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Volumn 444, Issue 7118, 2006, Pages 469-472

Watching hydrogen-bond dynamics in a β-turn by transient two-dimensional infrared spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BIOMATERIALS; INFRARED SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE; TRANSIENTS; X RAY CRYSTALLOGRAPHY;

EID: 33751313515     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05352     Document Type: Article
Times cited : (306)

References (28)
  • 1
    • 0038047431 scopus 로고    scopus 로고
    • Watching a protein as it functions with 150-ps time-resolved X-ray crystallography
    • Schotte, F. et al. Watching a protein as it functions with 150-ps time-resolved X-ray crystallography. Science 300, 1944-1947 (2003).
    • (2003) Science , vol.300 , pp. 1944-1947
    • Schotte, F.1
  • 2
    • 26844469318 scopus 로고    scopus 로고
    • 18O isotopomers of alanine residues in an α-helix
    • 18O isotopomers of alanine residues in an α-helix. J. Phys. Chem. B 109, 18652-18663 (2005).
    • (2005) J. Phys. Chem. B , vol.109 , pp. 18652-18663
    • Fang, C.1    Hochstrasser, R.M.2
  • 3
    • 33646238700 scopus 로고    scopus 로고
    • Local structure of β-hairpin isotopomers by FTIR, 2D IR, and ab initio theory
    • Wang, J., Chen, J. & Hochstrasser, R. M. Local structure of β-hairpin isotopomers by FTIR, 2D IR, and ab initio theory. J. Phys. Chem. B 110, 7545-7555 (2006).
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7545-7555
    • Wang, J.1    Chen, J.2    Hochstrasser, R.M.3
  • 4
    • 0347316753 scopus 로고    scopus 로고
    • Hydrogen bond dynamics probed with ultrafast infrared heterodyne-detected multidimensional vibrational stimulated echoes
    • Asbury, J. B. et al. Hydrogen bond dynamics probed with ultrafast infrared heterodyne-detected multidimensional vibrational stimulated echoes. Phys. Rev. Lett. 91, 237402 (2003).
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 237402
    • Asbury, J.B.1
  • 5
    • 0000873587 scopus 로고    scopus 로고
    • Multidimensional femtosecond correlation spectroscopies of electronic and vibrational excitations
    • Mukamel, S. Multidimensional femtosecond correlation spectroscopies of electronic and vibrational excitations. Annu. Rev. Phys. Chem. 51, 691-729 (2000).
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 691-729
    • Mukamel, S.1
  • 6
  • 7
    • 4243879778 scopus 로고    scopus 로고
    • Vibrational anharmonicities revealed by coherent two-dimensional infrared spectroscopy
    • Golonzka, O., Khalil, M., Demirdoven, N. & Tokmakoff, A. Vibrational anharmonicities revealed by coherent two-dimensional infrared spectroscopy. Phys. Rev. Lett. 86, 2154-2157 (2001).
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 2154-2157
    • Golonzka, O.1    Khalil, M.2    Demirdoven, N.3    Tokmakoff, A.4
  • 8
    • 15044356423 scopus 로고    scopus 로고
    • 2O
    • 2O. Nature 434, 199-202 (2005).
    • (2005) Nature , vol.434 , pp. 199-202
    • Cowan, M.L.1
  • 9
    • 0001326710 scopus 로고    scopus 로고
    • Structure of the amide I band of peptides measured by femtosecond nonlinear-infrared spectroscopy
    • Hamm, P., Lim, M. & Hochstrasser, R. M. Structure of the amide I band of peptides measured by femtosecond nonlinear-infrared spectroscopy. J. Phys. Chem. B 102, 6123-6138 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6123-6138
    • Hamm, P.1    Lim, M.2    Hochstrasser, R.M.3
  • 10
    • 0034315712 scopus 로고    scopus 로고
    • Structure determination of trialanine in water using polarization sensitive two-dimensional vibrational spectroscopy
    • Woutersen, S. & Hamm, P. Structure determination of trialanine in water using polarization sensitive two-dimensional vibrational spectroscopy. J. Phys. Chem. B 104, 11316-11320 (2000).
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11316-11320
    • Woutersen, S.1    Hamm, P.2
  • 11
    • 0037037802 scopus 로고    scopus 로고
    • Nonlinear two-dimensional vibrational spectroscopy of peptides
    • Woutersen, S. & Hamm, P. Nonlinear two-dimensional vibrational spectroscopy of peptides. J. Phys. Condens. Matter 14, R1035-R1062 (2002).
    • (2002) J. Phys. Condens. Matter , vol.14
    • Woutersen, S.1    Hamm, P.2
  • 12
    • 0041786766 scopus 로고    scopus 로고
    • Transient 2D-IR spectroscopy: Snapshots of the nonequilibrium ensemble during the picosecond conformational transition of a small peptide
    • Bredenbeck, J. et al. Transient 2D-IR spectroscopy: snapshots of the nonequilibrium ensemble during the picosecond conformational transition of a small peptide. J. Phys. Chem. B 107, 8654-8660 (2003).
    • (2003) J. Phys. Chem. B , vol.107 , pp. 8654-8660
    • Bredenbeck, J.1
  • 13
    • 5444250347 scopus 로고    scopus 로고
    • Transient two-dimensional infrared spectroscopy: Exploring the polarization dependence
    • Bredenbeck, J., Helbing, J. & Hamm, P. Transient two-dimensional infrared spectroscopy: exploring the polarization dependence. J. Chem. Phys. 121, 5943-5957 (2004).
    • (2004) J. Chem. Phys. , vol.121 , pp. 5943-5957
