메뉴 건너뛰기




Volumn 28, Issue 7-9, 2002, Pages 795-815

Photoinduced charge transfer in helical polypeptides

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; ELECTRON TRANSITIONS; HYDROGEN BONDS; PHOTOSYNTHESIS; PROTEINS; REACTION KINETICS; REDOX REACTIONS; THERMODYNAMICS;

EID: 0036960803     PISSN: 09226168     EISSN: None     Source Type: Journal    
DOI: 10.1163/15685670260469429     Document Type: Article
Times cited : (24)

References (102)
  • 2
    • 27844498814 scopus 로고    scopus 로고
    • Electron transfer kinetics of bifunctional redox protein maquettes
    • M. W. Mutz, J. F. Wishart and G. L. Mclendon, Electron transfer kinetics of bifunctional redox protein maquettes, Adv. Chem. Ser. 254, 145-159 (1998).
    • (1998) Adv. Chem. Ser. , vol.254 , pp. 145-159
    • Mutz, M.W.1    Wishart, J.F.2    Mclendon, G.L.3
  • 3
    • 0001374273 scopus 로고    scopus 로고
    • Electron transfer within synthetic polypeptides and de novo designed proteins
    • M. Y. Ogawa, Electron transfer within synthetic polypeptides and de novo designed proteins, Mol. Supramol. Photochem. 4, 113-150 (1999).
    • (1999) Mol. Supramol. Photochem. , vol.4 , pp. 113-150
    • Ogawa, M.Y.1
  • 4
    • 0343148642 scopus 로고
    • Chemical approaches to artificial photosynthesis
    • T. J. Meyer, Chemical Approaches to artificial photosynthesis, Acc. Chem. Res. 22, 163-170 (1989).
    • (1989) Acc. Chem. Res. , vol.22 , pp. 163-170
    • Meyer, T.J.1
  • 5
    • 0040891425 scopus 로고
    • Photoinduced electron transfer in supramolecular systems for artificial photosynthesis
    • M. R. Wasielevski, Photoinduced electron transfer in supramolecular systems for artificial photosynthesis, Chem. Rev. 92, 435-461 (1992).
    • (1992) Chem. Rev. , vol.92 , pp. 435-461
    • Wasielevski, M.R.1
  • 6
    • 11744372773 scopus 로고
    • Molecular mimicry of photosynthetic energy and electron transfer
    • D. Gust, T. A. Moore, and A. L. Moore, Molecular mimicry of photosynthetic energy and electron transfer, Acc. Chem. Res. 26, 198-205 (1983).
    • (1983) Acc. Chem. Res. , vol.26 , pp. 198-205
    • Gust, D.1    Moore, T.A.2    Moore, A.L.3
  • 7
    • 0033694923 scopus 로고    scopus 로고
    • De novo design of helical bundles as models for understanding protein folding and function
    • R. B. Hill, D. P. Raleigh, A. Lombardi and W. F. DeGrado, De novo design of helical bundles as models for understanding protein folding and function, Acc. Chem. Res. 33, 745-754 (2000).
    • (2000) Acc. Chem. Res. , vol.33 , pp. 745-754
    • Hill, R.B.1    Raleigh, D.P.2    Lombardi, A.3    Degrado, W.F.4
  • 8
    • 0030840469 scopus 로고    scopus 로고
    • Protein design: Proteins from scratch
    • W. F. DeGrado, Protein design: Proteins from scratch, Science 278, 80-81 (1997).
    • (1997) Science , vol.278 , pp. 80-81
    • Degrado, W.F.1
  • 9
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • M. D. Struthers, R. P. Cheng and B. Imperiali, Design of a monomeric 23-residue polypeptide with defined tertiary structure, Science 271, 342-345 (1996).
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 10
    • 0027245441 scopus 로고
    • A single-stranded amphipathic α-helix in aqueous solution: Design, structural characterization, and its application for determining α-helical propensities of amino acids
    • N. E. Zhou, C. M. Kay, B. D. Sykes and R. S. Hodges, A single-stranded amphipathic α-helix in aqueous solution: Design, structural characterization, and its application for determining α-helical propensities of amino acids, Biochemistry 32, 6190-6197 (1993).
    • (1993) Biochemistry , vol.32 , pp. 6190-6197
    • Zhou, N.E.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4
  • 11
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • D. L. Minor, Jr. and P. S. Kim, Context-dependent secondary structure formation of a designed protein sequence, Nature 380, 730-734 (1996).
