메뉴 건너뛰기




Volumn 85, Issue 3, 2003, Pages 1903-1913

Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; DICHLOROACETIC ACID; GLOBULAR PROTEIN; LYSOZYME; PEPSIN A; PEPTIDE;

EID: 0041320758     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74618-9     Document Type: Article
Times cited : (126)

References (50)
  • 2
    • 0030853055 scopus 로고    scopus 로고
    • The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
    • Barron, L. D., L. Hecht, and G. Wilson. 1997. The lubricant of life: a proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure. Biochemistry. 36: 13143-13147.
    • (1997) Biochemistry , vol.36 , pp. 13143-13147
    • Barron, L.D.1    Hecht, L.2    Wilson, G.3
  • 5
    • 0036708465 scopus 로고    scopus 로고
    • A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study
    • Bon, C., A. J. Dianoux, M. Ferrand, and M. S. Lehmann. 2002. A model for water motion in crystals of lysozyme based on an incoherent quasielastic neutron-scattering study. Biophys. J. 83:1578-1588.
    • (2002) Biophys. J. , vol.83 , pp. 1578-1588
    • Bon, C.1    Dianoux, A.J.2    Ferrand, M.3    Lehmann, M.S.4
  • 9
    • 0030862281 scopus 로고    scopus 로고
    • Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering
    • Diehl, M., W. Doster, W. Petry, and H. Schober. 1997. Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering. Biophys. J. 73:2726-2732.
    • (1997) Biophys. J. , vol.73 , pp. 2726-2732
    • Diehl, M.1    Doster, W.2    Petry, W.3    Schober, H.4
  • 10
    • 0037765220 scopus 로고    scopus 로고
    • Polarization-selective femtosecond raman spectrocopy of low-frequency motions in hydrated protein films
    • Eaves, J. D., C. J. Fecko, A. L. Stevens, P. Peng, and A. Tokmakoff. 2003. Polarization-selective femtosecond raman spectrocopy of low-frequency motions in hydrated protein films. Chem. Phys. Lett. 376:20-25
    • (2003) Chem. Phys. Lett. , vol.376 , pp. 20-25
    • Eaves, J.D.1    Fecko, C.J.2    Stevens, A.L.3    Peng, P.4    Tokmakoff, A.5
  • 11
    • 0014449314 scopus 로고
    • Nuclear magnetic resonance investigation of the helix to random coil transformation in poly-alpha-amino acids
    • Ferretti, J. A., and L. Paolillo. 1969. Nuclear magnetic resonance investigation of the helix to random coil transformation in poly-alpha-amino acids. Biopolymers. 7:155-171.
    • (1969) Biopolymers , vol.7 , pp. 155-171
    • Ferretti, J.A.1    Paolillo, L.2
  • 12
    • 0035940247 scopus 로고    scopus 로고
    • Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor
    • Fischer, S., J. C. Smith, and C. S. Verma. 2001. Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water molecule in bovine pancreatic trypsin inhibitor. J. Phys. Chem. B. 105:8050-8055.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 8050-8055
    • Fischer, S.1    Smith, J.C.2    Verma, C.S.3
  • 14
    • 0043094287 scopus 로고    scopus 로고
    • The effect of anion and cation substitution on the ultrafast solvent dynamics of ionic liquids: A time-resolved optical Kerr-effect spectroscopic study
    • Giraud, G., C. M. Gordon, I. R. Dunkin, and K. Wynne. 2003. The effect of anion and cation substitution on the ultrafast solvent dynamics of ionic liquids: a time-resolved optical Kerr-effect spectroscopic study. J. Chem. Phys. 119:464-477.
    • (2003) J. Chem. Phys. , vol.119 , pp. 464-477
    • Giraud, G.1    Gordon, C.M.2    Dunkin, I.R.3    Wynne, K.4
  • 15
    • 0037120827 scopus 로고    scopus 로고
    • Time-resolved optical Kerr-effect spectroscopy of low-frequency dynamics in Di-L-alanine, poly-L-alanine, and lysozyme in solution
    • Giraud, G., and K. Wynne. 2002. Time-resolved optical Kerr-effect spectroscopy of low-frequency dynamics in Di-L-alanine, poly-L-alanine, and lysozyme in solution. J. Am. Chem. Soc. 124:12110-12111.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12110-12111
    • Giraud, G.1    Wynne, K.2
  • 18
    • 0037069410 scopus 로고    scopus 로고
    • Impact of enzyme motion on activity
    • Hammes-Schiffer, S. 2002. Impact of enzyme motion on activity. Biochemistry. 41:13335-13343.
