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Volumn 37, Issue 10, 2004, Pages 754-762

Metal-assembled modular proteins: Toward functional protein design

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEIN; STRUCTURAL PROTEIN;

EID: 6944252206     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar960245+     Document Type: Article
Times cited : (47)

References (88)
  • 2
    • 0032254437 scopus 로고    scopus 로고
    • Hydrophobic Core Packing and Protein Design
    • Lazar, G. A.; Handel, T. M. Hydrophobic Core Packing and Protein Design. Curr. Opin. Chem. Biol. 1998, 2, 675-679.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 675-679
    • Lazar, G.A.1    Handel, T.M.2
  • 5
    • 0035471134 scopus 로고    scopus 로고
    • Enzyme Redesign
    • Penning, J. M.; Jez, J. M. Enzyme Redesign. Chem. Rev. 2001, 101, 3027-3046.
    • (2001) Chem. Rev. , vol.101 , pp. 3027-3046
    • Penning, J.M.1    Jez, J.M.2
  • 7
    • 0035782661 scopus 로고    scopus 로고
    • Review: Protein Design - Where We Were, Where We Are, Where We're Going
    • Pokala, N.; Handel, T. M. Review: Protein Design - Where We Were, Where We Are, Where We're Going. J. Struct. Biol. 2001, 134, 269-281.
    • (2001) J. Struct. Biol. , vol.134 , pp. 269-281
    • Pokala, N.1    Handel, T.M.2
  • 8
    • 0035424416 scopus 로고    scopus 로고
    • Emerging Principles of de Novo Catalyst Design
    • Baltzer, L.; Nilsson, J. Emerging Principles of De Novo Catalyst Design. Curr. Opin. Biotech. 2001, 12, 355-360.
    • (2001) Curr. Opin. Biotech. , vol.12 , pp. 355-360
    • Baltzer, L.1    Nilsson, J.2
  • 9
    • 0035313593 scopus 로고    scopus 로고
    • Improved Biocatalysts by Directed Evolution and Rational Protein Design
    • Bornscheuer, U. T.; Pohl, M. Improved Biocatalysts by Directed Evolution and Rational Protein Design. Curr. Opin. Chem. Biol. 2001, 5, 137-143.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 137-143
    • Bornscheuer, U.T.1    Pohl, M.2
  • 10
    • 0033694923 scopus 로고    scopus 로고
    • De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
    • Hill, R. B.; Raleigh, D. P.; Lombardi, A.; DeGrado, W. F. De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function. Acc. Chem. Res. 2000, 33, 745-754.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 745-754
    • Hill, R.B.1    Raleigh, D.P.2    Lombardi, A.3    DeGrado, W.F.4
  • 11
    • 0032167466 scopus 로고    scopus 로고
    • De Novo Design of Alpha-Helical Coiled Coils and Bundles: Models for the Development of Protein Design Principles
    • Kohn, W. D.; Hodges, R. S. De Novo Design of Alpha-Helical Coiled Coils and Bundles: Models for the Development of Protein Design Principles. Trends Biotechnol. 1998, 16, 379-389.