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor D.L., Jr.1    Kim, P.S.2
  • 12
    • 0034705987 scopus 로고    scopus 로고
    • A virtual library approach to investigate protein folding and internal packing
    • M. A. Case and G. L. McLendon, A virtual library approach to investigate protein folding and internal packing, J. Am. Chem. Soc. 122, 8089-8090 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8089-8090
    • Case, M.A.1    McLendon, G.L.2
  • 13
    • 0032582723 scopus 로고    scopus 로고
    • Photosynthetic reaction centers
    • J. P. Allen, and J. C. Williams, Photosynthetic reaction centers, FEBS Lett. 438, 5-9 (1998).
    • (1998) FEBS Lett. , vol.438 , pp. 5-9
    • Allen, J.P.1    Williams, J.C.2
  • 15
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber and H. Michel, Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution, Nature 318, 618-624 (1986).
    • (1986) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 16
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber and H. Michel, X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis, J. Mol. Biol. 180, 385-398 (1984).
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 17
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • P. Jordan, P. Fromme, H. T. Witt, O. Klukas, W. Saenger and N. Krauß, Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution, Nature 411, 909-917 (2001).
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauß, N.6
  • 18
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction center at 8 Å resolution
    • K.-H. Rhee, E. P. Morris, J. Barber and W. Kühlbrandt, Three-dimensional structure of the plant photosystem II reaction center at 8 Å resolution, Nature 396, 283 (1998).
    • (1998) Nature , vol.396 , pp. 283
    • Rhee, K.-H.1    Morris, E.P.2    Barber, J.3    Kühlbrandt, W.4
  • 19
    • 0034663537 scopus 로고    scopus 로고
    • Re-emerging structures: Continuing crystallography of the bacterial reaction center
    • P. K. Fyfe and M. R. Jones, Re-emerging structures: continuing crystallography of the bacterial reaction center, Biochim. Biophys. Acta 1459, 413-421 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 413-421
    • Fyfe, P.K.1    Jones, M.R.2
  • 20
    • 0025790423 scopus 로고
    • Structures of bacterial photosynthetic reaction centers
    • J. Deisenhofer and H. Michel, Structures of bacterial photosynthetic reaction centers, Annu. Rev. Cell Biol. 7, 1-23 (1991).
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 1-23
    • Deisenhofer, J.1    Michel, H.2
  • 21
    • 0001649143 scopus 로고
    • Site-directed mutagenesis of photosynthetic reaction centers
    • B. A. Diner, P. J. Nixon and J. W. Farchaus, Site-directed mutagenesis of photosynthetic reaction centers, Curr. Opin. Struct. Biol. 1, 546-554 (1991).
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 546-554
    • Diner, B.A.1    Nixon, P.J.2    Farchaus, J.W.3
  • 22
    • 0029647453 scopus 로고
    • Control of electron transfer between the L- and M-sides of photosynthetic reaction centers
    • B. Heller, D. Holten and C. Kirmaier, Control of electron transfer between the L- and M-sides of photosynthetic reaction centers, Science 269, 940-945 (1995).
    • (1995) Science , vol.269 , pp. 940-945
    • Heller, B.1    Holten, D.2    Kirmaier, C.3
  • 23
    • 0029794447 scopus 로고    scopus 로고
    • Site-directed mutations affecting the spectroscopic characteristics and midpoint potential of the primary donor in photosystem I
    • A. N. Webber, H. Su, S. E. Bingham, H. Käss, L. Krabben, M. Kuhn, R. Jordan, E. Schlodder and W. Lubitz, Site-directed mutations affecting the spectroscopic characteristics and midpoint potential of the primary donor in photosystem I, Biochemistry 35, 12857-12863 (1996).
    • (1996) Biochemistry , vol.35 , pp. 12857-12863
    • Webber, A.N.1    Su, H.2    Bingham, S.E.3    Käss, H.4    Krabben, L.5    Kuhn, M.6    Jordan, R.7    Schlodder, E.8    Lubitz, W.9
  • 24
    • 0027519330 scopus 로고
    • Kinetics and free energy gaps of electrontransfer reactions in Rhodobacter sphaeroides reaction centers
    • V. Nagarajan, W. Parson, D. Davis and C. C. Schenck, Kinetics and free energy gaps of electrontransfer reactions in Rhodobacter sphaeroides reaction centers, Biochemistry 32, 12324-12326 (1993).
