protein stability
    • Horovitz A., Serrano L., Avron B., Bycroft M., Fersht A.R. Strength and cooperativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 36
    • 0026674251 scopus 로고
    • α-Helix stability in proteins. II. Factors that influence stability at an internal position
    • Horovitz A., Matthews J.M., Fersht A.R. α-Helix stability in proteins. II. Factors that influence stability at an internal position. J. Mol. Biol. 227:1992;560-658
    • (1992) J. Mol. Biol. , vol.227 , pp. 560-658
    • Horovitz, A.1    Matthews, J.M.2    Fersht, A.R.3
  • 37
    • 0003151250 scopus 로고
    • The basic-region leucine-zipper family of DNA binding proteins
    • Hu J.C., Sauer R.T. The basic-region leucine-zipper family of DNA binding proteins. Nucl. Acids Mol. Biol. 6:1992;82-101
    • (1992) Nucl. Acids Mol. Biol. , vol.6 , pp. 82-101
    • Hu, J.C.1    Sauer, R.T.2
  • 38
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: Analysis with λ-repressor-GCN4 leucine zipper fusions
    • Hu J.C., O'Shea E.K., Kim P.S., Sauer R.T. Sequence requirements for coiled-coils Analysis with λ-repressor-GCN4 leucine zipper fusions. Science. 250:1990;1400-1403
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 39
    • 0027180729 scopus 로고
    • Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenensis
    • Hu J.C., Newell N.E., Tidor B., Sauer R.T. Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenensis. Protein Sci. 2:1993;1072-1084
    • (1993) Protein Sci. , vol.2 , pp. 1072-1084
    • Hu, J.C.1    Newell, N.E.2    Tidor, B.3    Sauer, R.T.4
  • 40
    • 0028882032 scopus 로고
    • Measuring the strength of side-chain hydrogen bonds in peptide helices: The Gln·Asp (i,i+4) interaction
    • Huyghues-Despointes B.M.P., Klingler T.M., Baldwin R.L. Measuring the strength of side-chain hydrogen bonds in peptide helices the Gln·Asp (i,i+4) interaction. Biochemistry. 34:1995;13267-13271
    • (1995) Biochemistry , vol.34 , pp. 13267-13271
    • Huyghues-Despointes, B.M.P.1    Klingler, T.M.2    Baldwin, R.L.3
  • 41
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices
    • Kammerer R.A., Schulthess T., Landwehr R., Lustig A., Fischer D., Engl J. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices. J. Biol. Chem. 273:1998;10602-10608
    • (1998) J. Biol. Chem. , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engl, J.6
  • 42
    • 0031008576 scopus 로고    scopus 로고
    • Hydrophobicity regained
    • Karplus P.A. Hydrophobicity regained. Protein Sci. 6:1997;1302-1307
    • (1997) Protein Sci. , vol.6 , pp. 1302-1307
    • Karplus, P.A.1
  • 43
    • 0032167466 scopus 로고    scopus 로고
    • De novo design of α-helical coiled-coils and bundles: Models for development of protein design principles
    • Kohn W.D., Hodges R.S. De novo design of α-helical coiled-coils and bundles models for development of protein design principles. Trends Biotech. 16:1998;379-389
    • (1998) Trends Biotech. , vol.16 , pp. 379-389
    • Kohn, W.D.1    Hodges, R.S.2
  • 44
    • 0028959280 scopus 로고
    • Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil
    • Kohn W.D., Kay C.M., Hodges R.S. Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil. Protein Sci. 4:1995;237-250
    • (1995) Protein Sci. , vol.4 , pp. 237-250
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 45
    • 0028805884 scopus 로고
    • The effects of interhelical repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils
    • Kohn W.D., Monera O.D., Kay C.M., Hodges R.S. The effects of interhelical repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 270:1995;25495-25506
    • (1995) J. Biol. Chem. , vol.270 , pp. 25495-25506
    • Kohn, W.D.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4
  • 46
    • 0031564608 scopus 로고    scopus 로고
    • Salt effects on protein stability: Two-stranded α-helical coiled-coils containing inter- or intrahelical ion-pairs
    • Kohn W.D., Kay C.M., Hodges R.S. Salt effects on protein stability two-stranded α-helical coiled-coils containing inter- or intrahelical ion-pairs. J. Mol. Biol. 267:1997;1039-1052
    • (1997) J. Mol. Biol. , vol.267 , pp. 1039-1052
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 47
  • 48
    • 0031133303 scopus 로고    scopus 로고
    • Positional dependence of the effects of negatively charged Glu side-chains on the stability of two-stranded α-helical coiled-coils
