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Volumn 334, Issue 5, 2003, Pages 1101-1115

Computational Design and Characterization of a Monomeric Helical Dinuclear Metalloprotein

Author keywords

Computational protein design; de novo design; di iron proteins; Metalloprotein; Side chain modeling

Indexed keywords

APOPROTEIN; COBALT; IRON; LIGAND; MANGANESE; METAL ION; METALLOPROTEIN; OLIGOMER; ZINC ION;

EID: 0345304457     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.004     Document Type: Article
Times cited : (127)

References (88)
  • 2
    • 0032144119 scopus 로고    scopus 로고
    • Functionalization of designed folded polypeptides
    • Baltzer L. Functionalization of designed folded polypeptides. Curr. Opin. Struct. Biol. 8:1998;466-470.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 466-470
    • Baltzer, L.1
  • 3
    • 0032835617 scopus 로고    scopus 로고
    • De novo design and structural characterization of proteins and metalloproteins
    • DeGrado W.F., Summa C.M., Pavone V., Nastri F., Lombardi A. De novo design and structural characterization of proteins and metalloproteins. Annu. Rev. Biochem. 68:1999;779-819.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 779-819
    • Degrado, W.F.1    Summa, C.M.2    Pavone, V.3    Nastri, F.4    Lombardi, A.5
  • 5
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat B.I., Mayo S.L. De novo protein design: fully automated sequence selection. Science. 278:1997;82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 6
    • 0035910266 scopus 로고    scopus 로고
    • Achieving stability and conformational specificity in designed proteins via binary patterning
    • Marshall S.A., Mayo S.L. Achieving stability and conformational specificity in designed proteins via binary patterning. J. Mol. Biol. 305:2001;619-631.
    • (2001) J. Mol. Biol. , vol.305 , pp. 619-631
    • Marshall, S.A.1    Mayo, S.L.2
  • 7
    • 0031746429 scopus 로고    scopus 로고
    • From coiled coils to small globular proteins: Design of a native-like three-helix bundle
    • Bryson J.W., Desjarlais J.R., Handel T.M., DeGrado W.F. From coiled coils to small globular proteins: design of a native-like three-helix bundle. Protein Sci. 7:1998;1404-1414.
    • (1998) Protein Sci. , vol.7 , pp. 1404-1414
    • Bryson, J.W.1    Desjarlais, J.R.2    Handel, T.M.3    Degrado, W.F.4
  • 9
    • 2642670311 scopus 로고    scopus 로고
    • Design of a 20-amino acid, three-stranded beta-sheet protein
    • Kortemme T., Ramirez-Alvarado M., Serrano L. Design of a 20-amino acid, three-stranded beta-sheet protein. Science. 281:1998;253-256.
    • (1998) Science , vol.281 , pp. 253-256
    • Kortemme, T.1    Ramirez-Alvarado, M.2    Serrano, L.3
  • 10
    • 0036385840 scopus 로고    scopus 로고
    • Computational design and characterization of an A2B2-heterotetrameric dimetal-binding protein
    • Summa C.M., Rosenblatt M.M., Hong J.-K., Lear J.D., DeGrado W.F. Computational design and characterization of an A2B2-heterotetrameric dimetal-binding protein. J. Mol. Biol. 321:2001;923-938.
    • (2001) J. Mol. Biol. , vol.321 , pp. 923-938
    • Summa, C.M.1    Rosenblatt, M.M.2    Hong, J.-K.3    Lear, J.D.4    Degrado, W.F.5
  • 11
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • Harbury P.B., Plecs J.J., Tidor B., Alber T., Kim P.S. High-resolution protein design with backbone freedom. Science. 282:1998;1462-1467.
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber, T.4    Kim, P.S.5
  • 12
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger L.L., Dwyer M.A., Smith J.J., Hellinga H.W. Computational design of receptor and sensor proteins with novel functions. Nature. 423:2003;185-190.