    • (1993) Biochemistry , vol.32 , pp. 12324-12326
    • Nagarajan, V.1    Parson, W.2    Davis, D.3    Schenck, C.C.4
  • 25
    • 0025196834 scopus 로고
    • Role of tyrosine M210 in the initial charge separation of reaction centers of Rhodobacter sphaeroides
    • U. Finkele, C. Lauterwasser, W. Zinth, K. A. Gray and D. Oesterhelt, Role of tyrosine M210 in the initial charge separation of reaction centers of Rhodobacter sphaeroides, Biochemistry 29, 8517-8521 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8517-8521
    • Finkele, U.1    Lauterwasser, C.2    Zinth, W.3    Gray, K.A.4    Oesterhelt, D.5
  • 26
    • 0028920636 scopus 로고
    • Characterization of bacterial reaction centers having mutations of aromatic residues in the binding site of the bacteriopheophytin intermediary electron carrier
    • B. Heller, D. Holten and C. Kirmaier, Characterization of bacterial reaction centers having mutations of aromatic residues in the binding site of the bacteriopheophytin intermediary electron carrier, Biochemistry 34, 5294-5302 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5294-5302
    • Heller, B.1    Holten, D.2    Kirmaier, C.3
  • 27
    • 0027245419 scopus 로고
    • Mutations designed to modify the environment of the primary electron donor of the reaction center from Rhodobacter sphaeroides: Phenylalanine to leucine at L167 and histidine to phenylalanine at L 168
    • H. A. Murchison, J. P. Alden, J. M. Peloquin, A. K. W. Taguchi, N. W. Woodbury and J. C. Williams, Mutations designed to modify the environment of the primary electron donor of the reaction center from Rhodobacter sphaeroides: Phenylalanine to leucine at L167 and histidine to phenylalanine at L 168, Biochemistry 32, 3498-3505 (1993).
    • (1993) Biochemistry , vol.32 , pp. 3498-3505
    • Murchison, H.A.1    Alden, J.P.2    Peloquin, J.M.3    Taguchi, A.K.W.4    Woodbury, N.W.5    Williams, J.C.6
  • 28
    • 0025907020 scopus 로고
    • Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin
    • C. Kirmaier, D. Gaul, R. DeBey, D. Holten and C. C. Schenck, Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin, Science 251, 992-927 (1991).
    • (1991) Science , vol.251 , pp. 992-927
    • Kirmaier, C.1    Gaul, D.2    DeBey, R.3    Holten, D.4    Schenck, C.C.5
  • 30
    • 0034841829 scopus 로고    scopus 로고
    • Structural basis of bacterial photosynthetic reaction centers
    • T. Nogi and K. Miki, Structural basis of bacterial photosynthetic reaction centers, J. Biochem. 130, 319-329 (2001).
    • (2001) J. Biochem. , vol.130 , pp. 319-329
    • Nogi, T.1    Miki, K.2
  • 31
    • 0002654528 scopus 로고
    • Photochemical reaction centers: Structure, organization, and function
    • A. N. Glazer and A. Melis, Photochemical reaction centers: structure, organization, and function, Annu. Rev. Plant Physiol. 38, 11-45 (1987).
    • (1987) Annu. Rev. Plant Physiol. , vol.38 , pp. 11-45
    • Glazer, A.N.1    Melis, A.2
  • 32
    • 0023055079 scopus 로고
    • Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: Characterization and reconstitution with iron(2+), manganese(2+), cobalt(2+), nickel(2+), copper(2+), and zinc(2+)
    • R. J. Debus, G. Feher and M. Y. Okamura, Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: characterization and reconstitution with iron(2+), manganese(2+), cobalt(2+), nickel(2+), copper(2+), and zinc(2+), Biochemistry 25, 2276-2287 (1986).
    • (1986) Biochemistry , vol.25 , pp. 2276-2287
    • Debus, R.J.1    Feher, G.2    Okamura, M.Y.3
  • 33
    • 0021871803 scopus 로고
    • LM complex of reaction centers from Rhodopseudomonas sphaeroides R-26: Characterization and reconstitution with the H subunit
    • R. J. Debus, G. Feher and M. Y. Okamura, LM complex of reaction centers from Rhodopseudomonas sphaeroides R-26: characterization and reconstitution with the H subunit, Biochemistry 24, 2488-2500 (1985).
    • (1985) Biochemistry , vol.24 , pp. 2488-2500
    • Debus, R.J.1    Feher, G.2    Okamura, M.Y.3
  • 34
    • 0000595922 scopus 로고
    • Evidence that a chlorophyll a' dimer constitutes the photochemical reaction center 1 (P700) in photosynthetic apparatus
    • T. Watanabe, M. Kobayashi, A. Hongu and T. Hiyama, Evidence that a chlorophyll a' dimer constitutes the photochemical reaction center 1 (P700) in photosynthetic apparatus, FEBS Lett. 235, 252-256 (1985).