    • (1998) Trends Biotechnol. , vol.16 , pp. 379-389
    • Kohn, W.D.1    Hodges, R.S.2
  • 12
    • 0038546882 scopus 로고    scopus 로고
    • Design and Characterization of a Homodimeric Antiparallel Coiled Coil
    • Gurnon, D. G.; Whitaker, J. A.; Oakley, M. G. Design and Characterization of a Homodimeric Antiparallel Coiled Coil. J. Am. Chem. Soc. 2003, 125, 7518-7519.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7518-7519
    • Gurnon, D.G.1    Whitaker, J.A.2    Oakley, M.G.3
  • 13
    • 0037864443 scopus 로고    scopus 로고
    • Design and Application of Basic Amino Acids Displaying Enhanced Hydrophobicity
    • Kretsinger, J. K.; Schneider, J. P. Design and Application of Basic Amino Acids Displaying Enhanced Hydrophobicity. J. Am. Chem. Soc. 2003, 125, 7907-7913.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7907-7913
    • Kretsinger, J.K.1    Schneider, J.P.2
  • 14
    • 0041315637 scopus 로고    scopus 로고
    • Clustering of Large Hydrophobes in the Hydrophobic Core of Two-Stranded Alpha-Helical Coiled-Coils Controls Protein Folding and Stability
    • Kwok, S. C.; Hodges, R. S. Clustering of Large Hydrophobes in the Hydrophobic Core of Two-Stranded Alpha-Helical Coiled-Coils Controls Protein Folding and Stability. J. Biol. Chem. 2003, 278, 35248-35254.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35248-35254
    • Kwok, S.C.1    Hodges, R.S.2
  • 15
    • 0035715173 scopus 로고    scopus 로고
    • Designing Heterodimeric Two-Stranded Alpha-Helical Coiled-Coils: The Effect of Chain Length on Protein Folding, Stability and Specificity
    • Litowski, J. R.; Hodges, R. S. Designing Heterodimeric Two-Stranded Alpha-Helical Coiled-Coils: The Effect of Chain Length on Protein Folding, Stability and Specificity. J. Pept. Res. 2001, 58, 477-492.
    • (2001) J. Pept. Res. , vol.58 , pp. 477-492
    • Litowski, J.R.1    Hodges, R.S.2
  • 16
    • 0031746429 scopus 로고    scopus 로고
    • From Coiled Coils to Small Globular Proteins: Design of a Nativelike 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 Nativelike Three-Helix Bundle. Protein Sci. 1998, 7, 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
  • 17
    • 0001141181 scopus 로고
    • A Convergent Approach to Protein Design. Metal-Ion Assisted Spontaneous Self-Assembly of a Polypeptide into a Triple Helix Bundle Protein
    • Ghadiri, M. R.; Soares, C.; Choi, C. A Convergent Approach to Protein Design. Metal-Ion Assisted Spontaneous Self-Assembly of a Polypeptide into a Triple Helix Bundle Protein. J. Am. Chem. Soc. 1992, 114, 825-831.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 825-831
    • Ghadiri, M.R.1    Soares, C.2    Choi, C.3
  • 18
    • 85007885646 scopus 로고
    • Iron(II) Organizes a Synthetic Peptide into 3-Helix Bundles
    • Lieberman, M.; Sasaki, T. Iron(II) Organizes a Synthetic Peptide into 3-Helix Bundles. J. Am. Chem. Soc. 1991, 113, 1470-1471.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1470-1471
    • Lieberman, M.1    Sasaki, T.2
  • 19
    • 0028103524 scopus 로고
    • Dynamic Structure and Potential-Energy Surface of a 3-Helix Bundle Protein
    • Lieberman, M.; Tabet, M.; Sasaki, T. Dynamic Structure and Potential-Energy Surface of a 3-Helix Bundle Protein. J. Am. Chem. Soc. 1994, 116, 5035-5044.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5035-5044
    • Lieberman, M.1    Tabet, M.2    Sasaki, T.3
  • 20
    • 84978150742 scopus 로고    scopus 로고
    • Analysis and Design of Three-Stranded Coiled Coils and Three-Helix Bundles
    • Schneider, J. P.; Lombardi, A.; DeGrado, W. F. Analysis and Design of Three-Stranded Coiled Coils and Three-Helix Bundles. Folding and Design 1998, 3, R29-R40.