    • Bredenbeck, J.1    Helbing, J.2    Hamm, P.3
  • 14
    • 0033578370 scopus 로고    scopus 로고
    • The speed limit for protein folding measured by triplet-triplet energy transfer
    • Bieri, O. et al. The speed limit for protein folding measured by triplet-triplet energy transfer. Proc. Natl Acad. Sci. USA 96, 9597-9601 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9597-9601
    • Bieri, O.1
  • 15
    • 8444230160 scopus 로고    scopus 로고
    • Small cyclic disulfide peptides: Synthesis in preparative amounts and characterization by means of NMR and FT-IR spectroscopy
    • Kolano, C., Gomann, K. & Sander, W. Small cyclic disulfide peptides: Synthesis in preparative amounts and characterization by means of NMR and FT-IR spectroscopy. Eur. J. Org. Chem. 20, 4167-4176 (2004).
    • (2004) Eur. J. Org. Chem. , vol.20 , pp. 4167-4176
    • Kolano, C.1    Gomann, K.2    Sander, W.3
  • 16
    • 0031251663 scopus 로고    scopus 로고
    • Peptide conformational dynamics and vibrational stark effects following photoinitiated disulfide cleavage
    • Volk, M. et al. Peptide conformational dynamics and vibrational stark effects following photoinitiated disulfide cleavage. J. Phys. Chem. B 101, 8607-8616 (1997).
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8607-8616
    • Volk, M.1
  • 17
    • 0030801107 scopus 로고    scopus 로고
    • Aminothiotyrosine disulfide, an optical trigger for initiation of protein folding
    • Lu, H. S. M. et al. Aminothiotyrosine disulfide, an optical trigger for initiation of protein folding. J. Am. Chem. Soc. 119, 7173-7180 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7173-7180
    • Lu, H.S.M.1
  • 18
    • 0038313065 scopus 로고    scopus 로고
    • Picosecond conformational transition and equilibration of a cyclic peptide
    • Bredenbeck, J. et al. Picosecond conformational transition and equilibration of a cyclic peptide. Proc. Natl Acad. Sci. USA 100, 6452-6457 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6452-6457
    • Bredenbeck, J.1
  • 19
    • 14044274349 scopus 로고    scopus 로고
    • α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy
    • Bredenbeck, J., Helbing, J., Kumita, J. R., Woolley, G. A. & Hamm, P. α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy. Proc. Natl Acad. Sci. USA 102, 2379-2384 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2379-2384
    • Bredenbeck, J.1    Helbing, J.2    Kumita, J.R.3    Woolley, G.A.4    Hamm, P.5
  • 20
    • 0000171168 scopus 로고    scopus 로고
    • Vibrational cooling after ultrafast photoisomerization of azobenzene measured by femtosecond infrared spectroscopy
    • Hamm, P., Ohline, S. M. & Zinth, W. Vibrational cooling after ultrafast photoisomerization of azobenzene measured by femtosecond infrared spectroscopy. J. Chem. Phys. 106, 519-529 (1997).
    • (1997) J. Chem. Phys. , vol.106 , pp. 519-529
    • Hamm, P.1    Ohline, S.M.2    Zinth, W.3
  • 22
    • 33746806939 scopus 로고    scopus 로고
    • Photoinduced conformational dynamics of a photoswitchable peptide: A nonequilibrium molecular dynamics simulation study
    • Nguyen, P. H., Gorbunov, R. D. & Stock, G. Photoinduced conformational dynamics of a photoswitchable peptide: a nonequilibrium molecular dynamics simulation study. Biophys. J. 91, 1224-1234 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 1224-1234
    • Nguyen, P.H.1    Gorbunov, R.D.2    Stock, G.3
  • 23
    • 0031587288 scopus 로고    scopus 로고
    • Kinetics of peptide folding: Computer simulations of SYPFDV and peptide variants in water
    • Mohanty, D., Elber, R., Thirumalai, D., Beglov, D. & Roux, B. Kinetics of peptide folding: computer simulations of SYPFDV and peptide variants in water. J. Mol. Biol. 272, 423-442 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 423-442
    • Mohanty, D.1    Elber, R.2    Thirumalai, D.3    Beglov, D.4    Roux, B.5
  • 24
    • 0034324530 scopus 로고    scopus 로고
    • Probing the role of local propensity in peptide turn formation
    • Mohanty, D., Elber, R. & Thirumalai, D. Probing the role of local propensity in peptide turn formation. Int. J. Quantum Chem. 80, 1125-1128 (2000).
    • (2000) Int. J. Quantum Chem. , vol.80 , pp. 1125-1128
    • Mohanty, D.1    Elber, R.2    Thirumalai, D.3
  • 26
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • Sadqi, M., Fushman, D. & Munoz, V. Atom-by-atom analysis of global downhill protein folding. Nature 442, 317-321 (2006).
    • (2006) Nature , vol.442 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Munoz, V.3
  • 27
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. & Gruebele, M. Folding at the speed limit. Nature 423, 193-197 (2003).
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 28
    • 7944223174 scopus 로고    scopus 로고
    • Picosecond dynamics in water-soluble azobenzene-peptides
    • Satzger, H. et al. Picosecond dynamics in water-soluble azobenzene-peptides. Chem. Phys. Lett. 396, 191-197 (2004).
    • (2004) Chem. Phys. Lett. , vol.396 , pp. 191-197
    • Satzger, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.