    • (1985) FEBS Lett. , vol.235 , pp. 252-256
    • Watanabe, T.1    Kobayashi, M.2    Hongu, A.3    Hiyama, T.4
  • 36
    • 0033034893 scopus 로고    scopus 로고
    • New and unexpected routes for ultrafast electron transfer in photosynthetic reaction centers
    • M. E. van Brederode and R. van Grondelle, New and unexpected routes for ultrafast electron transfer in photosynthetic reaction centers, FEBS Lett. 455, 1-7 (1999).
    • (1999) FEBS Lett. , vol.455 , pp. 1-7
    • Van Brederode, M.E.1    Van Grondelle, R.2
  • 37
    • 0000018906 scopus 로고    scopus 로고
    • The first events in photosynthesis: Electronic coupling and energy transfer dynamics in the photosynthetic reaction center from Rhodobacter sphaeroides
    • D. C. Arnett, C. C. Moser, P. L. Dutton and N. F. Scherer, The first events in photosynthesis: Electronic coupling and energy transfer dynamics in the photosynthetic reaction center from Rhodobacter sphaeroides, J. Phys. Chem. B 103, 2014-2032 (1999).
    • (1999) J. Phys. Chem. B , vol.103 , pp. 2014-2032
    • Arnett, D.C.1    Moser, C.C.2    Dutton, P.L.3    Scherer, N.F.4
  • 38
    • 0000645088 scopus 로고
    • Subpicosecond transient absorption difference spectroscopy on the reaction center of photosystem II: Radical pair formation at 77 K
    • H. M. Visser, M. L. Groot, F. van Mourik, I. H. M. van Stokkum, J. P. Dekker and R. van Grondelle, Subpicosecond transient absorption difference spectroscopy on the reaction center of photosystem II: Radical pair formation at 77 K, J. Phys. Chem. 99, 15304-15309 (1995).
    • (1995) J. Phys. Chem. , vol.99 , pp. 15304-15309
    • Visser, H.M.1    Groot, M.L.2    Van Mourik, F.3    Van Stokkum, I.H.M.4    Dekker, J.P.5    Van Grondelle, R.6
  • 39
    • 0029647453 scopus 로고
    • Control of electron transfer between the L- and M-sides of photosynthetic reaction centers
    • B. Heller, D. Holten and C. Kirmaier, Control of electron transfer between the L- and M-sides of photosynthetic reaction centers, Science 269, 940-945 (1995).
    • (1995) Science , vol.269 , pp. 940-945
    • Heller, B.1    Holten, D.2    Kirmaier, C.3
  • 40
    • 0031015412 scopus 로고    scopus 로고
    • Electron transfer and arrangement of the redox cofactors in photosystem I
    • K. Brettel, Electron transfer and arrangement of the redox cofactors in photosystem I., Biochim. Biophys. Acta 1318, 322-373 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 322-373
    • Brettel, K.1
  • 42
    • 0033600564 scopus 로고    scopus 로고
    • In vivo analysis of the electron transfer within photosystem I: Are the two phylloquinones involved?
    • P. Joliot and A. Joliot, In vivo analysis of the electron transfer within photosystem I: Are the two phylloquinones involved? Biochemistry 38, 11130-11136 (1999).
    • (1999) Biochemistry , vol.38 , pp. 11130-11136
    • Joliot, P.1    Joliot, A.2
  • 43
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • R. A. Marcus and N. Sutin, Electron transfers in chemistry and biology, Biochim. Biophys. Acta 811, 265-322 (1985).
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 44
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • C. W. Hoganson and G. T. Tabcock, A metalloradical mechanism for the generation of oxygen from water in photosynthesis, Science 277, 1953-1956 (1997).
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1    Tabcock, G.T.2
  • 45
    • 0035148647 scopus 로고    scopus 로고
    • Mimicking photosynthetic solar energy transduction
    • D. Gust, T. A. Moore and A. L. Moore, Mimicking photosynthetic solar energy transduction, Acc. Chem. Res. 34, 40-48 (2001).
    • (2001) Acc. Chem. Res. , vol.34 , pp. 40-48
    • Gust, D.1    Moore, T.A.2    Moore, A.L.3
  • 46
    • 0001623020 scopus 로고    scopus 로고
    • Mimicking bacterial photosynthesis
    • D. Gust, T. A. Moore and A. L. Moore, Mimicking bacterial photosynthesis, Pure Appl. Chem. 70, 2189-2200 (1998).