    • (1998) Folding and Design , vol.3
    • Schneider, J.P.1    Lombardi, A.2    DeGrado, W.F.3
  • 21
    • 84989506919 scopus 로고
    • Design of an Artificial 4-Helix Bundle Metalloprotein via a Novel Ruthenium(II)-Assisted Self-Assembly Process
    • Ghadiri, M. R.; Soares, C.; Choi, C. Design of an Artificial 4-Helix Bundle Metalloprotein via a Novel Ruthenium(II)-Assisted Self-Assembly Process. J. Am. Chem. Soc. 1992, 114, 4000-4002.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4000-4002
    • Ghadiri, M.R.1    Soares, C.2    Choi, C.3
  • 24
    • 0036903956 scopus 로고    scopus 로고
    • Multifunctional Folded Polypeptides from Peptide Synthesis and Site-Selective Self-Functionalization - Practical Scaffolds in Aqueous Solution
    • Andersson, L. K.; Dolphin, G. T.; Baltzer, L. Multifunctional Folded Polypeptides from Peptide Synthesis and Site-Selective Self-Functionalization - Practical Scaffolds in Aqueous Solution. Chembiochem 2002, 3, 741-751.
    • (2002) Chembiochem , vol.3 , pp. 741-751
    • Andersson, L.K.1    Dolphin, G.T.2    Baltzer, L.3
  • 25
    • 0035100686 scopus 로고    scopus 로고
    • Effects of Charged Amino Acids at b and c Heptad Positions on Specificity and Stability of Four-Chain Coiled Coils
    • Vu, C.; Robblee, J.; Fairman, R. Effects of Charged Amino Acids at b and c Heptad Positions on Specificity and Stability of Four-Chain Coiled Coils. Protein Sci. 2001, 10, 631-637.
    • (2001) Protein Sci. , vol.10 , pp. 631-637
    • Vu, C.1    Robblee, J.2    Fairman, R.3
  • 26
    • 0035109565 scopus 로고    scopus 로고
    • Conformation and Ion Channel Properties of a Five-Helix Bundle Protein
    • De, E.; Chaloin, L.; Heitz, A.; Mery, J.; Molle, G.; Heitz, F. Conformation and Ion Channel Properties of a Five-Helix Bundle Protein. J. Pept. Sci. 2001, 7, 41-49.
    • (2001) J. Pept. Sci. , vol.7 , pp. 41-49
    • De, E.1    Chaloin, L.2    Heitz, A.3    Mery, J.4    Molle, G.5    Heitz, F.6
  • 28
    • 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. 1997, 272, 2031-2034.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.H.2
  • 29
    • 0030878180 scopus 로고    scopus 로고
    • A Protein Designed by Binary Patterning of Polar and Nonpolar Amino Acids Displays Nativelike Properties
    • Roy, S.; Ratnaswamy, G.; Boice, J. A.; Fairman, R.; McLendon, G.; Hecht, M. H. A Protein Designed by Binary Patterning of Polar and Nonpolar Amino Acids Displays Nativelike Properties. J. Am. Chem. Soc. 1997, 119, 5302-5306.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5302-5306
    • Roy, S.1    Ratnaswamy, G.2    Boice, J.A.3    Fairman, R.4    McLendon, G.5    Hecht, M.H.6
  • 30
    • 0142242190 scopus 로고    scopus 로고
    • Letter to the Editor: H-1, C-13 and N-15 Resonance Assignments of S-824, a de Novo Protein from a Designed Combinatorial Library
    • Wei, Y.; Kim, S.; Fela, D.; Baum, J.; Hecht, M. H. Letter to the Editor: H-1, C-13 and N-15 Resonance Assignments of S-824, a De Novo Protein from a Designed Combinatorial Library. J. Biomol. NMR 2003, 27, 395-396.
    • (2003) J. Biomol. NMR , vol.27 , pp. 395-396
    • Wei, Y.1    Kim, S.2    Fela, D.3    Baum, J.4    Hecht, M.H.5
  • 32
    • 0037117483 scopus 로고    scopus 로고
    • Noncovalent Self-Assembly of a Heterotetrameric Diiron Protein
    • Marsh, E. N. G.; DeGrado, W. F. Noncovalent Self-Assembly of a Heterotetrameric Diiron Protein. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 5150-5154.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5150-5154
    • Marsh, E.N.G.1    DeGrado, W.F.2
  • 34
    • 0029113920 scopus 로고
    • Templates in Protein de Novo Design
    • Tuchscherer, G.; Mutter, M. Templates in Protein De Novo Design. J. Biotechnol. 1995, 41, 197-210.