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 13
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon D.N., Mayo S.L. Enzyme-like proteins by computational design. Proc. Natl Acad. Sci. USA. 98:2001;14274-14279.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14274-14279
    • Bolon, D.N.1    Mayo, S.L.2
  • 15
    • 0037022813 scopus 로고    scopus 로고
    • Converting a maltose receptor into a nascent binuclear copper oxygenase by computational design
    • Benson D.E., Haddy A.E., Hellinga H.W. Converting a maltose receptor into a nascent binuclear copper oxygenase by computational design. Biochemistry. 41:2002;3262-3269.
    • (2002) Biochemistry , vol.41 , pp. 3262-3269
    • Benson, D.E.1    Haddy, A.E.2    Hellinga, H.W.3
  • 16
    • 0037261324 scopus 로고    scopus 로고
    • De novo backbone and sequence design of an idealized alpha/beta-barrel protein: Evidence of a stable tertiary structure
    • Offredi F., Dubail F., Kischel P., Sarinski K., Stern A.S., Van de Weerdt C., et al. De novo backbone and sequence design of an idealized alpha/beta-barrel protein: evidence of a stable tertiary structure. J. Mol. Biol. 1:2003;163-174.
    • (2003) J. Mol. Biol. , vol.1 , pp. 163-174
    • Offredi, F.1    Dubail, F.2    Kischel, P.3    Sarinski, K.4    Stern, A.S.5    Van De Weerdt, C.6
  • 17
    • 0023155210 scopus 로고
    • Tertiary templates for proteins use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder J.W., Richards F.M. Tertiary templates for proteins use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193:1987;775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 19
    • 0027438090 scopus 로고
    • A new approach to the design of stable proteins
    • Shakhnovich E.I., Gutin A.M. A new approach to the design of stable proteins. Protein Eng. 6:1993;793-800.
    • (1993) Protein Eng. , vol.6 , pp. 793-800
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 20
    • 0028220365 scopus 로고
    • De novo protein design using pairwise potentials and a genetic algorithm
    • Jones D.T. De novo protein design using pairwise potentials and a genetic algorithm. Protein Sci. 3:1994;567-574.
    • (1994) Protein Sci. , vol.3 , pp. 567-574
    • Jones, D.T.1
  • 21
    • 0028237287 scopus 로고
    • Optimal sequence selection in proteins of known structure by simulated evolution
    • Hellinga H.W., Richards F.M. Optimal sequence selection in proteins of known structure by simulated evolution. Proc. Natl Acad. Sci. USA. 91:1994;5803-5807.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5803-5807
    • Hellinga, H.W.1    Richards, F.M.2
  • 22
    • 0033516509 scopus 로고    scopus 로고
    • Side-chain and backbone flexibility in protein core design
    • Desjarlais J.R., Handel T.M. Side-chain and backbone flexibility in protein core design. J. Mol. Biol. 290:1999;305-318.
    • (1999) J. Mol. Biol. , vol.290 , pp. 305-318
    • Desjarlais, J.R.1    Handel, T.M.2
  • 23
    • 0033566738 scopus 로고    scopus 로고
    • Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin
    • Johnson E.C., Lazar G.A., Desjarlais J.R., Handel T.M. Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin. Struct. Fold. Des. 7:1999;967-976.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 967-976
    • Johnson, E.C.1    Lazar, G.A.2    Desjarlais, J.R.3    Handel, T.M.4
  • 24
    • 0033998280 scopus 로고    scopus 로고
    • A new approach to the design of uniquely folded thermally stable proteins
    • Jiang X., Farid H., Pistor E., Farid R.S. A new approach to the design of uniquely folded thermally stable proteins. Protein Sci. 9:2000;403-416.
    • (2000) Protein Sci. , vol.9 , pp. 403-416
    • Jiang, X.1    Farid, H.2    Pistor, E.3    Farid, R.S.4
  • 25
    • 0031048122 scopus 로고    scopus 로고
    • A de novo designed protein with properties that characterize natural hyperthermophilic proteins
    • Jiang X., Bishop E.J., Farid R.S. A de novo designed protein with properties that characterize natural hyperthermophilic proteins. J. Am. Chem. Soc. 119:1997;838-839.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 838-839
    • Jiang, X.1    Bishop, E.J.2    Farid, R.S.3
  • 26
    • 0034625322 scopus 로고    scopus 로고
    • Trading accuracy for speed: A quantitative comparison of search algorithms in protein sequence design
    • Voigt C.A., Gordon D.B., Mayo S.L. Trading accuracy for speed: a quantitative comparison of search algorithms in protein sequence design. J. Mol. Biol. 299:2000;789-803.
