메뉴 건너뛰기




Volumn 86, Issue 4, 2004, Pages 2350-2362

Ultrafast Conformational Dynamics in Cyclic Azobenzene Peptides of Increased Flexibility

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOMETHYLBENZOIC ACID; 4 AMINOMETHYLPHENYLAZOBENZOIC ACID; AZOBENZENE DERIVATIVE; CARBENE; DISULFIDE; UNCLASSIFIED DRUG;

EID: 1942487384     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74292-7     Document Type: Article
Times cited : (75)

References (45)
  • 1
    • 0029858841 scopus 로고    scopus 로고
    • Observation of distinct nanosecond and microsecond protein folding events
    • Ballew, R. M., J. Sabelko, and M. Gruebele. 1996. Observation of distinct nanosecond and microsecond protein folding events. Nat. Struct. Biol. 3:923-926.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 923-926
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 3
    • 0032730716 scopus 로고    scopus 로고
    • Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties
    • Behrendt, R., M. Schenk, H.-J. Musiol, and L. Moroder. 1999b. Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties. J. Pept. Sci. 5:519-529.
    • (1999) J. Pept. Sci. , vol.5 , pp. 519-529
    • Behrendt, R.1    Schenk, M.2    Musiol, H.-J.3    Moroder, L.4
  • 4
    • 0032847748 scopus 로고    scopus 로고
    • Elementary steps in protein folding
    • Bieri, O., and T. Kiefhaber. 1999. Elementary steps in protein folding. Biol. Chem. 380:923-929.
    • (1999) Biol. Chem. , vol.380 , pp. 923-929
    • Bieri, O.1    Kiefhaber, T.2
  • 8
    • 0033557181 scopus 로고    scopus 로고
    • Folding-unfolding thermodynamics of a beta-heptapeptide from equilibrium simulations
    • Daura, X., W. F. van Gunsteren, and A. E. Mark. 1999. Folding-unfolding thermodynamics of a beta-heptapeptide from equilibrium simulations. Proteins. 34:269-280.
    • (1999) Proteins , vol.34 , pp. 269-280
    • Daura, X.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 9
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • Dill, K. A., and H. S. Chan. 1997. From levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 10
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan, Y., and P. A. Kollman. 1998. Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science. 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 11
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 13
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin, R., S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer. 1997. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:3709-3713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 14
    • 0000171168 scopus 로고    scopus 로고
    • Vibrational cooling after ultrafast photoisomerization of azobenzene measured by femtosecond infrared spectroscopy
    • Hamm, P., S. M. Ohline, and W. Zinth. 1997. Vibrational cooling after ultrafast photoisomerization of azobenzene measured by femtosecond infrared spectroscopy. J. Chem. Phys. 106:519-529.
    • (1997) J. Chem. Phys. , vol.106 , pp. 519-529
    • Hamm, P.1    Ohline, S.M.2    Zinth, W.3
  • 17
    • 0037183070 scopus 로고    scopus 로고
    • Real-time observation of photoinduced adiabatic electron transfer in strongly coupled dye/semiconductor colloidal systems with a 6 fs time constant
    • Huber, R., J. E. Moser, M. Grätzel, and J. Wachtveitl. 2002. Real-time observation of photoinduced adiabatic electron transfer in strongly coupled dye/semiconductor colloidal systems with a 6 fs time constant. J. Phys. Chem. B. 106:6494-6499.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6494-6499
    • Huber, R.1    Moser, J.E.2    Grätzel, M.3    Wachtveitl, J.4
  • 19
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., and J. Bandekar. 1986. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38:181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 20