    • (1995) J. Biotechnol. , vol.41 , pp. 197-210
    • Tuchscherer, G.1    Mutter, M.2
  • 35
    • 0000478078 scopus 로고
    • Templates that Induce Alpha-Helical, Beta-Sheet and Loop Conformations
    • Schneider, J. P.; Kelly, J. W. Templates that Induce Alpha-Helical, Beta-Sheet and Loop Conformations. Chem. Rev. 1995, 95, 2169-2187.
    • (1995) Chem. Rev. , vol.95 , pp. 2169-2187
    • Schneider, J.P.1    Kelly, J.W.2
  • 36
    • 0031434205 scopus 로고    scopus 로고
    • Non-Native Architectures in Protein Design and Mimicry
    • Mutter, M.; Tuchscherer, G. Non-Native Architectures in Protein Design and Mimicry. Cell. Mol. Life Sci. 1997, 53, 851-863.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 851-863
    • Mutter, M.1    Tuchscherer, G.2
  • 37
    • 0037184412 scopus 로고    scopus 로고
    • TREN (tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures
    • Kwak, J.; De Capua, A.; Locardi, E.; Goodman, M. TREN (tris(2-aminoethyl)amine): An Effective Scaffold for the Assembly of Triple Helical Collagen Mimetic Structures. J. Am. Chem. Soc. 2002, 124, 14085-14091.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14085-14091
    • Kwak, J.1    De Capua, A.2    Locardi, E.3    Goodman, M.4
  • 38
    • 0037130657 scopus 로고    scopus 로고
    • Structural Characterization of a Paramagnetic Metal-Ion-Assembled Three-Stranded α-Helical Coiled Coil
    • Gochin, M.; Khorosheva, V.; Case, M. A. Structural Characterization of a Paramagnetic Metal-Ion-Assembled Three-Stranded α-Helical Coiled Coil. J. Am. Chem. Soc. 2002, 124, 11018-11028.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11018-11028
    • Gochin, M.1    Khorosheva, V.2    Case, M.A.3
  • 39
  • 40
    • 0033552291 scopus 로고    scopus 로고
    • Structure Determination by Restrained Molecular Dynamics Using NMR Pseudocontact Shifts as Experimentally Determined Constraints
    • Tu, K.; Gochin, M. Structure Determination by Restrained Molecular Dynamics Using NMR Pseudocontact Shifts as Experimentally Determined Constraints. J. Am. Chem. Soc. 1999, 121, 9276-9285.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9276-9285
    • Tu, K.1    Gochin, M.2
  • 41
    • 6944234403 scopus 로고    scopus 로고
    • Applications of Paramagnetic NMR Spectroscopy for Monitoring Transition Metal Complex Stoichiometry and Speciation
    • Crans, D. C.; Yang, L. Q.; Gaidamauskas, E.; Khan, R.; An, W. Z.; Simonis, U. Applications of Paramagnetic NMR Spectroscopy for Monitoring Transition Metal Complex Stoichiometry and Speciation. ACS Symp. Ser. 2003, 858, 304-326.
    • (2003) ACS Symp. Ser. , vol.858 , pp. 304-326
    • Crans, D.C.1    Yang, L.Q.2    Gaidamauskas, E.3    Khan, R.4    An, W.Z.5    Simonis, U.6
  • 42
    • 0001869332 scopus 로고
    • Two-Dimensional NMR Exchange Spectroscopy. Qualitative Treatment of Multisite Exchanging Systems
    • Abel, E. W.; Coston, T. J. P.; Orrell, K. G.; Sik, V.; Stephenson, D. Two-Dimensional NMR Exchange Spectroscopy. Qualitative Treatment of Multisite Exchanging Systems. J. Magn. Reson. 1986, 70, 34-53.
