메뉴 건너뛰기




Volumn 7, Issue 11, 1998, Pages 2431-2437

Surface salt bridges stabilize the GCN4 leucine zipper

Author keywords

GCN4; Leucine zipper; Salt bridge; Thermal stability

Indexed keywords

ALANINE; LEUCINE ZIPPER PROTEIN; MUTANT PROTEIN;

EID: 0031764838     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071121     Document Type: Article
Times cited : (95)

References (57)
  • 1
    • 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 DE, Becktel WJ, Dahlquist FW. 1990. pH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29:2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 3
    • 0027236794 scopus 로고
    • Structural basis of amino acid α-helical propensity
    • Blaber M, Zhang XJ, Matthews BW. 1993. Structural basis of amino acid α-helical propensity. Science 260:1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 5
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan MK, Mukund S, Kletzin A, Adams MWW, Rees DC. 1995. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267:1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 6
    • 0029077857 scopus 로고
    • Interactions between hydrophobic side chains within alpha helices
    • Creamer TP, Rose GD. 1995. Interactions between hydrophobic side chains within alpha helices. Protein Sci 4:1305-1314.
    • (1995) Protein Sci , vol.4 , pp. 1305-1314
    • Creamer, T.P.1    Rose, G.D.2
  • 8
    • 0343742614 scopus 로고    scopus 로고
    • Automated design of the surface positions of protein helices
    • Dahiyat BI, Gordon B, Mayo SL. 1997. Automated design of the surface positions of protein helices. Protein Sci 6:1333-1337.
    • (1997) Protein Sci , vol.6 , pp. 1333-1337
    • Dahiyat, B.I.1    Gordon, B.2    Mayo, S.L.3
  • 9
    • 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 BW. 1991. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry 30:7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Dao-Pin, S.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 10
    • 0029900846 scopus 로고    scopus 로고
    • The magnitude of the backbone conformational entropy change in protein folding
    • D'Aquino JA, Gomez J, Hilser VJ, Lee KH, Amzel LM, Freire E. 1996. The magnitude of the backbone conformational entropy change in protein folding. Proteins 25:143-156.
    • (1996) Proteins , vol.25 , pp. 143-156
    • D'Aquino, J.A.1    Gomez, J.2    Hilser, V.J.3    Lee, K.H.4    Amzel, L.M.5    Freire, E.6
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T. 1993. A switch between two-, three-, and four stranded coiled coils in GCN4 leucine zipper mutants. Science 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 14
    • 0031584272 scopus 로고    scopus 로고
    • Solution structure of ferrodoxin from the thermophilic cyanobacterium Synechoccus elongatos and its thermostability
    • Hatanaka H, Tanimuri R, Katoh S, Inagaki F. 1997. Solution structure of ferrodoxin from the thermophilic cyanobacterium Synechoccus elongatos and its thermostability. J Mol Biol 268:922-933.
    • (1997) J Mol Biol , vol.268 , pp. 922-933
    • Hatanaka, H.1    Tanimuri, R.2    Katoh, S.3    Inagaki, F.4
  • 15
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, 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
  • 16
    • 0030822593 scopus 로고    scopus 로고
    • Stability and dynamics in a hyperthermophilic protein with temperature close to 200°C
    • Killer R, Zhou ZH, Adams MWW, Englander SW. 1997. Stability and dynamics in a hyperthermophilic protein with temperature close to 200°C. Proc Natl Acad Sci USA 94:11329-11332.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11329-11332
    • Killer, R.1    Zhou, Z.H.2    Adams, M.W.W.3    Englander, S.W.4
  • 17
    • 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. 1990. Strength and cooperativity of contributions of surface salt bridges to protein stability. J Mol Biol 216:1031-1044.
    • (1990) J Mol Biol , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 18
    • 0003151250 scopus 로고
    • The basic-region leucine-zipper family of DNA binding-proteins
    • Hu J, Sauer R. 1992. The basic-region leucine-zipper family of DNA binding-proteins. Nucleic Acids Mol Biol 6:82-101.
    • (1992) Nucleic Acids Mol Biol , vol.6 , pp. 82-101
    • Hu, J.1    Sauer, R.2
  • 19
    • 0027180729 scopus 로고
    • Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis
    • Hu JC, Newell NE, Tidor B, Sauer RT. 1993. Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis. Protein Sci 2:1072-1084.
    • (1993) Protein Sci , vol.2 , pp. 1072-1084
    • Hu, J.C.1    Newell, N.E.2    Tidor, B.3    Sauer, R.T.4
  • 20
    • 0027475153 scopus 로고
    • Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientation and spacings
    • Huyghues-Despointes BMP, Scholtz JM, Baldwin RL. 1993a. Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientation and spacings. Protein Sci 2:80-85.
    • (1993) Protein Sci , vol.2 , pp. 80-85
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 21
    • 0027359429 scopus 로고
    • Effect of a single aspartate on helix stability at different positions in a neutral alanine based peptide
    • Huyghues-Despointes BMP, Scholtz JM, Baldwin RL. 1993b. Effect of a single aspartate on helix stability at different positions in a neutral alanine based peptide. Protein Sci 2:1604-1611.
    • (1993) Protein Sci , vol.2 , pp. 1604-1611
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 22
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson ML, Correia JJ, Yphantis DA, Halvorson HR. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys J 36:575-588.
    • (1981) Biophys J , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 23
    • 0008863560 scopus 로고
    • Some factors in the interaction of protein denaturation
    • Kauzmann W. 1959. Some factors in the interaction of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 24
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer I, Steipe B, Huber R, Tomschy A, Jaenicke R. 1995. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J Mol Biol 246:511-521.
    • (1995) J Mol Biol , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 25
    • 0032546758 scopus 로고    scopus 로고
    • Inter-helical interactions in the leucine zipper coiled-coil dimer: PH and salt dependence of coupling energy between charged amino acids
    • Krylov D, Barchi J, Vinson C. 1998. Inter-helical interactions in the leucine zipper coiled-coil dimer: pH and salt dependence of coupling energy between charged amino acids. J Mol Biol 297:959-972.
    • (1998) J Mol Biol , vol.297 , pp. 959-972
    • Krylov, D.1    Barchi, J.2    Vinson, C.3
  • 26
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 27
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding SE, Rowe AJ, Horton JC, eds. Cambridge, UK: The Royal Society of Chemistry Cambridge
    • Laue TM, Shah BD, Ridgeway TM, Pellitier SL. 1992. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, eds. Analytical ultracentrifugation in biochemistry and polymer science. Cambridge, UK: The Royal Society of Chemistry Cambridge. pp 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pellitier, S.L.4
  • 28
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled coil stability and specificity of dimerization
    • Lavigne P, Sönnichen FD, Kay CM, Hodges RS. 1996. Interhelical salt bridges, coiled coil stability and specificity of dimerization. Science 271:1136-1137.
    • (1996) Science , vol.271 , pp. 1136-1137
    • Lavigne, P.1    Sönnichen, F.D.2    Kay, C.M.3    Hodges, R.S.4
  • 29
    • 0028306360 scopus 로고
    • Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4
    • Lumb KJ, Carr CM, Kim PS. 1994. Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4. Biochemistry 33:7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 30
    • 0029008590 scopus 로고
    • A buried interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • Lumb KJ, Kim PS. 1995. A buried interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry 34:8642-8648.
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 31
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled coil stability and specificity of dimerization
    • Lumb KJ, Kim PS. 1996. Interhelical salt bridges, coiled coil stability and specificity of dimerization. Science 271:1137-1138.
    • (1996) Science , vol.271 , pp. 1137-1138
    • Lumb, K.J.1    Kim, P.S.2
  • 32
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
    • Lyu PC, Gans PJ, Kallenbach NR. 1992. Energetic contribution of solvent-exposed ion pairs to alpha-helix structure. J Mol Biol 223:343-350.
    • (1992) J Mol Biol , vol.223 , pp. 343-350
    • Lyu, P.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 34
    • 0024974452 scopus 로고
    • Engineering protein thermal stability
    • Menendez-Arias L, Argos P. 1989. Engineering protein thermal stability. J Mol Biol 206:397-406.
    • (1989) J Mol Biol , vol.206 , pp. 397-406
    • Menendez-Arias, L.1    Argos, P.2
  • 35
    • 0025044559 scopus 로고
    • Positional independence and additivity of amino acid replacements on the helical stability in monomeric peptides
    • Merutka G, Stellwagen E. 1990. Positional independence and additivity of amino acid replacements on the helical stability in monomeric peptides. Biochemistry 29:894-898.
    • (1990) Biochemistry , vol.29 , pp. 894-898