    • (2000) J. Mol. Biol. , vol.299 , pp. 789-803
    • Voigt, C.A.1    Gordon, D.B.2    Mayo, S.L.3
  • 27
    • 0001686478 scopus 로고    scopus 로고
    • Radical performance enhancements for combinatorial optimization algorithms based on the dead-end elimination theorem
    • Gordon D.B., Mayo S.L. Radical performance enhancements for combinatorial optimization algorithms based on the dead-end elimination theorem. J. Comput. Chem. 19:1998;1505-1514.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1505-1514
    • Gordon, D.B.1    Mayo, S.L.2
  • 29
    • 0001114311 scopus 로고    scopus 로고
    • Conformational splitting: A more powerful criterion for dead-end elimination
    • Pierce N.A., Spriet J.A., Desmet J., Mayo S.L. Conformational splitting: a more powerful criterion for dead-end elimination. J. Comput. Chem. 21:2000;999-1009.
    • (2000) J. Comput. Chem. , vol.21 , pp. 999-1009
    • Pierce, N.A.1    Spriet, J.A.2    Desmet, J.3    Mayo, S.L.4
  • 30
    • 0033599586 scopus 로고    scopus 로고
    • Rubredoxin variant folds without iron
    • Strop P., Mayo S.L. Rubredoxin variant folds without iron. J. Am. Chem. Soc. 121:1999;2341-2345.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2341-2345
    • Strop, P.1    Mayo, S.L.2
  • 31
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure, and stability of a hyperthermophilic protein variant
    • Malakauskas S.M., Mayo S.L. Design, structure, and stability of a hyperthermophilic protein variant. Nature Struct. Biol. 5:1998;470-475.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 32
    • 0035942160 scopus 로고    scopus 로고
    • Conversion of a maltose receptor into a zinc biosensor by computational design
    • Marvin J.S., Hellinga H.W. Conversion of a maltose receptor into a zinc biosensor by computational design. Proc. Natl Acad. Sci. USA. 98:2001;4955-4960.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4955-4960
    • Marvin, J.S.1    Hellinga, H.W.2
  • 33
    • 0036407643 scopus 로고    scopus 로고
    • Modulating calmodulin binding specificity through computational protein design
    • Shifman J.M., Mayo S.L. Modulating calmodulin binding specificity through computational protein design. J. Mol. Biol. 323:2002;417-423.
    • (2002) J. Mol. Biol. , vol.323 , pp. 417-423
    • Shifman, J.M.1    Mayo, S.L.2
  • 34
    • 0034635349 scopus 로고    scopus 로고
    • Statistical theory of combinatorial libraries of folding proteins: Energetic discrimination of a target structure
    • Zou J., Saven J.G. Statistical theory of combinatorial libraries of folding proteins: energetic discrimination of a target structure. J. Mol. Biol. 296:2000;281-294.
    • (2000) J. Mol. Biol. , vol.296 , pp. 281-294
    • Zou, J.1    Saven, J.G.2
  • 35
    • 0035936702 scopus 로고    scopus 로고
    • Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure
    • Kono H., Saven J.G. Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure. J. Mol. Biol. 306:2001;607-628.
    • (2001) J. Mol. Biol. , vol.306 , pp. 607-628
    • Kono, H.1    Saven, J.G.2
  • 36
    • 0029869187 scopus 로고    scopus 로고
    • Mean-field minimization methods for biological macromolecules
    • Koehl P., Delarue M. Mean-field minimization methods for biological macromolecules. Curr. Opin. Struct. Biol. 6:1996;222-226.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 222-226
    • Koehl, P.1    Delarue, M.2
  • 37
    • 0035957360 scopus 로고    scopus 로고
    • Computational method to reduce the search space for directed protein evolution
    • Voigt C.A., Mayo S.L., Arnold F.H., Wang Z.G. Computational method to reduce the search space for directed protein evolution. Proc. Natl Acad. Sci. USA. 98:2001;3778-3783.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3778-3783
    • Voigt, C.A.1    Mayo, S.L.2    Arnold, F.H.3    Wang, Z.G.4
  • 38
    • 0037460608 scopus 로고    scopus 로고
    • Using self-consistent fields to bias Monte Carlo methods with application to designing and sampling protein sequences
    • Zou J., Saven J.G. Using self-consistent fields to bias Monte Carlo methods with application to designing and sampling protein sequences. J. Chem. Phys. 118:2002;3843-3854.