    • Kohn W.K., Kay C.M., Hodges R.S. Positional dependence of the effects of negatively charged Glu side-chains on the stability of two-stranded α-helical coiled-coils. J. Pept. Sci. 3:1997;209-223
    • (1997) J. Pept. Sci. , vol.3 , pp. 209-223
    • Kohn, W.K.1    Kay, C.M.2    Hodges, R.S.3
  • 49
    • 0031885037 scopus 로고    scopus 로고
    • Effects of lanthanide binding on the stability of de novo designed α-helical coiled-coils
    • Kohn W.D., Kay C.M., Hodges R.S. Effects of lanthanide binding on the stability of de novo designed α-helical coiled-coils. J. Pept. Res. 51:1998;9-18
    • (1998) J. Pept. Res. , vol.51 , pp. 9-18
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 50
    • 0032542575 scopus 로고    scopus 로고
    • Metal ion-induced folding of a de novo designed coiled-coil peptide
    • Kohn W.D., Kay C.M., Sykes B.D., Hodges R.S. Metal ion-induced folding of a de novo designed coiled-coil peptide. J. Am. Chem. Soc. 120:1998;1124-1132
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1124-1132
    • Kohn, W.D.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4
  • 51
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • König P., Richmond T.J. The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233:1993;139-154
    • (1993) J. Mol. Biol. , vol.233 , pp. 139-154
    • König, P.1    Richmond, T.J.2
  • 52
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: E and g interhelical interactions
    • Krylov D., Mikhailenko I., Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity e and g interhelical interactions. EMBO J. 13:1994;2849-2861
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 53
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
    • Lavigne P., Sonnichsen F.D., Kay C.M., Hodges R.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1136-1137
    • (1996) Science , vol.271 , pp. 1136-1137
    • Lavigne, P.1    Sonnichsen, F.D.2    Kay, C.M.3    Hodges, R.S.4
  • 54
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • Lounnas V., Wade R.C. Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry. 36:1997;5402-5417
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 55
    • 0000820879 scopus 로고
    • Comparative study of the α-helical muscle proteins. Tyrosyl titration and effect of pH on conformation
    • Lowey S. Comparative study of the α-helical muscle proteins. Tyrosyl titration and effect of pH on conformation. J. Biol. Chem. 240:1965;2421-2427
    • (1965) J. Biol. Chem. , vol.240 , pp. 2421-2427
    • Lowey, S.1
  • 56
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • Lumb K.J., Kim P.S. A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry. 34:1995;8642-8648
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 57
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb K.J., Kim P.S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 268:1995;436-439
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 58
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
    • Lumb K.J., Kim P.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1137-1138
    • (1996) Science , vol.271 , pp. 1137-1138
    • Lumb, K.J.1    Kim, P.S.2
  • 59
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. Coiled coils new structures and new functions. Trends Biochem. Sci. 21:1996;375-382
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 60
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
    • Lyu P.C., Gans P.J., Kallenbach N.R. Energetic contribution of solvent-exposed ion pairs to alpha-helix structure. J. Mol. Biol. 223:1992;343-350
    • (1992) J. Mol. Biol. , vol.223 , pp. 343-350
    • Lyu, P.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 61
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan A.D., Stewart M. Tropomyosin coiled-coil interactions evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 62
    • 0025666831 scopus 로고
    • The thermal denaturation of nonpolymerizable αα-tropomyosin and its segments as a function of ionic strength
    • Mo J., Holtzer M.E., Holtzer A. The thermal denaturation of nonpolymerizable αα-tropomyosin and its segments as a function of ionic strength. Biopolymers. 30:1990;921-927
    • (1990) Biopolymers , vol.30 , pp. 921-927
    • Mo, J.1    Holtzer, M.E.2    Holtzer, A.3
  • 63
    • 0030804094 scopus 로고    scopus 로고
    • Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil
    • Moitra J., Szilak L., Krylov D., Vinson C. Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil. Biochemistry. 36:1997;12567-12573
    • (1997) Biochemistry , vol.36 , pp. 12567-12573
    • Moitra, J.1    Szilak, L.2    Krylov, D.3    Vinson, C.4
  • 64
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils
    • Monera O.D., Kay C.M., Hodges R.S. Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils. Biochemistry. 33:1994;3862-3871
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 65
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera O.D., Kay C.M., Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3:1994;1984-1991
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 66
    • 0032031405 scopus 로고    scopus 로고
    • Electrostatic contributions to protein-protein binding affinities: Application to Rap/Raf interaction
    • Muegge I., Schweins T., Warshel A. Electrostatic contributions to protein-protein binding affinities application to Rap/Raf interaction. Proteins: Struct. Funct. Genet. 30:1998;407-423
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 407-423
    • Muegge, I.1    Schweins, T.2    Warshel, A.3
  • 67
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers J.K., Pace C.N. Hydrogen bonding stabilizes globular proteins. Biophys. J. 71:1996;2033-2039
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 68
    • 0030858237 scopus 로고    scopus 로고
    • Helix propensities are identical in proteins and peptides
    • Myers J.K., Pace C.N., Scholtz J.M. Helix propensities are identical in proteins and peptides. Biochemistry. 36:1997;10923-10929
    • (1997) Biochemistry , vol.36 , pp. 10923-10929
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 70
    • 0027502369 scopus 로고
    • Successful prediction of the coiled-coil geometry of the GCN4 leucine zipper domain by simulated annealing: Comparison to the X-ray structure
    • Nilges M., Brunger A.T. Successful prediction of the coiled-coil geometry of the GCN4 leucine zipper domain by simulated annealing comparison to the X-ray structure. Proteins: Struct. Funct. Genet. 15:1993;133-146
    • (1993) Proteins: Struct. Funct. Genet. , vol.15 , pp. 133-146
    • Nilges, M.1    Brunger, A.T.2
  • 72
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids
    • O'Neil K.T., DeGrado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science. 250:1990;646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 73
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil
    • O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil. Science. 254:1991;539-544
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 74
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea E.K., Rutkowski R., Kim P.S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell. 68:1992;699-708
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 75
    • 0000236570 scopus 로고
    • Peptide "velcro": Design of a heterodimeric coiled-coil
    • O'Shea E.K., Lumb K.J., Kim P.S. Peptide "Velcro" design of a heterodimeric coiled-coil. Curr. Biol. 3:1993;658-667
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 76
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 77
    • 0026777217 scopus 로고
    • Contribution of the hydrophobic effect to globular protein stability
    • Pace C.N. Contribution of the hydrophobic effect to globular protein stability. J. Mol. Biol. 226:1992;29-35
    • (1992) J. Mol. Biol. , vol.226 , pp. 29-35
    • Pace, C.N.1
  • 78
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace C.N., Shirley B.A., McNutt M., Gajiwala K. Forces contributing to the conformational stability of proteins. FASEB J. 10:1996;75-83
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 79
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47:1995;83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 80
    • 0027321875 scopus 로고
    • Dimerization of leucine zippers analyzed by random selection
    • Pu W.T., Struhl K. Dimerization of leucine zippers analyzed by random selection. Nucl. Acids Res. 21:1993;4348-4355
    • (1993) Nucl. Acids Res. , vol.21 , pp. 4348-4355
    • Pu, W.T.1    Struhl, K.2
  • 81
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl C.A., Chakrabartty A., Baldwin R.L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5:1996;2623-2637