    • (1986) J. Magn. Reson. , vol.70 , pp. 34-53
    • Abel, E.W.1    Coston, T.J.P.2    Orrell, K.G.3    Sik, V.4    Stephenson, D.5
  • 43
    • 0003435322 scopus 로고
    • NMR of Paramagnetic Molecules in Biological Systems
    • Lever, A. B. P.; Gray, H. B., Eds.; Benjamin/Cummins Publishing Co. Inc.: Reading, MA
    • Bertini, I.; Luchinat, C. NMR of Paramagnetic Molecules in Biological Systems. Physical Bioinorganic Chemistry Series; Lever, A. B. P.; Gray, H. B., Eds.; Benjamin/Cummins Publishing Co. Inc.: Reading, MA, 1986; Vol. 3.
    • (1986) Physical Bioinorganic Chemistry Series , vol.3
    • Bertini, I.1    Luchinat, C.2
  • 44
    • 0028900809 scopus 로고
    • Protein-Structure Refinement Based on Paramagnetic NMR shifts - Applications to Wild-Type and Mutant Forms of Cytochrome c
    • Gochin, M.; Roder, H. Protein-Structure Refinement Based on Paramagnetic NMR shifts - Applications to Wild-Type and Mutant Forms of Cytochrome c. Protein Sci. 1995, 4, 296-305.
    • (1995) Protein Sci. , vol.4 , pp. 296-305
    • Gochin, M.1    Roder, H.2
  • 45
    • 0033518594 scopus 로고    scopus 로고
    • De Novo Design of Protein Function: Predictable Structure-Function Relationships in Synthetic Redox Proteins
    • Mutz, M. M.; Case, M. A.; Wishart, J. F.; Ghadiri, M. R.; McLendon, G. L. De Novo Design of Protein Function: Predictable Structure-Function Relationships in Synthetic Redox Proteins. J. Am. Chem. Soc. 1999, 121, 858-859.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 858-859
    • Mutz, M.M.1    Case, M.A.2    Wishart, J.F.3    Ghadiri, M.R.4    McLendon, G.L.5
  • 46
    • 0026434593 scopus 로고
    • Protein Electron-Transfer Rates Set by the Bridging Secondary and Tertiary Structure
    • Beratan, D. N.; Betts, J. N.; Onuchic, J. N. Protein Electron-Transfer Rates Set by the Bridging Secondary and Tertiary Structure. Science 1991, 252, 1285-1288.
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 49
    • 0030806879 scopus 로고    scopus 로고
    • High and Low Resolution Theories of Protein Electron Transfer
    • Skourtis, S. S.; Beratan, D. N. High and Low Resolution Theories of Protein Electron Transfer. J. Biol. Inorg. Chem. 1997, 2, 378-386.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 378-386
    • Skourtis, S.S.1    Beratan, D.N.2
  • 50
    • 0343191086 scopus 로고    scopus 로고
    • Theories of Structure-Function Relationships for Bridge-Mediated Electron-Transfer Reactions
    • Skourtis, S. S.; Beratan, D. N. Theories of Structure-Function Relationships for Bridge-Mediated Electron-Transfer Reactions. Adv. Chem. Phys 1999, 106, 377-452.
    • (1999) Adv. Chem. Phys. , vol.106 , pp. 377-452
    • Skourtis, S.S.1    Beratan, D.N.2
  • 51
    • 0026697272 scopus 로고
    • Electron-Tunneling Pathways in Cytochrome c
    • Wuttke, D. S.; Bjerrum, M. J.; Winkler, J. R.; Gray, H. B. Electron-Tunneling Pathways in Cytochrome c. Science 1992, 256, 1007-1009.