    • (2002) J. Chem. Phys. , vol.118 , pp. 3843-3854
    • Zou, J.1    Saven, J.G.2
  • 40
  • 41
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • Wallar B.J., Lipscomb J.D. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96:1996;2625-2657.
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 42
    • 0009411657 scopus 로고
    • Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry
    • Feig A.L., Lippard S.J. Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry. Chem. Rev. 94:1994;759-805.
    • (1994) Chem. Rev. , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.J.2
  • 43
    • 0033120905 scopus 로고    scopus 로고
    • Recent advances in the understanding of the biological chemistry of manganese
    • Yocum C.F., Pecoraro V.L. Recent advances in the understanding of the biological chemistry of manganese. Curr. Opin. Chem. Biol. 3:1999;182-187.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 182-187
    • Yocum, C.F.1    Pecoraro, V.L.2
  • 44
    • 0000063535 scopus 로고    scopus 로고
    • Manganese enzymes with binuclear active sites
    • Dismukes G.C. Manganese enzymes with binuclear active sites. Chem. Rev. 96:1996;2909-2926.
    • (1996) Chem. Rev. , vol.96 , pp. 2909-2926
    • Dismukes, G.C.1
  • 45
    • 0037396273 scopus 로고    scopus 로고
    • Di-iron-tyrosyl radical ribonulceotide reductases
    • Stubbe J. Di-iron-tyrosyl radical ribonulceotide reductases. Curr. Opin. Struct. Biol. 7:2003;183-188.
    • (2003) Curr. Opin. Struct. Biol. , vol.7 , pp. 183-188
    • Stubbe, J.1
  • 46
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • Nordlund P., Eklund H. Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 232:1993;123-164.
    • (1993) J. Mol. Biol. , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 47
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • Stubbe J., Riggs-Gelasco P. Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase. Trends Biochem. Sci. 23:1998;438-443.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 48
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins
    • Merkx M., Kopp D.A., Sazinsky M.H., Blazyk J.L., Müller J., Lippard S.J. Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins. Angew. Chem. Int. Ed. 40:2001;2782-2807.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 2782-2807
    • Merkx, M.1    Kopp, D.A.2    Sazinsky, M.H.3    Blazyk, J.L.4    Müller, J.5    Lippard, S.J.6
  • 49
    • 0035819656 scopus 로고    scopus 로고
    • Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site
    • Whittington D.A., Lippard S.J. Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site. J. Am. Chem. Soc. 123:2001;827-838.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 827-838
    • Whittington, D.A.1    Lippard, S.J.2
  • 52
    • 0035956544 scopus 로고    scopus 로고
    • Toward the de novo design of a catalytically active helix-bundle: A substrate accessible carboxylate-bridged dinuclear metal center
    • Di Costanzo L., Wade H., Geremia S., Randaccio L., Pavone V., DeGrado W.F., Lombardi A. Toward the de novo design of a catalytically active helix-bundle: a substrate accessible carboxylate-bridged dinuclear metal center. J. Am. Chem. Soc. 123:2001;12749-12757.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12749-12757
    • Di Costanzo, L.1    Wade, H.2    Geremia, S.3    Randaccio, L.4    Pavone, V.5    Degrado, W.F.6    Lombardi, A.7
  • 53
    • 0037117483 scopus 로고    scopus 로고
    • Noncovalent self-assembly of a heterotetrameric diiron protein
    • Marsh E.N., DeGrado W.F. Noncovalent self-assembly of a heterotetrameric diiron protein. Proc. Natl Acad. Sci. USA. 99:2002;5150-5154.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5150-5154
    • Marsh, E.N.1    Degrado, W.F.2
  • 54
    • 0035800902 scopus 로고    scopus 로고
    • Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
    • Gomes C.M., Le Gall J., Xavier A.V., Teixeira M. Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase? ChemBiochem. 2:2001;583-587.