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 82
    • 0025911856 scopus 로고
    • Surface electrostatic interactions contribute little to stability of barnase
    • Sali D., Baycroft M., Fersht A.R. Surface electrostatic interactions contribute little to stability of barnase. J. Mol. Biol. 220:1991;779-788
    • (1991) J. Mol. Biol. , vol.220 , pp. 779-788
    • Sali, D.1    Baycroft, M.2    Fersht, A.R.3
  • 84
    • 0025938866 scopus 로고
    • Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: A circular dichroism and mutagenesis study
    • Schmidt-Dörr T., Oertel-Buchheit P., Pernelle C., Bracco L., Schnarr M., Granger-Schnarr M. Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper a circular dichroism and mutagenesis study. Biochemistry. 30:1991;9657-9664
    • (1991) Biochemistry , vol.30 , pp. 9657-9664
    • Schmidt-Dörr, T.1    Oertel-Buchheit, P.2    Pernelle, C.3    Bracco, L.4    Schnarr, M.5    Granger-Schnarr, M.6
  • 85
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz J.M., Qian H., Robbins V.H., Baldwin R.L. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry. 32:1993;9668-9676
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 86
    • 0026073643 scopus 로고
    • Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization
    • Schuermann M., Hunter J.B., Hennig G., Muller R. Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization. Nucl. Acids Res. 19:1991;739-746
    • (1991) Nucl. Acids Res. , vol.19 , pp. 739-746
    • Schuermann, M.1    Hunter, J.B.2    Hennig, G.3    Muller, R.4
  • 87
    • 0028113997 scopus 로고
    • Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions: Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains
    • Sereda T.J., Mant C.T., Sonnichsen F.D., Hodges R.S. Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains. J. Chromatog. 676:1994;139-153
    • (1994) J. Chromatog. , vol.676 , pp. 139-153
    • Sereda, T.J.1    Mant, C.T.2    Sonnichsen, F.D.3    Hodges, R.S.4
  • 88
    • 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.R. 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.R.5
  • 89
    • 0026926768 scopus 로고
    • The contribution of residue ion pairs to the helical stability of a model peptide
    • Stellwagen E., Park S.H., Shalongo W., Jain A. The contribution of residue ion pairs to the helical stability of a model peptide. Biopolymers. 32:1992;1193-1200
    • (1992) Biopolymers , vol.32 , pp. 1193-1200
    • Stellwagen, E.1    Park, S.H.2    Shalongo, W.3    Jain, A.4
  • 90
    • 0001647480 scopus 로고
    • Tropomyosin: A model protein for studying coiled-coil and α-helix stabilization
    • Talbot J.A., Hodges R.S. Tropomyosin a model protein for studying coiled-coil and α-helix stabilization. Acc. Chem. Res. 15:1982;224-230
    • (1982) Acc. Chem. Res. , vol.15 , pp. 224-230
    • Talbot, J.A.1    Hodges, R.S.2
  • 91
    • 0029146297 scopus 로고
    • A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper
    • Thompson-Kenar K., Garcia-Moreno B., Freire E. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci. 4:1995;1934-1938
    • (1995) Protein Sci. , vol.4 , pp. 1934-1938
    • Thompson-Kenar, K.1    Garcia-Moreno, B.2    Freire, E.3
  • 92
    • 0027176792 scopus 로고
    • Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: Prediction and rational design
    • Vinson C.R., Hai T., Boyd S.M. Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding prediction and rational design. Genes Dev. 7:1993;1047-1058
    • (1993) Genes Dev. , vol.7 , pp. 1047-1058
    • Vinson, C.R.1    Hai, T.2    Boyd, S.M.3
  • 93
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • Warshel A., Russell S.T. Calculations of electrostatic interactions in biological systems and in solutions. Quart. Rev. Biophys. 17:1984;283-422
    • (1984) Quart. Rev. Biophys. , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 94
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus-protein folding: The role of hydrophilic bridges in protein associations
    • Xu D., Lin S.L., Nussinov R. Protein binding versus-protein folding the role of hydrophilic bridges in protein associations. J. Mol. Biol. 265:1997;68-84
    • (1997) J. Mol. Biol. , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 95
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang A.-S., Honig B. On the pH dependence of protein stability. J. Mol. Biol. 231:1993;459-474