    • (1992) Science , vol.256 , pp. 1007-1009
    • Wuttke, D.S.1    Bjerrum, M.J.2    Winkler, J.R.3    Gray, H.B.4
  • 53
    • 0030744604 scopus 로고    scopus 로고
    • Electron Tunneling in Proteins: Role of the Intervening Medium
    • Winkler J. R.; Gray, H. B. Electron Tunneling in Proteins: Role of the Intervening Medium. J. Biol. Inorg. Chem. 1997, 2, 399-404.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 399-404
    • Winkler, J.R.1    Gray, H.B.2
  • 55
  • 56
    • 0000325019 scopus 로고    scopus 로고
    • Thermodynamic and Structural Effects of a Single Backbone Hydrogen Bond Deletion in a Metal-Assembled Helical Bundle Protein
    • Zhou, J.; Case, M. A.; Wishart, J. F.; McLendon, G. L. Thermodynamic and Structural Effects of a Single Backbone Hydrogen Bond Deletion in a Metal-Assembled Helical Bundle Protein. J. Phys. Chem. 1998, 102, 9975-9980.
    • (1998) J. Phys. Chem. , vol.102 , pp. 9975-9980
    • Zhou, J.1    Case, M.A.2    Wishart, J.F.3    McLendon, G.L.4
  • 57
    • 0041696876 scopus 로고    scopus 로고
    • Do Main Chain Hydrogen Bonds Create Dominant Electron-Transfer Pathways? An Investigation in Designed Proteins
    • Zheng, Y.; Case, M. A.; Wishart, J. F.; McLendon, G. L. Do Main Chain Hydrogen Bonds Create Dominant Electron-Transfer Pathways? An Investigation in Designed Proteins. J. Phys. Chem. B 2003, 107, 7288-7292.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 7288-7292
    • Zheng, Y.1    Case, M.A.2    Wishart, J.F.3    McLendon, G.L.4
  • 60
    • 0030810994 scopus 로고    scopus 로고
    • Biological Electron Tunneling through Native Protein Media
    • Moser, C. C.; Page, C. C.; Chen, X.; Dutton, P. L. Biological Electron Tunneling through Native Protein Media. J. Biol. Inorg. Chem. 1997, 2, 393-398.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 393-398
    • Moser, C.C.1    Page, C.C.2    Chen, X.3    Dutton, P.L.4
  • 61
    • 0042880952 scopus 로고    scopus 로고
    • Multiple versus Single Pathways in Electron Transfer in Proteins: Influence of Protein Dynamics and Hydrogen Bonds
    • Kobayashi, C.; Baldridge, K.; Onuchic, J. N. Multiple versus Single Pathways in Electron Transfer in Proteins: Influence of Protein Dynamics and Hydrogen Bonds. J. Chem. Phys. 2003, 119, 3550-3558.
    • (2003) J. Chem. Phys. , vol.119 , pp. 3550-3558
    • Kobayashi, C.1    Baldridge, K.2    Onuchic, J.N.3
  • 64
    • 0031906349 scopus 로고    scopus 로고
    • Stereoselection in Designed Three-Helix Bundle Metalloproteins
    • Case, M. A.; Ghadiri, M. R.; Mutz, M. M.; McLendon, G. L. Stereoselection in Designed Three-Helix Bundle Metalloproteins. Chirality 1998, 10, 35-40.