    • (2002) Biochemistry , vol.41 , pp. 13335-13343
    • Hammes-Schiffer, S.1
  • 19
    • 0017881332 scopus 로고
    • The alpha-helix dipole and the properties of proteins
    • Hol, W. G. J., P. T. van Duijnen, and H. J. C. Berendsen. 1978. The alpha-helix dipole and the properties of proteins. Nature. 273:443-446,
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 20
    • 0037034419 scopus 로고    scopus 로고
    • Flexibility of an antibody binding site measured with photon echo spectroscopy
    • Jimenez, R., D. A. Case, and F. E. Romesberg. 2002. Flexibility of an antibody binding site measured with photon echo spectroscopy. J. Phys. Chem. B. 106:1090-1103.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1090-1103
    • Jimenez, R.1    Case, D.A.2    Romesberg, F.E.3
  • 21
    • 20644453308 scopus 로고    scopus 로고
    • Two-dimensional infrared, two-dimensional Raman, and two-dimensional infrared and Raman heterospectral correlation studies of secondary structure of beta-lactoglobulin in buffer solutions
    • Jung, Y. M., B. Czamik-Matusewicz, and Y. Ozaki. 2000. Two-dimensional infrared, two-dimensional Raman, and two-dimensional infrared and Raman heterospectral correlation studies of secondary structure of beta-lactoglobulin in buffer solutions. J. Phys. Chem. B. 104:7812-7817.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7812-7817
    • Jung, Y.M.1    Czamik-Matusewicz, B.2    Ozaki, Y.3
  • 22
    • 84949218859 scopus 로고
    • A stochastic theory of lineshape
    • Kubo, R. 1969. A stochastic theory of lineshape. Adv. Chem. Phys. 15:101-127.
    • (1969) Adv. Chem. Phys. , vol.15 , pp. 101-127
    • Kubo, R.1
  • 23
    • 0032741871 scopus 로고    scopus 로고
    • Solution structure and dynamics of bovine beta-lactoglobulin A
    • Kuwata, K., M. Hoshino, V. Forge, S. Era, C. A. Batt, and Y. Goto. 1999. Solution structure and dynamics of bovine beta-lactoglobulin A. Protein Sci. 8:2541-2545.
    • (1999) Protein Sci. , vol.8 , pp. 2541-2545
    • Kuwata, K.1    Hoshino, M.2    Forge, V.3    Era, S.4    Batt, C.A.5    Goto, Y.6
  • 24
    • 0002233264 scopus 로고    scopus 로고
    • Polarized Raman spectra of oriented films of alpha-helical poly(L-alanine) and its N-deuterated analogue
    • Lee, S. H., and S. Krimm. 1998a. Polarized Raman spectra of oriented films of alpha-helical poly(L-alanine) and its N-deuterated analogue. J. Raman Spectrosc. 29:73-80.
    • (1998) J. Raman Spectrosc. , vol.29 , pp. 73-80
    • Lee, S.H.1    Krimm, S.2
  • 25
    • 0032189518 scopus 로고    scopus 로고
    • Ab initio-based vibrational analysis of alpha-poly(L-alanine)
    • Lee, S.-H., and S. Krimm. 1998b. Ab initio-based vibrational analysis of alpha-poly(L-alanine). Biopolymers. 46:283-317.
    • (1998) Biopolymers , vol.46 , pp. 283-317
    • Lee, S.-H.1    Krimm, S.2
  • 26
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics-trypsin-inhibitor, crambin, ribonuclease and lysozyme
    • Levitt, M., C. Sander, and P. S. Stern. 1985. Protein normal-mode dynamics-trypsin-inhibitor, crambin, ribonuclease and lysozyme. J. Mol. Biol. 181:423-447.
    • (1985) J. Mol. Biol. , vol.181 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 27
    • 0025811817 scopus 로고
    • Lysozyme and alpha-lactalbumin-structure, function, and interrelationships
    • McKenzie, H. A., and F. H. White. 1991. Lysozyme and alpha-lactalbumin-structure, function, and interrelationships. Adv. Protein Chem. 41:173-315.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White, F.H.2
  • 28
    • 0026260096 scopus 로고
    • Separation of nuclear and electronic contributions to femtosecond four-wave-mixing data
    • McMorrow, D. 1991. Separation of nuclear and electronic contributions to femtosecond four-wave-mixing data. Opt. Commun. 86:236-244.