    • (2001) ChemBiochem , vol.2 , pp. 583-587
    • Gomes, C.M.1    Le Gall, J.2    Xavier, A.V.3    Teixeira, M.4
  • 55
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund P., Sjoberg B., Eklund H. Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature. 345:1990;593-598.
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjoberg, B.2    Eklund, H.3
  • 57
    • 0025974401 scopus 로고
    • Structure of alpha-alpha-hairpins with short connections
    • Efimov A.V. Structure of alpha-alpha-hairpins with short connections. Protein Eng. 4:1991;245-250.
    • (1991) Protein Eng. , vol.4 , pp. 245-250
    • Efimov, A.V.1
  • 58
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 59
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack R.L. Jr, Cohen F.E. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci. 6:1997;1661-1681.
    • (1997) Protein Sci. , vol.6 , pp. 1661-1681
    • Dunbrack Jr., R.L.1    Cohen, F.E.2
  • 60
    • 84988053694 scopus 로고
    • An all atom forcefield for simulations of proteins and nucleic acid
    • Weiner S.J., Kollman P.A., Nguyen D.T., Case D.A. An all atom forcefield for simulations of proteins and nucleic acid. J. Comput. Chem. 7:1986;230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 61
    • 0000382373 scopus 로고    scopus 로고
    • A new method for side-chain conformation prediction using a hopfield network and reproduced rotamers
    • Kono H., Doi J. A new method for side-chain conformation prediction using a hopfield network and reproduced rotamers. J. Comput. Chem. 17:1996;1667-1683.
    • (1996) J. Comput. Chem. , vol.17 , pp. 1667-1683
    • Kono, H.1    Doi, J.2
  • 62
    • 0029155035 scopus 로고
    • Helix design, prediction and stability
    • Munoz V., Serrano L. Helix design, prediction and stability. Curr. Opin. Biotech. 6:1995;382-386.
    • (1995) Curr. Opin. Biotech. , vol.6 , pp. 382-386
    • Munoz, V.1    Serrano, L.2
  • 63
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245:1995;275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 64
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Munoz V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 41:1997;495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 65
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix bundle protein
    • Nagi A.D., Regan L. An inverse correlation between loop length and stability in a four-helix bundle protein. Fold. Des. 2:1997;67-75.
    • (1997) Fold. Des. , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 66
    • 0033548061 scopus 로고    scopus 로고
    • Using loop length variants to dissect the folding pathway of a four-helix-bundle protein
    • Nagi A.D., Anderson K.S., Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein. J. Mol. Biol. 286:1999;257-265.
    • (1999) J. Mol. Biol. , vol.286 , pp. 257-265
    • Nagi, A.D.1    Anderson, K.S.2    Regan, L.3
  • 67
    • 0035059933 scopus 로고    scopus 로고
    • Proton and metal ion-dependent assembly of a model diiron protein
    • Pasternak A., Kaplan J., Lear J.D., Degrado W.F. Proton and metal ion-dependent assembly of a model diiron protein. Protein Sci. 10:2001;958-969.
    • (2001) Protein Sci. , vol.10 , pp. 958-969
    • Pasternak, A.1    Kaplan, J.2    Lear, J.D.3    Degrado, W.F.4
  • 68
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro M.M., Bolen D.W. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry. 31:1992;4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 70
    • 0030592840 scopus 로고    scopus 로고
    • Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites
    • Le Brun N.E., Keech A.M., Mauk M.R., Mauk A.G., Andrews S.C., Thomson A.J., Moore G.R. Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. FEBS Letters. 397:1996;159-163.
    • (1996) FEBS Letters , vol.397 , pp. 159-163
    • Le Brun, N.E.1    Keech, A.M.2    Mauk, M.R.3    Mauk, A.G.4    Andrews, S.C.5    Thomson, A.J.6    Moore, G.R.7
  • 71
    • 0027492116 scopus 로고
    • Unusual clustering of carboxyl side-chains in the core of iron-free ribonucleotide reductase
    • Aberg A., Nordlund P., Eklund H. Unusual clustering of carboxyl side-chains in the core of iron-free ribonucleotide reductase. Nature. 361:1993;276-278.