    • 33751154443 scopus 로고    scopus 로고
    • Femtosecond time-resolved uv-visible absorption spectroscopy of trans-azobenzene in solution
    • Lednev, I. K., T. Ye, R. E. Hester, and J. N. Moore. 1996. Femtosecond time-resolved uv-visible absorption spectroscopy of trans-azobenzene in solution. J. Phys. Chem. 100:13338-13341.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13338-13341
    • Lednev, I.K.1    Ye, T.2    Hester, R.E.3    Moore, J.N.4
  • 22
    • 0012973572 scopus 로고    scopus 로고
    • Femtosecond fluorescence dynamics of trans-azobenzene in hexane on excitation to the s1(n,π*) state
    • Lu, Y. C., C. W. Chang, and E. W. G. Diau. 2002. Femtosecond fluorescence dynamics of trans-azobenzene in hexane on excitation to the s1(n,π*) state. J. Chin. Chem. Soc.-TAIP. 49:693-701.
    • (2002) J. Chin. Chem. Soc.-TAIP , vol.49 , pp. 693-701
    • Lu, Y.C.1    Chang, C.W.2    Diau, E.W.G.3
  • 23
    • 0001776024 scopus 로고
    • Features of the photochemically active state surfaces of azobenzene
    • Monti, S., G. Orlandi, and P. Palmieri. 1982. Features of the photochemically active state surfaces of azobenzene. Chem. Phys. 71:87-99.
    • (1982) Chem. Phys. , vol.71 , pp. 87-99
    • Monti, S.1    Orlandi, G.2    Palmieri, P.3
  • 24
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Munoz, V., P. A. Thompson, J. Hofrichter, and W. A. Eaton. 1997. Folding dynamics and mechanism of beta-hairpin formation. Nature. 390: 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 27
    • 84942322948 scopus 로고
    • Azo compounds
    • H. Dürr and H. Bouas-Laurent, editors. Elsevier, Amsterdam, The Netherlands
    • Rau, H. 1990. Azo compounds. In Studies in Organic Chemistry, Photochroism, Molecules and Systems. H. Dürr and H. Bouas-Laurent, editors. Elsevier, Amsterdam, The Netherlands. 165-192.
    • (1990) Studies in Organic Chemistry, Photochroism, Molecules and Systems , pp. 165-192
    • Rau, H.1
  • 28
    • 0036290843 scopus 로고    scopus 로고
    • Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent
    • Renner, C., R. Behrendt, N. Heim, and L. Moroder. 2002. Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent. Biopolymers. 63:382-393.
    • (2002) Biopolymers , vol.63 , pp. 382-393
    • Renner, C.1    Behrendt, R.2    Heim, N.3    Moroder, L.4
  • 29
    • 0034578592 scopus 로고    scopus 로고
    • Photomodulation of conformational states. I. Mono- and bicyclic peptides with (4-amino)phenylazobenzoic acid as backbone constituent
    • Renner, C., R. Behrendt, S. Spörlein, J. Wachtveitl, and L. Moroder. 2000a. Photomodulation of conformational states. I. Mono- and bicyclic peptides with (4-amino)phenylazobenzoic acid as backbone constituent. Biopolymers. 54:489-500.
    • (2000) Biopolymers , vol.54 , pp. 489-500
    • Renner, C.1    Behrendt, R.2    Spörlein, S.3    Wachtveitl, J.4    Moroder, L.5
  • 30
    • 0034578637 scopus 로고    scopus 로고
    • Photomodulation of conformational states. II. Mono- and bicyclic peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent
    • Renner, C., J. Cramer, R. Behrendt, and L. Moroder. 2000b. Photomodulation of conformational states. II. Mono- and bicyclic peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent. Biopolymers. 54:501-514.
    • (2000) Biopolymers , vol.54 , pp. 501-514
    • Renner, C.1    Cramer, J.2    Behrendt, R.3    Moroder, L.4
  • 32
    • 0037461222 scopus 로고    scopus 로고
    • Fluorescence spectra of trans- and cis-azobenzene - Emission from the Franck-Condon state
    • Satzger, H., S. Spörlein, C. Root, J. Wachtveitl, W. Zinth, and P. Gilch. 2003. Fluorescence spectra of trans- and cis-azobenzene - emission from the Franck-Condon state. Chem. Phys. Lett. 372:216-223.