    • (1998) Pure Appl. Chem. , vol.70 , pp. 2189-2200
    • Gust, D.1    Moore, T.A.2    Moore, A.L.3
  • 47
    • 0031033975 scopus 로고    scopus 로고
    • Conversion of light energy to proton potential in liposomes by artificial photosynthetic reaction centers
    • G. Steinberg-Yfrach, P. A. Liddell, S.-C. Hung, A. L. Moore, D. Gust and T. A. Moore, Conversion of light energy to proton potential in liposomes by artificial photosynthetic reaction centers, Nature 385, 239-241 (1997).
    • (1997) Nature , vol.385 , pp. 239-241
    • Moore, G.1    Steinberg-Yfrach, P.A.2    Liddell, S.-C.3    Hung, A.L.4    Gust, D.5    Moore, T.A.6
  • 49
    • 0025368499 scopus 로고
    • Electrostatic control of charge separation in bacterial photosynthesis
    • W. Parson, Z. T. Chu and A. Warshel, Electrostatic control of charge separation in bacterial photosynthesis, Biochim. Biophys. Acta 1017, 251-272 (1990).
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 251-272
    • Parson, W.1    Chu, Z.T.2    Warshel, A.3
  • 50
    • 0030859221 scopus 로고    scopus 로고
    • Electric field effects on electron transfer rates in dichromophoric peptides: The effect of helix unfolding
    • M. A. Fox and E. Galoppini, Electric field effects on electron transfer rates in dichromophoric peptides: The effect of helix unfolding, J. Am. Chem. Soc. 119, 5277-5285 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5277-5285
    • Fox, M.A.1    Galoppini, E.2
  • 51
    • 0029931828 scopus 로고    scopus 로고
    • Effect of the electric field generated by the helix dipole on photoinduced intramolecular electron transfer in dichromophoric α-helical peptides
    • E. Galoppini and M. A. Fox, Effect of the electric field generated by the helix dipole on photoinduced intramolecular electron transfer in dichromophoric α-helical peptides, J. Am. Chem. Soc. 118, 2299-2300 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2299-2300
    • Galoppini, E.1    Fox, M.A.2
  • 52
    • 0000380201 scopus 로고    scopus 로고
    • Photoinduced intramolecular electron transfer in dichromophore-appended α-helical peptides: Spectroscopic properties and preferred conformations
    • A. Knorr, E. Galoppini and M. A. Fox, Photoinduced intramolecular electron transfer in dichromophore-appended α-helical peptides: spectroscopic properties and preferred conformations, J. Phys. Org. Chem. 10, 484 (1997).
    • (1997) J. Phys. Org. Chem. , vol.10 , pp. 484
    • Knorr, A.1    Galoppini, E.2    Fox, M.A.3
  • 53
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • W. G. J. Hol, The role of the α-helix dipole in protein function and structure, Prog. Biophys. Mol. Biol. 45, 149-195 (1985).
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.J.1
  • 54
    • 0032835617 scopus 로고    scopus 로고
    • De novo design and structural characterization of proteins and metalloproteins
    • W. F. DeGrado, C. M. Summa, V. Pavone, F. Nastri and A. Lombardi, De novo design and structural characterization of proteins and metalloproteins, Annu. Rev. Biochem. 68, 779-819 (1999).
    • (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
  • 55
    • 0030345054 scopus 로고
    • De novo design of α-helical proteins: Basic research to medical applications
    • Boehringer Mannheim Award Lecture 1995/La conference Boehringer Mannheim
    • R. S. Hodges, Boehringer Mannheim Award Lecture 1995/La conference Boehringer Mannheim 1995. De novo design of α-helical proteins: basic research to medical applications, Biochem. Cell Biol. 74, 133-154 (1996).
    • (1995) Biochem. Cell Biol. , vol.74 , pp. 133-154
    • Hodges, R.S.1
  • 57
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • W. F. DeGrado, Z. R. Wasserman and J. D. Lear, Protein design, a minimalist approach, Science 243, 622-628 (1989).
    • (1989) Science , vol.243 , pp. 622-628
    • DeGrado, W.F.1    Wasserman, Z.R.2    Lear, J.D.3
  • 58
    • 0027756896 scopus 로고
    • A switch between two-, three-, and fourstranded coiled coils in GCN4 leucine zipper mutants
    • P. B. Harbury, T. Zhang, P. S. Kim and T. Alber, A switch between two-, three-, and fourstranded coiled coils in GCN4 leucine zipper mutants, Science 262, 1401-1407 (1993).