    • (1998) Chirality , vol.10 , pp. 35-40
    • Case, M.A.1    Ghadiri, M.R.2    Mutz, M.M.3    McLendon, G.L.4
  • 65
    • 0034705987 scopus 로고    scopus 로고
    • A Virtual Library Approach to Investigate Protein Folding and Internal Packing
    • Case, M. A.; McLendon, G. L. A Virtual Library Approach to Investigate Protein Folding and Internal Packing. J. Am. Chem. Soc. 2000, 122, 8089-8090.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8089-8090
    • Case, M.A.1    McLendon, G.L.2
  • 66
    • 0024438708 scopus 로고
    • Electrospray Ionization for Mass Spectrometry of Large Biomolecules
    • Fenn, J. B.; Mann, M.; Meng, C. K.; Wong, S. F.; Whitehouse, C. M. Electrospray Ionization for Mass Spectrometry of Large Biomolecules. Science 1989, 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 68
    • 0032621297 scopus 로고    scopus 로고
    • Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
    • Hendrickson, C. L.; Emmett, M. R. Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Annu. Rev. Phys. Chem. 1999, 50, 517-536.
    • (1999) Annu. Rev. Phys. Chem. , vol.50 , pp. 517-536
    • Hendrickson, C.L.1    Emmett, M.R.2
  • 69
    • 0032786326 scopus 로고    scopus 로고
    • Electrospray Ionization Fourier Transform Mass Spectrometry of Macromolecules: The First Decade
    • Lorenz, S. A.; Maziarz, E. P. I.; Wood, T. D. Electrospray Ionization Fourier Transform Mass Spectrometry of Macromolecules: The First Decade. Appl. Spectrosc. 1999, 53, 18A-36A.
    • (1999) Appl. Spectrosc. , vol.53
    • Lorenz, S.A.1    Maziarz, E.P.I.2    Wood, T.D.3
  • 70
    • 0031623267 scopus 로고    scopus 로고
    • Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: A Primer
    • Marshall, A. G.; Hendrickson, C. L.; Jackson, G. S. Fourier Transform Ion Cyclotron Resonance Mass Spectrometry: A Primer. Mass Spectrom. Rev. 1998, 17, 1-35.
    • (1998) Mass Spectrom. Rev. , vol.17 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 71
    • 0001268221 scopus 로고
    • Fourier Transform Ion Cyclotron Resonance Spectroscopy
    • Comisarow, M. B.; Marshall, A. G. Fourier Transform Ion Cyclotron Resonance Spectroscopy. Chem. Phys. Lett. 1974, 25, 282-283.
    • (1974) Chem. Phys. Lett. , vol.25 , pp. 282-283
    • Comisarow, M.B.1    Marshall, A.G.2
  • 72
    • 0030621966 scopus 로고    scopus 로고
    • Studying Noncovalent Protein Complexes by Electrospray Ionization Mass Spectrometry
    • Loo, J. A. Studying Noncovalent Protein Complexes by Electrospray Ionization Mass Spectrometry. Mass Spectrom. Rev. 1997, 16, 1-23.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 73
    • 0027657256 scopus 로고
    • The Observation of Noncovalent Interactions in Solution by Electrospray Ionization Mass Spectrometry - Promise, Pitfalls and Prognosis
    • Smith, R. D.; Light-Wahl, K. J. The Observation of Noncovalent Interactions in Solution by Electrospray Ionization Mass Spectrometry - Promise, Pitfalls and Prognosis. Biol. Mass Spectrom. 1993, 22, 493-501.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 493-501
    • Smith, R.D.1    Light-Wahl, K.J.2
  • 75
    • 0034614047 scopus 로고    scopus 로고
    • Dynamic Combinatorial Libraries of Macrocyclic Disulfides in Water
    • Otto, S.; Furlan, R. L. E.; Sanders, J. K. M. Dynamic Combinatorial Libraries of Macrocyclic Disulfides in Water. J. Am. Chem. Soc. 2000, 122, 12063-12064.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12063-12064
    • Otto, S.1    Furlan, R.L.E.2    Sanders, J.K.M.3
  • 76
    • 0038631820 scopus 로고    scopus 로고
    • Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometric Analysis of Metal-Ion Selected Dynamic Protein Libraries
    • Cooper, H. J.; Case, M. A.; McLendon, G. L.; Marshall, A. G. Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometric Analysis of Metal-Ion Selected Dynamic Protein Libraries. J. Am. Chem. Soc. 2003, 125, 5331-5339.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5331-5339
    • Cooper, H.J.1    Case, M.A.2    McLendon, G.L.3    Marshall, A.G.4
  • 77
    • 0027997748 scopus 로고
    • Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing
    • Little, D. P.; Speir, J. P.; Senko, M. W.; O'Connor, P. B.; McLafferty, F. W. Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing. Anal. Chem. 1994, 66, 2809-2815.