    • (1991) Opt. Commun. , vol.86 , pp. 236-244
    • McMorrow, D.1
  • 29
    • 0002996041 scopus 로고
    • The frequency-response of condensed-phase media to femtosecond optical pulses - Spectral-filter effects
    • McMorrow, D., and W. T. Lotshaw. 1990. The frequency-response of condensed-phase media to femtosecond optical pulses - spectral-filter effects. Chem. Phys. Lett. 174:85-94.
    • (1990) Chem. Phys. Lett. , vol.174 , pp. 85-94
    • McMorrow, D.1    Lotshaw, W.T.2
  • 30
    • 0023966087 scopus 로고
    • Femtosecond optical Kerr studies on the origin of the nonlinear responses in simple liquids
    • McMorrow, D., W. T. Lotshaw, and G. A. Kenney-Wallace. 1988. Femtosecond optical Kerr studies on the origin of the nonlinear responses in simple liquids. IEEE J. Quantum Electron. 24:443-454.
    • (1988) IEEE J. Quantum Electron. , vol.24 , pp. 443-454
    • McMorrow, D.1    Lotshaw, W.T.2    Kenney-Wallace, G.A.3
  • 31
    • 0021192461 scopus 로고
    • Biophysical applications of quasi-elastic and inelastic neutron-scattering
    • Middendorf, H. D. 1984. Biophysical applications of quasi-elastic and inelastic neutron-scattering. Annu. Rev. Biophys. Bioeng. 13:425-451.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 425-451
    • Middendorf, H.D.1
  • 32
    • 0000163027 scopus 로고    scopus 로고
    • Liquid structure of acetic acid studied by Raman spectroscopy and ab initio molecular orbital calculations
    • Nakabayashi, T., K. Kosugi, and N. Nishi. 1999. Liquid structure of acetic acid studied by Raman spectroscopy and ab initio molecular orbital calculations. J. Phys. Chem. A. 103:8595-8603.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 8595-8603
    • Nakabayashi, T.1    Kosugi, K.2    Nishi, N.3
  • 33
    • 0035819192 scopus 로고    scopus 로고
    • Low-frequency vibrational anomalies in beta-lactoglobulin: Contribution of different hydrogen classes revealed by inelastic neutron scattering
    • Orecchini, A., A. Paciaroni. A. R. Bizzarri, and S. Cannistraro. 2001. Low-frequency vibrational anomalies in beta-lactoglobulin: contribution of different hydrogen classes revealed by inelastic neutron scattering. J. Phys. Chem. B. 105:12150-12156,
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12150-12156
    • Orecchini, A.1    Paciaroni, A.2    Bizzarri, A.R.3    Cannistraro, S.4
  • 34
    • 0001182665 scopus 로고    scopus 로고
    • Neutron scattering evidence of a boson peak in protein hydration water
    • Paciaroni, A., A. R. Bizzarri, and S. Cannistraro. 1999. Neutron scattering evidence of a boson peak in protein hydration water. Phys. Rev. E. 60:R2476-R2479.
    • (1999) Phys. Rev. E , vol.60
    • Paciaroni, A.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 35
    • 0027016652 scopus 로고
    • Protein-water interactions determined by dielectric methods
    • Pethig, R. 1992. Protein-water interactions determined by dielectric methods. Annu. Rev. Phys. Chem. 43:177-205.
    • (1992) Annu. Rev. Phys. Chem. , vol.43 , pp. 177-205
    • Pethig, R.1
  • 39
    • 0025354599 scopus 로고
    • Molecular and crystal-structures of monoclinic porcine pepsin refined at 1.8-Å resolution
    • Sielecki, A. R., A. A. Fedorov, A. Boodhoo, N. S. Andreeva, and M. N. G. James. 1990. Molecular and crystal-structures of monoclinic porcine pepsin refined at 1.8-Å resolution. J. Mol. Biol. 214:143-170.
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, M.N.G.5
  • 40
    • 0030325168 scopus 로고    scopus 로고
    • Polar fluctuations in proteins: Molecular-dynamic studies of cytochrome c in aqueous solution
    • Simonson, T., and D. Perahia. 1996. Polar fluctuations in proteins: molecular-dynamic studies of cytochrome c in aqueous solution. Faraday Discuss. 103:71-90.
    • (1996) Faraday Discuss. , vol.103 , pp. 71-90
    • Simonson, T.1    Perahia, D.2
  • 41
    • 0036192659 scopus 로고    scopus 로고
    • Optically-heterodyne-detected optical Kerr effect (OHD-OKE): Applications in condensed phase dynamics
    • Smith, N. A., and S. R. Meech. 2002. Optically-heterodyne-detected optical Kerr effect (OHD-OKE): applications in condensed phase dynamics. Int. Rev. Phys. Chem. 21:75-100.