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 59
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • D. L. Akey, V. N. Malashkevich and P. S. Kim, Buried polar residues in coiled-coil interfaces, Biochemistry 40, 6352-6360 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 60
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • K. J. Lumb and P. S. Kim, Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper, Science 268, 436-439 (1995).
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 61
    • 0000236570 scopus 로고
    • Peptide 'Velcro': Design of a heterodimeric coiled coil
    • E. K. O'Shea, K. J. Lumb and P. S. Kim, Peptide 'Velcro': design of a heterodimeric coiled coil, Curr. Biol. 3, 658-667 (1993).
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 62
    • 0033549080 scopus 로고    scopus 로고
    • A fluorescence assay for leucine zipper dimerization: Avoiding unintended consequences of fluorophore attachment
    • D. L. Daugherty and S. H. Gellman, A fluorescence assay for leucine zipper dimerization: Avoiding unintended consequences of fluorophore attachment, J. Am. Chem. Soc. 121, 4325-4333 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4325-4333
    • Daugherty, D.L.1    Gellman, S.H.2
  • 63
    • 0035833701 scopus 로고    scopus 로고
    • Contribution of a pyrene fluorescence probe to the aggregation propensity of polypeptides
    • G. Jones, II and V. I. Vullev, Contribution of a pyrene fluorescence probe to the aggregation propensity of polypeptides, Org. Lett. 3, 2457-2460 (2001).
    • (2001) Org. Lett. , vol.3 , pp. 2457-2460
    • Jones G. II1    Vullev, V.I.2
  • 64
    • 0000141002 scopus 로고    scopus 로고
    • Engineering oriented heme protein maquette monolayers through surface residue charge distribution patterns
    • X. Chen, C. C. Moser, D. L. Pilloud, B. R. Gibney and P. L. Dutton, Engineering oriented heme protein maquette monolayers through surface residue charge distribution patterns, J. Phys. Chem. B 103, 9029-9037 (1999).
    • (1999) J. Phys. Chem. B , vol.103 , pp. 9029-9037
    • Chen, X.1    Moser, C.C.2    Pilloud, D.L.3    Gibney, B.R.4    Dutton, P.L.5
  • 65
  • 66
    • 0032577018 scopus 로고    scopus 로고
    • A native-like threeα-helix bundle protein from structure-based redesign: A novel maquette scaffold
    • J. S. Johansson, B. R. Gibney, J. J. Skalicky, A. J. Wand and P. L. Dutton, A native-like threeα-helix bundle protein from structure-based redesign: A novel maquette scaffold, J. Am. Chem. Soc. 120, 3881-3886 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3881-3886
    • Johansson, J.S.1    Gibney, B.R.2    Skalicky, J.J.3    Wand, A.J.4    Dutton, P.L.5
  • 67
    • 0030878180 scopus 로고    scopus 로고
    • A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties
    • S. Roy, G. Ratnaswamy, J. A. Boice, R. Fairman, G. McLendon and M. H. Hecht, A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties, J. Am. Chem. Soc. 119, 5302-5306 (1997).
    • (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
  • 68
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • N. J. Greenfield and G. D. Fasman, Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116 (1969).
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.D.2
  • 69
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Y.-H. Chen, J. T. Yang and K. H. Chau, Determination of the helix and β form of proteins in aqueous solution by circular dichroism, Biochemistry 13, 3350-3359 (1974).
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 70
    • 0000206550 scopus 로고
    • Determination of the molecular weights of membrane proteins and polypeptides
    • W. W. Fish, Determination of the molecular weights of membrane proteins and polypeptides, Methods Membr. Biol. 4, 189-276 (1975).
    • (1975) Methods Membr. Biol. , vol.4 , pp. 189-276
    • Fish, W.W.1
  • 72
    • 84991138979 scopus 로고
    • Kinetics of fluorescence quenching by electron and hydrogen-atom transfer
    • D. Rehm and A. Weller, Kinetics of fluorescence quenching by electron and hydrogen-atom transfer, Israel J. Chem. 8, 259-271 (1970).
    • (1970) Israel J. Chem. , vol.8 , pp. 259-271
    • Rehm, D.1    Weller, A.2
  • 73
    • 0033410470 scopus 로고    scopus 로고
    • Photoinduced electron transfer in molecular systems: Recent developments
    • P. Piotrowiak, Photoinduced electron transfer in molecular systems: recent developments, Chem. Soc. Rev. 28, 143-150 (1999).