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 78
    • 0000944563 scopus 로고    scopus 로고
    • Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
    • Zubarev, R. A.; Kelleher, N. L.; McLafferty, F. W. Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process. J. Am. Chem. Soc. 1998, 120, 3265-3266.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 81
    • 0029974730 scopus 로고    scopus 로고
    • An Engineered Allosteric Switch in Leucine-Zipper Oligomerization
    • Gonzalez, L.; Plecs, J. J.; Alber, T. An Engineered Allosteric Switch in Leucine-Zipper Oligomerization. Nature Struct. Biol. 1996, 3, 510-515.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 510-515
    • Gonzalez, L.1    Plecs, J.J.2    Alber, T.3
  • 82
    • 0026331267 scopus 로고
    • X-ray Structure of the GCN4 Leucine Zipper, a 2-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 2-Stranded, Parallel Coiled Coil. Science 1991, 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.4
  • 83
    • 0028306360 scopus 로고
    • Subdomain Folding of the Coiled-Coil Leucine-Zipper from the Bzip Transcriptional Activator GCN4
    • Lumb, K. J.; Carr, C. M.; Kim, P. S. Subdomain Folding of the Coiled-Coil Leucine-Zipper from the Bzip Transcriptional Activator GCN4. Biochemistry 1994, 33, 7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 84
    • 16944366990 scopus 로고    scopus 로고
    • Buried Polar Residues and Structural Specificity in the GCN4 Leucine Zipper
    • Gonzalez, L. J.; Woolfson, D. N.; Alber, T. Buried Polar Residues and Structural Specificity in the GCN4 Leucine Zipper. Nat. Struct. Biol. 1996, 3, 1011-1018.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzalez, L.J.1    Woolfson, D.N.2    Alber, T.3
  • 85
    • 16944363590 scopus 로고    scopus 로고
    • Crystal Structures of a Single Coiled-Coil Peptide in Two Oligomeric States Reveal the Basis for Structural Polymorphism
    • Gonzalez, L. J.; Brown, R. A.; Richardson, D.; Alber, T. Crystal Structures of a Single Coiled-Coil Peptide in Two Oligomeric States Reveal the Basis for Structural Polymorphism. Nat. Struct. Biol. 1996, 3, 1002-1009.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1002-1009
    • Gonzalez, L.J.1    Brown, R.A.2    Richardson, D.3    Alber, T.4
  • 86
    • 0036893645 scopus 로고    scopus 로고
    • J. Fluorine-NMR Competition Binding Experiments for High-Throughput Screening of Large Compound Mixtures
    • Dalvit, C.; Flocco, M.; Veronesi, M.; Stockman, B. J. Fluorine-NMR Competition Binding Experiments for High-Throughput Screening of Large Compound Mixtures. Comb. Chem. High Throughput Screen 2002, 5, 605-611.
    • (2002) Comb. Chem. High Throughput Screen , vol.5 , pp. 605-611
    • Dalvit, C.1    Flocco, M.2    Veronesi, M.3    Stockman, B.4
  • 87
    • 0024850562 scopus 로고
    • Fluorine Nuclear-Magnetic-Resonance of Fluorinated Ligands
    • Gerig, J. T. Fluorine Nuclear-Magnetic-Resonance of Fluorinated Ligands. Methods Enzymol. 1989, 177, 3-23.
    • (1989) Methods Enzymol. , vol.177 , pp. 3-23
    • Gerig, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.