    • (2003) Chem. Phys. Lett. , vol.372 , pp. 216-223
    • Satzger, H.1    Spörlein, S.2    Root, C.3    Wachtveitl, J.4    Zinth, W.5    Gilch, P.6
  • 33
    • 0031124054 scopus 로고    scopus 로고
    • A multichannel detection system for application in ultrafast spectroscopy
    • Seel, M., E. Wildermuth, and W. Zinth. 1997. A multichannel detection system for application in ultrafast spectroscopy. Meas. Sci. Technol. 1997:449-452.
    • (1997) Meas. Sci. Technol. , vol.1997 , pp. 449-452
    • Seel, M.1    Wildermuth, E.2    Zinth, W.3
  • 36
    • 36449001245 scopus 로고
    • Model-calculations on the amide-i infrared bands of globular-proteins
    • Torii, H., and M. Tasumi. 1992. Model-calculations on the amide-i infrared bands of globular-proteins. J. Chem. Phys. 96:3379-3387.
    • (1992) J. Chem. Phys. , vol.96 , pp. 3379-3387
    • Torii, H.1    Tasumi, M.2
  • 37
    • 0001934802 scopus 로고    scopus 로고
    • Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix
    • Torii, H., and M. Tasumi. 1998. Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix. J. Raman Spectrosc. 29:81-86.
    • (1998) J. Raman Spectrosc. , vol.29 , pp. 81-86
    • Torii, H.1    Tasumi, M.2
  • 38
    • 0027963642 scopus 로고
    • The synthesis of a light-switchable amino-acid for inclusion into conformationally mobile peptides
    • Ulysse, L., and J. Chmielewski. 1994. The synthesis of a light-switchable amino-acid for inclusion into conformationally mobile peptides. Bioorg. Med. Chem. Lett. 4:2145-2146.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 2145-2146
    • Ulysse, L.1    Chmielewski, J.2
  • 39
    • 0029122069 scopus 로고
    • Photoregulation of cyclic peptide conformation
    • Ulysse, L., J. Cubillos, and J. Chmielewski. 1995. Photoregulation of cyclic peptide conformation. J. Am. Chem. Soc. 117:8466-8467.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8466-8467
    • Ulysse, L.1    Cubillos, J.2    Chmielewski, J.3
  • 40
    • 0031251663 scopus 로고    scopus 로고
    • Peptide conformational dynamics and vibrational stark effects following photoinitiated disulfide cleavage
    • Volk, M., Y. Kholodenko, H. S. M. Lu, E. A. Gooding, W. F. DeGrado, and R. M. Hochstrasser. 1997. Peptide conformational dynamics and vibrational stark effects following photoinitiated disulfide cleavage. J. Phys. Chem. B. 101:8607-8616.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8607-8616
    • Volk, M.1    Kholodenko, Y.2    Lu, H.S.M.3    Gooding, E.A.4    DeGrado, W.F.5    Hochstrasser, R.M.6
  • 42
    • 0037123067 scopus 로고    scopus 로고
    • Dynamics of the primary processes of protein folding: Helix nucleation
    • Werner, J. H., R. B. Dyer, R. M. Fesinmeyer, and N. H. Andersen. 2002. Dynamics of the primary processes of protein folding: helix nucleation. J. Phys. Chem. B. 106:487-494.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 487-494
    • Werner, J.H.1    Dyer, R.B.2    Fesinmeyer, R.M.3    Andersen, N.H.4
  • 43
    • 5344280469 scopus 로고    scopus 로고
    • Sub-20-fs pulses tunable across the visible from a blue-pumped single-pass noncollinear parametric converter
    • Wilhelm, T., J. Piel, and E. Riedle. 1997. Sub-20-fs pulses tunable across the visible from a blue-pumped single-pass noncollinear parametric converter. Opt. Lett. 22:1494-1496.
    • (1997) Opt. Lett. , vol.22 , pp. 1494-1496
    • Wilhelm, T.1    Piel, J.2    Riedle, E.3
  • 45
    • 0033598375 scopus 로고    scopus 로고
    • Interpreting the folding kinetics of helical proteins
    • Zhou, Y. Q., and M. Karplus. 1999. Interpreting the folding kinetics of helical proteins. Nature. 401:400-403.
    • (1999) Nature , vol.401 , pp. 400-403
    • Zhou, Y.Q.1    Karplus, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.