    • (1999) Chem. Soc. Rev. , vol.28 , pp. 143-150
    • Piotrowiak, P.1
  • 74
    • 85050425247 scopus 로고    scopus 로고
    • Elementary photoprocesses in designed chromophore sequence on α-helical polypeptides
    • M. Sisido, Elementary photoprocesses in designed chromophore sequence on α-helical polypeptides, Adv. Photochem. 22, 197-228 (1997).
    • (1997) Adv. Photochem. , vol.22 , pp. 197-228
    • Sisido, M.1
  • 76
    • 0343072870 scopus 로고    scopus 로고
    • A spectroscopic and structural investigation on model compounds of biomimetic systems in solution
    • B. Pispisa, A. Palleschi, M. Venanzi, G. Zanotti and L. Stella, A spectroscopic and structural investigation on model compounds of biomimetic systems in solution, Photochem. Photobiol. 3, 11-34 (1999).
    • (1999) Photochem. Photobiol. , vol.3 , pp. 11-34
    • Pispisa, B.1    Palleschi, A.2    Venanzi, M.3    Zanotti, G.4    Stella, L.5
  • 77
    • 0031592339 scopus 로고    scopus 로고
    • Influence of secondary structure on the decay kinetics of fluorescent donor-acceptor labeled peptides
    • G. Hungerford, F. Donald, D. J. S. Birch and B. D. Moore, Influence of secondary structure on the decay kinetics of fluorescent donor-acceptor labeled peptides, Biosens. Bioelectron. 12, 1183-1190 (1997).
    • (1997) Biosens. Bioelectron. , vol.12 , pp. 1183-1190
    • Hungerford, G.1    Donald, F.2    Birch, D.J.S.3    Moore, B.D.4
  • 78
    • 0002807377 scopus 로고    scopus 로고
    • Site-specific modification of a-helical peptides with electron donors and acceptors
    • B. I. Dahiyat, T. J. Meade and S. L. Mayo, Site-specific modification of a-helical peptides with electron donors and acceptors, Inorg. Chim. Acta 243, 207-212 (1996).
    • (1996) Inorg. Chim. Acta , vol.243 , pp. 207-212
    • Dahiyat, B.I.1    Meade, T.J.2    Mayo, S.L.3
  • 79
    • 0000245465 scopus 로고
    • New perspectives on long-range electron transfer in conformationally organized peptides and electron-transfer proteins: An experimental approach
    • S. S. Isied, I. Moreira, J. F. Wishart, M. Y. Ogawa, A. Vassilian, B. Arbo and J. Sun, New perspectives on long-range electron transfer in conformationally organized peptides and electron-transfer proteins: an experimental approach, J. Photochem. Photobiol. A 82, 203-210 (1994).
    • (1994) J. Photochem. Photobiol. A , vol.82 , pp. 203-210
    • Isied, S.S.1    Moreira, I.2    Wishart, J.F.3    Ogawa, M.Y.4    Vassilian, A.5    Arbo, B.6    Sun, J.7
  • 80
    • 0011051660 scopus 로고
    • Photoinduced electron transfer in a single α-helical polypeptide chain: Evidence of a through-space mechanism
    • Y. Inai, M. Sisido and Y. Imanishi, Photoinduced electron transfer in a single α-helical polypeptide chain: evidence of a through-space mechanism, J. Phys. Chem. 95, 3847-3851 (1991).
    • (1991) J. Phys. Chem. , vol.95 , pp. 3847-3851
    • Inai, Y.1    Sisido, M.2    Imanishi, Y.3
  • 83
    • 0007758337 scopus 로고
    • Peptide-mediated intramolecular electron transfer: Long-range distance dependence
    • S. S. Isied, M. Y. Ogawa and J. F. Wishart, Peptide-mediated intramolecular electron transfer: Long-range distance dependence, Chem. Rev. 92, 381-394 (1992).
    • (1992) Chem. Rev. , vol.92 , pp. 381-394
    • Isied, S.S.1    Ogawa, M.Y.2    Wishart, J.F.3
  • 84
    • 0000670923 scopus 로고
    • The structure of poly-L-proline
    • P. M. Cowan and S. McGavin, The structure of poly-L-proline, Nature 176, 501-503 (1955).
    • (1955) Nature , vol.176 , pp. 501-503
    • Cowan, P.M.1    McGavin, S.2
  • 85
    • 0000316625 scopus 로고
    • Structure of poly-L-proline I
    • W. Traub and U. Shmueli, Structure of poly-L-proline I, Nature 198, 1165-1166 (1963).