    • Merutka, G.1    Stellwagen, E.2
  • 36
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia B, Buchner V, Arad D. 1995. Complex salt bridges in proteins: Statistical analysis of structure and function. J Mol Biol 254:761-770.
    • (1995) J Mol Biol , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 37
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers KT, Pace CN, Scholtz JM. 1997. A direct comparison of helix propensity in proteins and peptides. Proc Natl Acad Sci USA 94:2833-2837.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2833-2837
    • Myers, K.T.1    Pace, C.N.2    Scholtz, J.M.3
  • 38
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • Nakamura H. 1996. Roles of electrostatic interaction in proteins. Q Rev Biophys 29:1-90.
    • (1996) Q Rev Biophys , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 40
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil KT, DeGrado WF. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 41
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two stranded parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber TA. 1991. X-ray structure of the GCN4 leucine zipper, a two stranded parallel coiled coil. Science 254:539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.A.4
  • 42
    • 0031565980 scopus 로고    scopus 로고
    • Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Pappenberger G, Schurig H, Jaenicke R. 1997. Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. J Mol Biol 274:676-683.
    • (1997) J Mol Biol , vol.274 , pp. 676-683
    • Pappenberger, G.1    Schurig, H.2    Jaenicke, R.3
  • 43
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • Perutz MF. 1978. Electrostatic effects in proteins. Science 201:1187-1191.
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 44
    • 0031865608 scopus 로고    scopus 로고
    • Novel evolutionary histories and adaptive features of proteins from hyperthermophiles
    • Robb FT, Maeder DL. 1998. Novel evolutionary histories and adaptive features of proteins from hyperthermophiles. Curr Opin Biotech 9:288-292.
    • (1998) Curr Opin Biotech , vol.9 , pp. 288-292
    • Robb, F.T.1    Maeder, D.L.2
  • 45
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 percent trifluoroethanol
    • Rohl CA, Chakrabartty A, Baldwin RL. 1996. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 percent trifluoroethanol. Protein Sci 5:2623-2637.
    • (1996) Protein Sci , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 47
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz JM, Qian H, Robbins VH, Baldwin RL. 1993. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry 32:9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 48
    • 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 AR. 1990. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double mutant cycles. Biochemistry 29:9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 49
    • 0032488654 scopus 로고    scopus 로고
    • Energetics of polar side-chain interactions in helical peptides: Salt effects on ion pairs and hydrogen bonds
    • Smith JS, Scholtz JM. 1998. Energetics of polar side-chain interactions in helical peptides: Salt effects on ion pairs and hydrogen bonds. Biochemistry 37:33-40.
    • (1998) Biochemistry , vol.37 , pp. 33-40
    • Smith, J.S.1    Scholtz, J.M.2
  • 51
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson KS, Vinson CR, Freire E. 1993. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 32:5491-5496.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 52
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt G, Argos P. 1997. Protein thermal stability: Hydrogen bonds or internal packing? Fold Design 2:S40-S46.
    • (1997) Fold Design , vol.2
    • Vogt, G.1    Argos, P.2
  • 53
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger CD, Schildbach JF, Sauer RT. 1995. Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol 2:122-128.
    • (1995) Nat Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 54
    • 0029591937 scopus 로고
    • Composition analysis of α-helices in thermophilic organisms
    • Warren GL, Petsko GA. 1995. Composition analysis of α-helices in thermophilic organisms. Protein Eng 8:905-913.
    • (1995) Protein Eng , vol.8 , pp. 905-913
    • Warren, G.L.1    Petsko, G.A.2
  • 56
    • 0022503457 scopus 로고
    • Calculation of protein conformation form circular dichroism
    • Yang YT, Wu CSC, Martinez HM. 1986. Calculation of protein conformation form circular dichroism. Methods Enzymol 130:208-257.
    • (1986) Methods Enzymol , vol.130 , pp. 208-257
    • Yang, Y.T.1    Wu, C.S.C.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.