    • (1993) J. Mol. Biol. , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 96
    • 0030925636 scopus 로고    scopus 로고
    • The role of context on α-helix stabilization: Host-guest analysis in a mixed background peptide model
    • Yang J., Spek E.J., Gong Y., Zhou H., Kallenbach N.R. The role of context on α-helix stabilization Host-guest analysis in a mixed background peptide model. Protein Sci. 6:1997;1264-1272
    • (1997) Protein Sci. , vol.6 , pp. 1264-1272
    • Yang, J.1    Spek, E.J.2    Gong, Y.3    Zhou, H.4    Kallenbach, N.R.5
  • 99
    • 0029919676 scopus 로고    scopus 로고
    • Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
    • Yu Y., Monera O.D., Hodges R.S., Privalov P.L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:1996;367-372
    • (1996) J. Mol. Biol. , vol.255 , pp. 367-372
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 100
    • 0030769231 scopus 로고    scopus 로고
    • Oligomerization properties of GCN4 leucine zipper e and g position mutants
    • Zeng X., Zhu H., Lashuel H.A., Hu J.C. Oligomerization properties of GCN4 leucine zipper e and g position mutants. Protein Sci. 6:1997;2218-2226
    • (1997) Protein Sci. , vol.6 , pp. 2218-2226
    • Zeng, X.1    Zhu, H.2    Lashuel, H.A.3    Hu, J.C.4
  • 101
    • 0026795513 scopus 로고
    • Synthetic model proteins: Positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils
    • Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 267:1992;2664-2670
    • (1992) J. Biol. Chem. , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 102
    • 0026650710 scopus 로고
    • Synthetic model proteins: The relative contribution of leucine residues at the non-equivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil
    • Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins the relative contribution of leucine residues at the non-equivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil. Biochemistry. 31:1992;5739-5746
    • (1992) Biochemistry , vol.31 , pp. 5739-5746
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 103
    • 0026609553 scopus 로고
    • The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions
    • Zhou N.E., Zhu B.-Y., Kay C.M., Hodges R.S. The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions. Biopolymers. 32:1992;419-426
    • (1992) Biopolymers , vol.32 , pp. 419-426
    • Zhou, N.E.1    Zhu, B.-Y.2    Kay, C.M.3    Hodges, R.S.4
  • 104
    • 0027480940 scopus 로고
    • Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil
    • Zhou N.E., Kay C.M., Hodges R.S. Disulfide bond contribution to protein stability positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil. Biochemistry. 32:1993;3178-3187
    • (1993) Biochemistry , vol.32 , pp. 3178-3187
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 105
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou N.E., Kay C.M., Hodges R.S. The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7:1994;1365-1372
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 106
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability: De novo designed synthetic two-stranded α-helical coiled-coils
    • Zhou N.E., Kay C.M., Hodges R.S. The role of interhelical ionic interactions in controlling protein folding and stability de novo designed synthetic two-stranded α-helical coiled-coils. J. Mol. Biol. 237:1994;500-512
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 107
    • 0027995873 scopus 로고
    • α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix
    • Zhou N.E., Monera O.D., Kay C.M., Hodges R.S. α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix. Protein Pept. Letters. 1:1994;114-119
    • (1994) Protein Pept. Letters , vol.1 , pp. 114-119
    • Zhou, N.E.1    Monera, O.D.2    Kay, C.M.3    Hodges, R.S.4
  • 108
    • 0027475082 scopus 로고
    • Packing and hydrophobicity effects on protein folding and stability: Effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled-coils/leucine zippers
    • Zhu B.Y., Zhou N.E., Kay C.M., Hodges R.S. Packing and hydrophobicity effects on protein folding and stability effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled-coils/leucine zippers. Protein Sci. 2:1993;383-394
    • (1993) Protein Sci. , vol.2 , pp. 383-394
    • Zhu, B.Y.1    Zhou, N.E.2    Kay, C.M.3    Hodges, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.