    • (1963) Nature , vol.198 , pp. 1165-1166
    • Traub, W.1    Shmueli, U.2
  • 86
    • 0012729496 scopus 로고
    • The mutarotation of poly(L-proline)
    • A. R. Downie and A. A. Randall, The mutarotation of poly(L-proline), Trans. Faraday Soc. 55, 2132-2140 (1959).
    • (1959) Trans. Faraday Soc. , vol.55 , pp. 2132-2140
    • Downie, A.R.1    Randall, A.A.2
  • 87
    • 0033518594 scopus 로고    scopus 로고
    • De novo design of protein function: Predictable structure-function relationships in synthetic redox protein
    • M. W. Mutz, M. A. Case, J. F. Wishart, M. R. Ghadiri and G. L. McLendon, De novo design of protein function: Predictable structure-function relationships in synthetic redox protein, J. Am. Chem. Soc. 121, 858-859 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 858-859
    • Mutz, M.W.1    Case, M.A.2    Wishart, J.F.3    Ghadiri, M.R.4    McLendon, G.L.5
  • 90
    • 0030828321 scopus 로고    scopus 로고
    • Electron transfer across a peptide-peptide interface within a designed metalloprotein
    • G. V. Kozlov and M. Y. Ogawa, Electron Transfer across a Peptide-Peptide interface within a designed metalloprotein, J. Am. Chem. Soc. 119, 8377-8378 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8377-8378
    • Kozlov, G.V.1    Ogawa, M.Y.2
  • 92
    • 0035833977 scopus 로고    scopus 로고
    • Effect of surface charges on the rates of intermolecular electron-transfer between de novo designed metalloproteins
    • A. Y. Kornilova, J. F. Wishar and M. Y. Ogawa, Effect of surface charges on the rates of intermolecular electron-transfer between de novo designed metalloproteins, Biochemistry 40, 12186-12192 (2001).
    • (2001) Biochemistry , vol.40 , pp. 12186-12192
    • Kornilova, A.Y.1    Wishar, J.F.2    Ogawa, M.Y.3
  • 93
    • 0036007603 scopus 로고    scopus 로고
    • Site-specific modification of de novo designed coiled-coil polypeptides with inorganic redox complexes
    • A. Fedorova and M. Y. Ogawa, Site-specific modification of de novo designed coiled-coil polypeptides with inorganic redox complexes, Bioconjugate Chemistry 13, 150-154 (2002).
    • (2002) Bioconjugate Chemistry , vol.13 , pp. 150-154
    • Fedorova, A.1    Ogawa, M.Y.2
  • 94
    • 0033984117 scopus 로고    scopus 로고
    • Multistep photoinduced electron transfer in a de novo helix bundle. Multimer self-assembly of peptide chains including a chromophore special pair
    • G. Jones, II, V. I. Vullev, E. Braswell and D. Zhu, Multistep photoinduced electron transfer in a de novo helix bundle. Multimer self-assembly of peptide chains including a chromophore special pair, J. Am. Chem. Soc. 122, 388-389 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 388-389
    • Jones G. II1    Vullev, V.I.2    Braswell, E.3    Zhu, D.4
  • 95
    • 0035812136 scopus 로고    scopus 로고
    • Ground- and excited-state aggregation properties of a pyrene derivative in aqueous media
    • G. Jones, II, V. I. Vullev, Ground- and excited-state aggregation properties of a pyrene derivative in aqueous media, J. Phys. Chem. A 105, 6402-6406 (2001).
    • (2001) J. Phys. Chem. A , vol.105 , pp. 6402-6406
    • Jones G. II1    Vullev, V.I.2
  • 98
    • 0030066841 scopus 로고    scopus 로고
    • Toward the synthesis of a photosynthetic reaction center maquette: A cofacial porphyrin pair assembled between two subunits of a synthetic four-helix bundle multiheme protein
    • F. Rabanal, W. F. DeGrado and P. L. Dutton, Toward the synthesis of a photosynthetic reaction center maquette: A cofacial porphyrin pair assembled between two subunits of a synthetic four-helix bundle multiheme protein, J. Am. Chem. Soc. 118, 473-474 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 473-474
    • Rabanal, F.1    DeGrado, W.F.2    Dutton, P.L.3
  • 100
  • 102
    • 0012622003 scopus 로고    scopus 로고
    • This paper is No. 12 in the series
    • This paper is No. 12 in the series, Photoactive polypeptides.
    • Photoactive Polypeptides


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.