    • (2002) Int. Rev. Phys. Chem. , vol.21 , pp. 75-100
    • Smith, N.A.1    Meech, S.R.2
  • 42
    • 0000695363 scopus 로고    scopus 로고
    • High-resolution structure (1.33 angstrom) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission
    • Vaney, M. C., S. Maignan, M. Rieskautt, and A. Ducruix. 1996. High-resolution structure (1.33 angstrom) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Crystallogr. D-Biol. Crystallogr. 52:505-517.
    • (1996) Acta Crystallogr. D-Biol. Crystallogr. , vol.52 , pp. 505-517
    • Vaney, M.C.1    Maignan, S.2    Rieskautt, M.3    Ducruix, A.4
  • 43
    • 0000670840 scopus 로고
    • Broadening a nd shifts of vibrational bands due to the effect of thermal chemical-reactions
    • Wood, K. A., and H. L. Strauss. 1990. Broadening a nd shifts of vibrational bands due to the effect of thermal chemical-reactions. J. Phys. Chem. 94:5677-5684.
    • (1990) J. Phys. Chem. , vol.94 , pp. 5677-5684
    • Wood, K.A.1    Strauss, H.L.2
  • 44
    • 0035935379 scopus 로고    scopus 로고
    • Time-resolved two-dimensional vibrational spectroscopy of a short alpha-helix in water
    • Woutersen, S., and P. Hamm. 2001. Time-resolved two-dimensional vibrational spectroscopy of a short alpha-helix in water. J. Chem. Phys. 115:7737-7743.
    • (2001) J. Chem. Phys. , vol.115 , pp. 7737-7743
    • Woutersen, S.1    Hamm, P.2
  • 45
    • 0033898627 scopus 로고    scopus 로고
    • Tunneling of single-cycle terahertz pulses through waveguides
    • Wynne, K., J. J. Carey, J. Zawadzka, and D. A. Jaroszynski. 2000. Tunneling of single-cycle terahertz pulses through waveguides. Opt. Commun. 176:429-435.
    • (2000) Opt. Commun. , vol.176 , pp. 429-435
    • Wynne, K.1    Carey, J.J.2    Zawadzka, J.3    Jaroszynski, D.A.4
  • 46
    • 0036041539 scopus 로고    scopus 로고
    • Excited-state lifetimes of far-infrared collective modes in proteins
    • Xie, A., L. van der Meer, and R. H. Austin. 2002. Excited-state lifetimes of far-infrared collective modes in proteins. J. Biol. Phys. 28:147-154.
    • (2002) J. Biol. Phys. , vol.28 , pp. 147-154
    • Xie, A.1    Van der Meer, L.2    Austin, R.H.3
  • 47
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • Xie, A. H., L. Kelemen, J. Hendriks, B. J. White, K. J. Hellingwerf, and W. D. Hoff. 2001. Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation. Biochemistry. 40:1510-1517.
    • (2001) Biochemistry , vol.40 , pp. 1510-1517
    • Xie, A.H.1    Kelemen, L.2    Hendriks, J.3    White, B.J.4    Hellingwerf, K.J.5    Hoff, W.D.6
  • 48
    • 0035443168 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy: A promising new method for the time resolution of structures
    • Zanni, M. T., and R. M. Hochstrasser. 2001. Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures. Curr. Opin. Struct, Biol. 11:516-522.
    • (2001) Curr. Opin. Struct, Biol. , vol.11 , pp. 516-522
    • Zanni, M.T.1    Hochstrasser, R.M.2
  • 49
    • 0041631877 scopus 로고    scopus 로고
    • Solvent dependent conformational dynamics of dipeptides studied with two-dimensional infrared spectroscopy
    • Zanni, M. T., J. Stenger, M. C. Asplund, and R. M. Hochstrasser. 2001. Solvent dependent conformational dynamics of dipeptides studied with two-dimensional infrared spectroscopy. Biophys. J. 80:38.
    • (2001) Biophys. J. , vol.80 , pp. 38
    • Zanni, M.T.1    Stenger, J.2    Asplund, M.C.3    Hochstrasser, R.M.4
  • 50
    • 0032482925 scopus 로고    scopus 로고
    • Conformation gating as a mechanism for enzyme specificity
    • Zhou, H. X., S. T. Wlodek, and J. A. McCammon. 1998. Conformation gating as a mechanism for enzyme specificity. Proc. Natl. Acad. Sci. USA. 95:9280-9283.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9280-9283
    • Zhou, H.X.1    Wlodek, S.T.2    McCammon, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.