    • (1993) Nature , vol.361 , pp. 276-278
    • Aberg, A.1    Nordlund, P.2    Eklund, H.3
  • 72
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • G.L. Eichhorn, & L.G. Marzilli. New York: Elsevier
    • Bertini I., Luchinat C. High spin cobalt(II) as a probe for the investigation of metalloproteins. Eichhorn G.L., Marzilli L.G. Advances in Inorganic Biochemistry. 1984;71-111 Elsevier, New York.
    • (1984) Advances in Inorganic Biochemistry , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 74
    • 0018790558 scopus 로고
    • Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotemetry
    • Englander J.J., Calhoun D.B., Englander S.W. Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotemetry. Anal. Biochem. 92:1979;517-524.
    • (1979) Anal. Biochem. , vol.92 , pp. 517-524
    • Englander, J.J.1    Calhoun, D.B.2    Englander, S.W.3
  • 75
    • 0031029551 scopus 로고    scopus 로고
    • Protein design: The choice of de novo sequences
    • Beasley J.R., Hecht M.H. Protein design: the choice of de novo sequences. J. Biol. Chem. 272:1997;2031-2034.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.H.2
  • 77
    • 0028247281 scopus 로고
    • Side-chain entropy and packing in proteins
    • Bromberg S., Dill K.A. Side-chain entropy and packing in proteins. Protein Sci. 3:1994;997-1009.
    • (1994) Protein Sci. , vol.3 , pp. 997-1009
    • Bromberg, S.1    Dill, K.A.2
  • 78
    • 0034901412 scopus 로고    scopus 로고
    • Are proteins well-packed?
    • Liang J., Dill K.A. Are proteins well-packed? Biophys. J. 81:2001;751-766.
    • (2001) Biophys. J. , vol.81 , pp. 751-766
    • Liang, J.1    Dill, K.A.2
  • 79
    • 0035979751 scopus 로고    scopus 로고
    • D(n)-Symmetrical tertiary templates for the design of tubular proteins
    • North B., Summa C.M., Ghirlanda G., DeGrado W.F. D(n)-Symmetrical tertiary templates for the design of tubular proteins. J. Mol. Biol. 311:2001;1081-1090.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1081-1090
    • North, B.1    Summa, C.M.2    Ghirlanda, G.3    Degrado, W.F.4
  • 80
    • 0021757436 scopus 로고
    • A new force field for molecular mechanical simulation of nucleic acids and proteins
    • Weiner S.J., Kollman P.A., Case D.A., Singh U.C., Ghio C., Alagona G., et al. A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc. 106:1984;765-784.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 765-784
    • Weiner, S.J.1    Kollman, P.A.2    Case, D.A.3    Singh, U.C.4    Ghio, C.5    Alagona, G.6
  • 82
    • 0034682869 scopus 로고    scopus 로고
    • Automatic protein design with all atom force-fields by exact and heuristic optimization
    • Wernisch L., Hery S., Wodak S.J. Automatic protein design with all atom force-fields by exact and heuristic optimization. J. Mol. Biol. 301:2000;713-736.
    • (2000) J. Mol. Biol. , vol.301 , pp. 713-736
    • Wernisch, L.1    Hery, S.2    Wodak, S.J.3
  • 83
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge: The Royal Society of Chemistry
    • Laue T., Shaw B.D., Ridgeway T.M., Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;90-125 The Royal Society of Chemistry, Cambridge.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.1    Shaw, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 84
    • 0001330828 scopus 로고
    • Development and use of a mac based data-analysis package for equilibrium sedimentation data from the analytical centrifuge
    • Brooks I.S., Soneson K.K., Hensley P. Development and use of a mac based data-analysis package for equilibrium sedimentation data from the analytical centrifuge. Biophys. J. 64:1993;a244.
    • (1993) Biophys. J. , vol.64 , pp. 244
    • Brooks, I.S.1    Soneson, K.K.2    Hensley, P.3
  • 85
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein?
    • Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein? Protein Sci. 4:1995;2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 86
    • 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
  • 88
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3


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